Yang B

References (101)

Title : Discovery of Enzyme Inhibitors from Mangrove Sediment Derived Fungus Trichoderma harzianum SCSIO 41051 - Huang_2024_Chem.Biodivers__e202400070
Author(s) : Huang L , Chen C , Cai J , Chen Y , Zhu Y , Yang B , Zhou X , Liu Y , Tao H
Ref : Chem Biodivers , :e202400070 , 2024
Abstract : One new fatty acid derivative, (2E,4E)-6,7-dihydroxy-2-methylocta-2,4-dienoic acid (1), and 16 known compounds (2-17) were isolated from the mangrove sediment derived fungus Trichoderma harzianum SCSIO 41051. Their structures were established by spectroscopic methods, computational ECD, and Mo2(OAc)4-induced ECD experiment. All the compounds were evaluated for their acetylcholinesterase (AChE) and pancreatic lipase (PL) inhibition. Compounds 9 and 14 exhibited moderate AChE inhibitory activities with IC50 values of 2.49 and 2.92 microM, respectively, which compounds 8 and 9 displayed moderate inhibition on PL with IC50 value of 2.30 and 2.34 microM, respectively.
ESTHER : Huang_2024_Chem.Biodivers__e202400070
PubMedSearch : Huang_2024_Chem.Biodivers__e202400070
PubMedID: 38356321

Title : The acute neurotoxicity of inorganic mercury in Mactra chinensis philippi - Ma_2024_Aquat.Toxicol_270_106896
Author(s) : Ma B , Zhao X , Zhang X , Yang B , Cai Z , Xing Z , Xu M , Mi L , Zhang J , Wang L , Zhao Y , Liu X
Ref : Aquat Toxicol , 270 :106896 , 2024
Abstract : Inorganic mercury (IHg) is hazardous to marine organisms especially resulting in neurotoxicity, bivalves are sensitive to pollutants as "ocean sentinel", but data on the neurotoxicity of IHg in bivalves are sparse. So we chosed M. chinensis philippi with typical neural structures in bivalves to investigate the neurotoxicity of IHg, which could be helpful to understand the specificity of neural regulation and the response characteristics of bivalves. After acute exposed to IHg (HgCl(2)) for 24 h, the metabolites of ganglion tissues in M. chinensis philippi were evaluated using (1)H-nuclear magnetic resonance based metabolomics; Ca(2+), neurotransmitters (nitric oxide, glutamate, acetylcholine) and related enzymes (calcineurin, nitric oxide synthase and acetylcholinesterase) were measured using biochemical detection. Compared to the control group, the levels of the nitric oxide (81.04 +/- 12.84 micromol/g prot) and acetylcholine (30.93 +/- 12.57 microg/mg prot) in M. chinensis philippi of IHg-treated were decreased, while glutamate (2.11 +/- 0.61 mmol/L) increased significantly; the activity of nitric oxide synthase (679.34 +/- 135.33 U/mg prot) was increased, while acetylcholinesterase (1.39 +/- 0.44 U/mg prot) decreased significantly, and the activity of calcineurin (0.52 +/- 0.02 U/mg prot) had a statistically insignificant increasing tendency. The concentration of Ca(2+) (0.92 +/- 0.46 mmol/g prot) in the IHg-treated group was significantly higher than that in the control group. OPLS-DA was performed to reveal the difference in metabolites between the control and IHg-challenged groups, the metabolites of glucose, glutamine, inosine, succinate, glutamate, homarine, and alanine were sensitive to IHg, subsequently metabolic pathways that were affected including glucose metabolism, glutamine metabolism, nucleotide metabolism, Krebs cycle, amino acid metabolism and osmotic regulation. In our study, IHg interfered with metabolites in M. chinensis philippi, thus the corresponding metabolic pathways were changed, which influenced the neurotransmitters subsequently. Furthermore, Ca(2+)overload affected the synthesis or degradation of the neurotransmitters, and then the altered neurotransmitters involved in changes in metabolic pathways again. Overall, we hypothesized that the neurotoxic effects of IHg on bivalve were in close contact with metabolism, neurotransmitters, related enzymes and Ca(2+), which could be effective neurotoxic biomarkers for marine environmental quality assessment, and also provide effective data for the study of the regulatory mechanism of the nervous system in response to IHg in bivalves.
ESTHER : Ma_2024_Aquat.Toxicol_270_106896
PubMedSearch : Ma_2024_Aquat.Toxicol_270_106896
PubMedID: 38490093

Title : Exploration of the SIRT1-mediated BDNF-TrkB signaling pathway in the mechanism of brain damage and learning and memory effects of fluorosis - Wang_2023_Front.Public.Health_11_1247294
Author(s) : Wang F , Li Y , Tang D , Yang B , Tian T , Tian M , Meng N , Xie W , Zhang C , He Z , Zhu X , Ming D , Liu Y
Ref : Front Public Health , 11 :1247294 , 2023
Abstract : INTRODUCTION: Fluoride is considered an environmental pollutant that seriously affects organisms and ecosystems, and its harmfulness is a perpetual public health concern. The toxic effects of fluoride include organelle damage, oxidative stress, cell cycle destruction, inflammatory factor secretion, apoptosis induction, and synaptic nerve transmission destruction. To reveal the mechanism of fluorosis-induced brain damage, we analyzed the molecular mechanism and learning and memory function of the SIRT1-mediated BDNF-TrkB signaling pathway cascade reaction in fluorosis-induced brain damage through in vivo experiments. METHODS: This study constructed rat models of drinking water fluorosis using 50 mg/L, 100 mg/L, and 150 mg/L fluoride, and observed the occurrence of dental fluorosis in the rats. Subsequently, we measured the fluoride content in rat blood, urine, and bones, and measured the rat learning and memory abilities. Furthermore, oxidative stress products, inflammatory factor levels, and acetylcholinesterase (AchE) and choline acetyltransferase (ChAT) activity were detected. The pathological structural changes to the rat bones and brain tissue were observed. The SIRT1, BDNF, TrkB, and apoptotic protein levels were determined using western blotting. RESULTS: All rats in the fluoride exposure groups exhibited dental fluorosis; decreased learning and memory abilities; and higher urinary fluoride, bone fluoride, blood fluoride, oxidative stress product, and inflammatory factor levels compared to the control group. The fluoride-exposed rat brain tissue had abnormal AchE and ChAT activity, sparsely arranged hippocampal neurons, blurred cell boundaries, significantly fewer astrocytes, and swollen cells. Furthermore, the nucleoli were absent from the fluoride-exposed rat brain tissue, which also contained folded neuron membranes, deformed mitochondria, absent cristae, vacuole formation, and pyknotic and hyperchromatic chromatin. The fluoride exposure groups had lower SIRT1, BDNF, and TrkB protein levels and higher apoptotic protein levels than the control group, which were closely related to the fluoride dose. The findings demonstrated that excessive fluoride caused brain damage and affected learning and memory abilities. DISCUSSION: Currently, there is no effective treatment method for the tissue damage caused by fluorosis. Therefore, the effective method for preventing and treating fluorosis damage is to control fluoride intake.
ESTHER : Wang_2023_Front.Public.Health_11_1247294
PubMedSearch : Wang_2023_Front.Public.Health_11_1247294
PubMedID: 37711250

Title : Using a Battery of Bioassays to Assess the Toxicity of Wastewater Treatment Plant Effluents in Industrial Parks - Yang_2023_Toxics_11_702
Author(s) : Yang B , Cui H , Gao J , Cao J , Klobucar G , Li M
Ref : Toxics , 11 :702 , 2023
Abstract : Bioassays, as an addition to physico-chemical water quality evaluation, can provide information on the toxic effects of pollutants present in the water. In this study, a broad evaluation of environmental health risks from industrial wastewater along the Yangtze River, China, was conducted using a battery of bioassays. Toxicity tests showed that the wastewater treatment processes were effective at lowering acetylcholinesterase (AChE) inhibition, HepG2 cells' cytotoxicity, the estrogenic effect in T47D-Kbluc cells, DNA damage of Euglena gracilis and the mutagenicity of Salmonella typhimurium in the analyzed wastewater samples. Polycyclic aromatic hydrocarbons (PAHs) were identified as potential major toxic chemicals of concern in the wastewater samples of W, J and T wastewater treatment plants; thus, the potential harm of PAHs to aquatic organisms has been investigated. Based on the health risk assessment model, the risk index of wastewater from the industrial parks along the Yangtze River was below one, indicating that the PAHs were less harmful to human health through skin contact or respiratory exposure. Overall, the biological toxicity tests used in this study provide a good basis for the health risk assessment of industrial wastewater and a scientific reference for the optimization and operation of the treatment process.
ESTHER : Yang_2023_Toxics_11_702
PubMedSearch : Yang_2023_Toxics_11_702
PubMedID: 37624206

Title : An esterase-responsive ibuprofen nano-micelle pre-modified embryo derived nucleus pulposus progenitor cells promote the regeneration of intervertebral disc degeneration - Xia_2023_Bioact.Mater_21_69
Author(s) : Xia KS , Li DD , Wang CG , Ying LW , Wang JK , Yang B , Shu JW , Huang XP , Zhang YA , Yu C , Zhou XP , Li FC , Slater NKH , Tang JB , Chen QX , Liang CZ
Ref : Bioact Mater , 21 :69 , 2023
Abstract : Stem cell-based transplantation is a promising therapeutic approach for intervertebral disc degeneration (IDD). Current limitations of stem cells include with their insufficient cell source, poor proliferation capacity, low nucleus pulposus (NP)-specific differentiation potential, and inability to avoid pyroptosis caused by the acidic IDD microenvironment after transplantation. To address these challenges, embryo-derived long-term expandable nucleus pulposus progenitor cells (NPPCs) and esterase-responsive ibuprofen nano-micelles (PEG-PIB) were prepared for synergistic transplantation. In this study, we propose a biomaterial pre-modification cell strategy; the PEG-PIB were endocytosed to pre-modify the NPPCs with adaptability in harsh IDD microenvironment through inhibiting pyroptosis. The results indicated that the PEG-PIB pre-modified NPPCs exhibited inhibition of pyroptosis in vitro; their further synergistic transplantation yielded effective functional recovery, histological regeneration, and inhibition of pyroptosis during IDD regeneration. Herein, we offer a novel biomaterial pre-modification cell strategy for synergistic transplantation with promising therapeutic effects in IDD regeneration.
ESTHER : Xia_2023_Bioact.Mater_21_69
PubMedSearch : Xia_2023_Bioact.Mater_21_69
PubMedID: 36017070

Title : Ovalbumin-coated gold nanoparticles with interesting colloidal stability for colorimetric detection of carbaryl in complex media - Hao_2023_Food.Chem_403_134485
Author(s) : Hao H , Zhu J , Yang B , Peng L , Lou S
Ref : Food Chem , 403 :134485 , 2023
Abstract : Pesticide carbaryl can cause serious environmental pollution and its sensitive detection is of increasing interest. Gold nanoparticles (AuNPs) are classically colorimetric probes for detection of many analytes, but the instability in complex media limits their application. Here, Au@Ova NPs have been developed as a stable, effective, sensitive, and selective sensing system for colorimetric detection of carbaryl. Au@Ova NPs present unique and proper colloidal stability in various medias containing salt, small molecules, organic solvent (DMSO), and seawater, which are distinct from previous ones including citrate (or rhodamine B) capped AuNPs. Compared with Au@BSA NPs, Au@Ova NPs showed efficient responses to carbaryl by inhibiting acetylcholinesterase, with a linear concentration range between 0 and 25 g/L and a detection limit of 0.25 g/L. In addition, this nanoprobe also has good selectivity and can be applied in different real samples analysis, including fruit juice (tomato and apple) and real water samples (artificial urine and seawater).
ESTHER : Hao_2023_Food.Chem_403_134485
PubMedSearch : Hao_2023_Food.Chem_403_134485
PubMedID: 36358087

Title : A New Brominated Isocoumarin from the Marine Starfish-Associated Fungus Aspergillus sp. WXF1904 - Li_2023_Chem.Biodivers__e202301706
Author(s) : Li C , Lin X , Wang S , Guan D , Wang X , Yang B , Zhou X , Li J , Xiong B , Liu Y , Sun Y
Ref : Chem Biodivers , :e202301706 , 2023
Abstract : Based on the one strain many compounds strategy, a new brominated isocoumarin, 5-bromo-6,8-dihydroxy-3,7-dimethylisocoumarin (1), along with four new natural products, methyl 3-bromo-2,4-dihydroxy-6-methylbenzoate (2), methyl 2-bromo-4,6-dihydroxybenzoate (3), (E)-3-(3-bromo-4-hydroxyphenyl) acrylic acid (4) and 4-hydroxy-3-methyl-6-phenyl-2H-pyran-2-one (5), and four known compounds, methyl orsellinate (6), 4-hydroxy-3-methyl-6-(1-methyl-1-propenyl)-2H-pyran-2-one (7), pilobolusate (8) and cis-ferulic acid (9), were isolated from the ethyl acetate extract of the fungus Aspergillus sp. WXF1904 under the condition of adding bromine salt to the production medium. The structures of the new compounds were established by analysis of NMR and MS data. Compounds (1-9) were evaluated for inhibitory activity of acetylcholinesterase and pancreatic lipase, the new compound 1, known compounds 6 and 7 displayed weak inhibitory activity against acetylcholinesterase, compounds 257 and 8 showed weak inhibitory activity against pancreatic lipase.
ESTHER : Li_2023_Chem.Biodivers__e202301706
PubMedSearch : Li_2023_Chem.Biodivers__e202301706
PubMedID: 38079052

Title : Bioactive secondary metabolites isolated from the soft coral derived Penicillium sp. SCSIO 41038 - Li_2023_Nat.Prod.Res__1
Author(s) : Li H , Long J , Wang X , She J , Liu Y , Li Y , Yang B
Ref : Nat Prod Res , :1 , 2023
Abstract : Chemical investigation of the Penicillium sp. SCSIO 41038 led to the isolation and characterization of one new cyclopiazonic acid-type alkaloid, speradine I (1), and one new phloroglucinol derivative, speradine J (8), along with 13 known compounds. Their structures were determined on the basis of extensive spectroscopic analysis, and by a comparison with data from the literature. All the compounds were evaluated for their antitumor (22Rv1 and PC-3) and enzyme inhibitory activity against acetylcholinesterase (AChE) in vitro.
ESTHER : Li_2023_Nat.Prod.Res__1
PubMedSearch : Li_2023_Nat.Prod.Res__1
PubMedID: 37129009

Title : Bioactive Polyketides and Benzene Derivatives from Two Mangrove Sediment-Derived Fungi in the Beibu Gulf - Peng_2023_Mar.Drugs_21_
Author(s) : Peng B , Cai J , Xiao Z , Liu M , Li X , Yang B , Fang W , Huang YY , Chen C , Zhou X , Tao H
Ref : Mar Drugs , 21 : , 2023
Abstract : To discover bioactive natural products from mangrove sediment-derived microbes, a chemical investigation of the two Beibu Gulf-derived fungi strains, Talaromyces sp. SCSIO 41050 and Penicillium sp. SCSIO 41411, led to the isolation of 23 natural products. Five of them were identified as new ones, including two polyketide derivatives with unusual acid anhydride moieties named cordyanhydride A ethyl ester (1) and maleicanhydridane (4), and three hydroxyphenylacetic acid derivatives named stachylines H-J (10-12). Their structures were determined by detailed nuclear magnetic resonance (NMR) and mass spectroscopic (MS) analyses, while the absolute configurations were established by theoretical electronic circular dichroism (ECD) calculation. A variety of bioactive screens revealed three polyketide derivatives (1-3) with obvious antifungal activities, and 4 displayed moderate cytotoxicity against cell lines A549 and WPMY-1. Compounds 1 and 6 at 10 microM exhibited obvious inhibition against phosphodiesterase 4 (PDE4) with inhibitory ratios of 49.7% and 39.6%, respectively, while 5, 10, and 11 showed the potential of inhibiting acetylcholinesterase (AChE) by an enzyme activity test, as well as in silico docking analysis.
ESTHER : Peng_2023_Mar.Drugs_21_
PubMedSearch : Peng_2023_Mar.Drugs_21_
PubMedID: 37367652

Title : Visualization of production and remediation of acetaminophen-induced liver injury by a carboxylesterase-2 enzyme-activatable near-infrared fluorescent probe - Yang_2023_Talanta_269_125418
Author(s) : Yang B , Ding X , Zhang Z , Li J , Fan S , Lai J , Su R , Wang X , Wang B
Ref : Talanta , 269 :125418 , 2023
Abstract : Acetaminophen (APAP) overdose, also known as APAP poisoning, may directly result in hepatic injury, acute liver failure and even death. Nowadays, APAP-induced liver injury (AILI) has become an urgent public health issue in the developing world so the early accurate diagnosis and the revelation of underlying molecular mechanism of AILI are of great significance. As a major detoxifying organ, liver is responsible for metabolizing chemical substances, in which human carboxylesterase-2 (CES2) is present. Hence, we chose CES2 as an effective biomarker for evaluating AILI. By developing a CES2-activatable and water-soluble fluorescent probe PFQ-E with superior affinity (K(m) = 5.9 microM), great sensitivity (limit of detection = 1.05 ng/mL), near-infrared emission (655 nm) and large Stokes shift (135 nm), activity and distribution of CES2 in cells were determined or imaged effectively. More importantly, the APAP-induced hepatotoxicity and the underlying molecular mechanism of pathogenesis of AILI were investigated by measuring the "light-up" response of PFQ-E towards endogenous CES2 in vivo for the first time. Based on the superior performance of the probe PFQ-E for sensing CES2, we believe that it has broad potential in clinical diagnosis and therapy response evaluation of AILI.
ESTHER : Yang_2023_Talanta_269_125418
PubMedSearch : Yang_2023_Talanta_269_125418
PubMedID: 37988783

Title : Secondary Metabolites from the Coral-Derived Fungus Aspergillus austwickii SCSIO41227 with Pancreatic Lipase and Neuraminidase Inhibitory Activities - Chen_2023_Mar.Drugs_21_
Author(s) : Chen Y , He Y , Pang X , Zhou X , Liu Y , Yang B
Ref : Mar Drugs , 21 : , 2023
Abstract : The coral-derived fungus Aspergillus austwickii SCSIO41227 from Beibu Gulf yielded four previously uncharacterized compounds, namely asperpentenones B-E (1-4), along with twelve known compounds (5-16). Their structures were elucidated using HRESIMS and NMR ((1)H and (13)C NMR, HSQC, HMBC), among which the stereo-structure of compounds 1-3 was determined by calculated ECD. Furthermore, compounds 1-16 were evaluated in terms of their enzyme (acetylcholinesterase (AChE), pancreatic lipase (PL), and neuraminidase (NA)) inhibitory activities. These bioassay results revealed that compounds 2 and 14 exerted noticeable NA inhibitory effects, with IC(50) values of 31.28 and 73.64 microM, respectively. In addition, compound 3 exhibited a weak inhibitory effect against PL. Furthermore, these compounds showed the potential of inhibiting enzymes in silico docking analysis to demonstrate the interactions between compounds and proteins.
ESTHER : Chen_2023_Mar.Drugs_21_
PubMedSearch : Chen_2023_Mar.Drugs_21_
PubMedID: 37999391

Title : A green photocatalytic-biosensor for colorimetric detection of pesticide (carbaryl) based on inhibition of acetylcholinesterase - Peng_2022_Talanta_246_123525
Author(s) : Peng L , Zhu J , Yang B , Hao H , Lou S
Ref : Talanta , 246 :123525 , 2022
Abstract : Carbaryl is a widely-used carbamate pesticide and the detection of its residues in environmental, food and clinical samples is of great importance. In this sturdy, we developed a green photocatalytic-biosensor based on double strand DNA-SYBR green I complex for sensitively colorimetric detection of carbaryl. This green photocatalytic-biosensor can oxidize 3,3',5,5'-tetramethylbenzidine (TMB) into blue ox-TMB. Meanwhile thiocholine is catalytically produced by acetylcholinesterase (AChE) to directly reduce blue ox-TMB into colorless TMB. But the activity of AChE will be suppressed by carbaryl, thus generating less thiocholine and resulting in more ox-TMB for colorimetric analysis. After the careful optimization of sensing conditions (2 microM for DNA concentration, 50 x concentration for SYBR Green I, 10 min for illumination time), the lowest detectable concentration for carbaryl is 0.008 ng/mL with a linear response in the range of 0.01-0.25 ng/mL. In addition, this photocatalytic-biosensor has good selectivity over non-target chemicals (acetamiprid, atrazine, carbendazim, melamine, bisphenol A, estradiol). It also allows detection of pesticides in real samples verified by a standard HPLC method.
ESTHER : Peng_2022_Talanta_246_123525
PubMedSearch : Peng_2022_Talanta_246_123525
PubMedID: 35533565

Title : Asperbenzophenone A and Versicolamide C, New Fungal Metabolites from the Soft Coral Derived Aspergillus sp. SCSIO 41036 - Long_2022_Chem.Biodivers__e202100925
Author(s) : Long J , Pang X , Lin X , Liao S , Zhou X , Wang J , Yang B , Liu Y
Ref : Chem Biodivers , :e202100925 , 2022
Abstract : Two new compounds, asperbenzophenone A (1) and versicolamide C (5), together with fifteen known compounds were isolated from a soft coral derived fungus Aspergillus sp. SCSIO 41036. Their structures were elucidated by spectroscopic methods, ECD analysis, and by a comparison with data from the literature. In bioassay, compound 8 showed significant inhibitory activity against lipopolysaccharide-inducted nitric oxide (NO) in RAW264.7 cells at the concentration of 10microM. Additionally, the anti-acetylcholinesterase activity assay showed that 14 exhibited weak inhibition with an IC(50) value of 157.8microM.
ESTHER : Long_2022_Chem.Biodivers__e202100925
PubMedSearch : Long_2022_Chem.Biodivers__e202100925
PubMedID: 35194907

Title : Alcohol inhibits the metabolism of dimethyl fumarate to the active metabolite responsible for decreasing relapse frequency in the treatment of multiple sclerosis - Yang_2022_PLoS.One_17_e0278111
Author(s) : Yang B , Parker RB , Meibohm B , Temrikar ZH , Srivastava A , Laizure SC
Ref : PLoS ONE , 17 :e0278111 , 2022
Abstract : Dimethyl fumarate (DMF) is a first-line prodrug for the treatment of relapsing-remitting multiple sclerosis (RRMS) that is completely metabolized to monomethyl fumarate (MMF), the active metabolite, before reaching the systemic circulation. Its metabolism has been proposed to be due to ubiquitous esterases in the intestines and other tissues, but the specific enzymes involved are unknown. We hypothesized based on its structure and extensive presystemic metabolism that DMF would be a carboxylesterase substrate subject to interaction with alcohol. We sought to determine the enzymes(s) responsible for the extensive presystemic metabolism of DMF to MMF and the effect of alcohol on its disposition by conducting metabolic incubation studies in human recombinant carboxylesterase-1 (CES1), carboxylesterase-2 (CES2) and human intestinal microsomes (HIM), and by performing a follow-up study in an in vivo mouse model. The in vitro incubation studies demonstrated that DMF was only metabolized to MMF by CES1. Consistent with the incubation studies, the mouse pharmacokinetic study demonstrated that alcohol decreased the maximum concentration and area-under-the-curve of MMF in the plasma and the brain after dosing with DMF. We conclude that alcohol may markedly decrease exposure to the active MMF metabolite in the plasma and brain potentially decreasing the effectiveness of DMF in the treatment of RRMS.
ESTHER : Yang_2022_PLoS.One_17_e0278111
PubMedSearch : Yang_2022_PLoS.One_17_e0278111
PubMedID: 36441753

Title : Possible Charged Residue Switch for Acylglycerol Selectivity of Lipase MAS1 - Yang_2022_Appl.Biochem.Biotechnol__
Author(s) : Yang Y , Wang J , Yang B , Lan D , Wang Y
Ref : Appl Biochem Biotechnol , : , 2022
Abstract : The amino acid residues lining the substrate binding pocket play quite an important role during the lipase catalytic process. The conversion of those residues might cause a dramatic change in the lipase properties, such as the substrate selectivity of lipase. In our study, T237 residue sitting on the entrance of the catalytic pocket in lipase MAS1 was important for the catalytic performance. When replacing polar Thr with the positively charged Arg, the synthesis ratio of partial glycerides/triglycerides increases to 6.32 rather than 1.21 of MAS1 wild type (WT), as the substrate ratio of glycerol and fatty acids is 1:3. And the fatty acid preference shifted to long-chain substrates for mutant T237R rather than middle-chain substrates for MAS1 WT. Molecular docking analysis revealed that hydrophobic and side chain properties of Arg might contribute to the change of the MAS1 lipase catalytic performance. This work would pave a way for the accurate rational transformation of the lipases to produce value lipid for industrial application.
ESTHER : Yang_2022_Appl.Biochem.Biotechnol__
PubMedSearch : Yang_2022_Appl.Biochem.Biotechnol__
PubMedID: 35695952
Gene_locus related to this paper: 9actn-h0b8d4

Title : Carboxylesterase-2 plays a critical role in dabigatran etexilate active metabolite formation - Laizure_2022_Drug.Metab.Pharmacokinet_47_100479
Author(s) : Laizure SC , Chen F , Farrar JE , Ali D , Yang B , Parker RB
Ref : Drug Metab Pharmacokinet , 47 :100479 , 2022
Abstract : Dabigatran etexilate (DABE), an oral anticoagulant prodrug, is nearly completely metabolized to the dabigatran (DAB) active metabolite by carboxylesterase-1 (CES1) and carboxylesterase-2 (CES2). The high interpatient variation in DAB plasma concentrations, coupled with its low therapeutic index, emphasizes the need to understand how CES1 and CES2 impact active metabolite formation. Previous work focused on CES1 enzyme activity but the contributions of CES2 remain unclear. The purpose of this study was to determine how CES2 activity influences DAB active metabolite formation. We compared the efficiency of DAB formation from DABE when exposed sequentially to human intestinal and then human hepatic microsomes (mimicking the normal metabolic sequence) with the reverse metabolic sequence in which DABE is exposed to hepatic and then intestinal microsomes. The poor efficiency of DAB formation with reverse sequential hydrolysis indicates that CES2 activity is crucial for active metabolite formation. Thus, the decrease in DAB formation with normal sequential hydrolysis was more sensitive to CES2 inhibition by verapamil (CES2 IC50 = 3.4 M) than CES1 inhibition by diltiazem (CES2 IC50 = 9.1 M). These results show CES2 activity plays a crucial role in DAB formation and that variability in its activity is an important determinant of therapeutic response.
ESTHER : Laizure_2022_Drug.Metab.Pharmacokinet_47_100479
PubMedSearch : Laizure_2022_Drug.Metab.Pharmacokinet_47_100479
PubMedID: 36375226

Title : Multiple acetylcholinesterases in Pardosa pseudoannulata brain worked collaboratively to provide protection from organophosphorus insecticides - Lin_2022_Ecotoxicol.Environ.Saf_248_114301
Author(s) : Lin X , Zhang Y , Yang B , Zhang L , Chen Y , Liu Z
Ref : Ecotoxicology & Environmental Safety , 248 :114301 , 2022
Abstract : Acetylcholinesterase (AChE) is an essential neurotransmitter hydrolase in nervous systems of animals and its number varies among species. So far, five AChEs have been identified in the natural enemy Pardosa pseudoannulata. Here we found that Ppace1, Ppace2 and Ppace5 were highly expressed in the spider brain, among which the mRNA level of Ppace5, but not Ppace1 and Ppace2, could be up-regulated by organophosphorus insecticides at their sublethal concentrations. In spider brain, the treatment by organophosphorus insecticides at the sublethal concentrations could increase total AChE activity, although high concentrations inhibited the activity. The activity that increased from the sublethal concentration pretreatment could compensate for the activity inhibition due to subsequent application of organophosphorus insecticides at lethal concentrations, and consequently reduce the mortality of spiders. PpAChE1 and PpAChE2 were highly sensitive to organophosphorus insecticides, and their activities would be strongly inhibited by the insecticides. In contrast, PpAChE5 displayed relative insensitivity towards organophosphorus insecticides, but with the highest catalytic efficiency for ACh. That meant the up-regulation of Ppace5 under insecticide exposure was important for maintaining AChE activity in spider brain, when PpAChE1 and PpAChE2 were inhibited by organophosphorus insecticides. The study demonstrated that multiple AChEs in the spider brain worked collaboratively, with part members for maintaining AChE activity and other members responding to organophosphorus inhibition, to provide protection from organophosphorus insecticides. In fields, high concentration insecticides are often applied when ineffective controls of insect pests occur due to relative-low concentration of insecticides in last round application. This application pattern of organophosphorus insecticides provides more chances for P. pseudoannulata to survive and controlling insect pests as a natural enemy.
ESTHER : Lin_2022_Ecotoxicol.Environ.Saf_248_114301
PubMedSearch : Lin_2022_Ecotoxicol.Environ.Saf_248_114301
PubMedID: 36410143
Gene_locus related to this paper: 9arac-KU501290 , 9arac-KU501289 , 9arac-KU501288 , 9arac-KU501287 , 9arac-v5qqc6 , 9arac-v5qqr1

Title : Probing the interaction of superparamagnetic iron oxide nanoparticles with lipase and their interacting consequences at the molecular level - Yang_2022_Toxicol.Res.(Camb)_11_654
Author(s) : Yang B , Jia R , Fang M , Wang S , Lv Z , Wang J
Ref : Toxicol Res (Camb) , 11 :654 , 2022
Abstract : BACKGROUND: Although superparamagnetic iron oxide nanoparticles (SPIONs) are used as carriers for candida rugosa lipase (CRL) in biomedical fields, their interactions and the influences on CRL are still unknown. Consequently, SPIONs were synthesized, characterized, and incubated with CRL to explore their molecular interactions and interacting consequences in this study. METHODS: The toxic effects of SPIONs on CRL and their molecular interactions were explored through transmission electron microscope, isothermal titration calorimetry, zeta potential measurements, multi-spectroscopic techniques, and biological enzyme activity tests. RESULTS: Results revealed the adsorption of SPIONs to CRL and the reduction of CRL aggregation. The unfolding and loosening of CRL structure as well as the change of secondary structure with the decrease of alpha-helix were found under SPIONs exposure. Moreover, higher SPIONs concentrations contributed to larger conformational changes and less aggregation of CRL. Meanwhile, it showed that hydrophobic forces were the dominant driving forces in the binding process, with the participation of electrostatic forces. CRL binds to SPIONs with the stoichiometry of 20.7 and the binding constant of 9.9 x 10(6) M(-1). No obvious changes were found in CRL activity due to no interference to Ser-209, Glu-341, and His-449 residues. CONCLUSION: This study examined the biological compatibility of SPIONs at the molecular level and provided important information about the structure and function of CRL upon binding to SPIONs. Our work might contribute to comprehend the molecular toxicity of SPIONs and the risks of engineered nanoparticles to human health.
ESTHER : Yang_2022_Toxicol.Res.(Camb)_11_654
PubMedSearch : Yang_2022_Toxicol.Res.(Camb)_11_654
PubMedID: 36051670

Title : New Carboxamides and a New Polyketide from the Sponge-Derived Fungus Arthrinium sp. SCSIO 41421 - She_2022_Mar.Drugs_20_
Author(s) : She J , Chen Y , Ye Y , Lin X , Yang B , Xiao J , Liu Y , Zhou X
Ref : Mar Drugs , 20 : , 2022
Abstract : New carboxamides, (+/-)-vochysiamide C (1) and (+)-vochysiamide B (2), and a new polyketide, 4S,3aS,9aR-3a,9a-deoxy-3a hydroxy-1-dehydroxyarthrinone (3), were isolated and identified from the sponge-derived fungus Arthrinium sp. SCSIO 41421, together with other fifteen known natural products (4-18). Their structures including absolute configurations were determined by detailed NMR, MS spectroscopic analyses, calculated electronic circular dichroism (ECD), as well as quantum-chemical NMR calculations. Preliminary bioactivity screening and molecular docking analysis revealed that several natural products exhibited obvious enzyme inhibitory activities against acetylcholinesterase (AChE), such as 2,3,6,8-tetrahydroxy-1-methylxanthone (4) with an inhibitory rate 86% at 50 microg/mL.
ESTHER : She_2022_Mar.Drugs_20_
PubMedSearch : She_2022_Mar.Drugs_20_
PubMedID: 35892943

Title : Monoacylglycerol lipase from marine Geobacillus sp. showing lysophospholipase activity and its application in efficient soybean oil degumming - Liu_2022_Food.Chem_406_134506
Author(s) : Liu X , Wang W , Zhao Z , Xu L , Yang B , Lan D , Wang Y
Ref : Food Chem , 406 :134506 , 2022
Abstract : Enzymatic degumming is an essential refining process to improve oil quality. In this study, a monoacylglycerol lipase GMGL was derived from marine Geobacillus sp., and was found that not only took monoacylglycerol (MAG) as substrate, but also had activity toward lysophosphatidylcholine (LPC), lysophosphatidylethanolamine (LPE) and glycerolphosphatidylcholine (GPC). Binding free energy showed LPC and LPE could bind with enzyme stably as MAG. It presented great potential in the field of enzymatic degumming. The phosphorus content in crude soybean oil decreased from 680.50 to 2.01 mg/kg and the yield of oil reached to 98.80 % after treating with phospholipase A1 (Lecitase Ultra) combined with lipase GMGL. An ultrahigh-performance liquid chromatography coupled with quadrupole time-of-flight mass spectrometry (UPLC-Q-TOF-MS) was developed to identify 21 differential phospholipids between crude soybean oil and enzymatic treatment. This work might shed some light on understanding the catalytic mechanism of monoacylglycerol lipase and provide an effective strategy for enzymatic degumming.
ESTHER : Liu_2022_Food.Chem_406_134506
PubMedSearch : Liu_2022_Food.Chem_406_134506
PubMedID: 36463594

Title : Diversified Chaetoglobosins from the Marine-Derived Fungus Emericellopsis sp. SCSIO41202 - Shao_2022_Molecules_27_
Author(s) : Shao S , Wang X , She J , Zhang H , Pang X , Lin X , Zhou X , Liu Y , Li Y , Yang B
Ref : Molecules , 27 : , 2022
Abstract : Two undescribed cytochalasins, emeriglobosins A (1) and B (2), together with nine previously reported analogues (3-11) and two known tetramic acid derivatives (12, 13) were isolated from the solid culture of Emericellopsis sp. SCSIO41202. Their structures, including the absolute configurations of their stereogenic carbons, were fully elucidated based on spectroscopic analysis and the calculated ECD. Some of the isolated compounds were evaluated for their cytotoxicity and enzyme inhibitory activity against acetylcholinesterase (AChE) in vitro. Among them, 8 showed potent AChE inhibitory activity, with an IC(50) value of 1.31 microM, and 5 showed significant cytotoxicity against PC-3 cells, with an IC(50) value of 2.32 microM.
ESTHER : Shao_2022_Molecules_27_
PubMedSearch : Shao_2022_Molecules_27_
PubMedID: 35335187

Title : Multifunctional Fluorescent Probe for Simultaneously Detecting Microviscosity, Micropolarity, and Carboxylesterases and Its Application in Bioimaging - Qi_2022_Anal.Chem__
Author(s) : Qi YL , Wang HR , Chen LL , Yang B , Yang YS , He ZX , Zhu HL
Ref : Analytical Chemistry , : , 2022
Abstract : Based on OR logic gate, we proposed a smart near-infrared (NIR) fluorescent probe, named VPCPP, for simultaneously monitoring local microviscosity, micropolarity, and carboxylesterases (CEs) in living cells through blue and red channels. This proposed probe was capable of distinguishing cancer cells from normal cells and had good potential for identifying living liver cell lines. Furthermore, the fluctuations of the three analytes of interest in different cell status was successfully explored. Particularly, facilitated with high-content analysis (HCA) and VPCPP, a simple and efficient high-throughput screening (HTS) platform was first constructed for screening antitumor drugs and studying their effect on the analytes. For the first time, we found that sorafenib-induced ferroptosis led to an increase in the microviscosity and up-regulation of CEs at the same time. Additionally, the procedure that aristolochic acid (AA) induced the overexpression of CEs was verified. Besides, VPCPP was utilized for imaging the variations of the two microenvironment parameters and CEs in the inflammation model. Finally, VPCPP was able to image the tumor ex vivo and in vivo through two channels and one channel separately, as well as to visualize the kidneys and liver ex vivo with dual emissions, which indicated that the probe had great potential for imaging applications such as medical diagnosis, preclinical research, and imaging-guided surgery.
ESTHER : Qi_2022_Anal.Chem__
PubMedSearch : Qi_2022_Anal.Chem__
PubMedID: 35255210

Title : Pyrrolyl 4-quinolone alkaloids from the mangrove endophytic fungus Penicillium steckii SCSIO 41025: Chiral resolution, configurational assignment, and enzyme inhibitory activities - Chen_2021_Phytochemistry_186_112730
Author(s) : Chen CM , Chen WH , Pang XY , Liao SR , Wang JF , Lin XP , Yang B , Zhou XF , Luo XW , Liu YH
Ref : Phytochemistry , 186 :112730 , 2021
Abstract : Six undescribed 4-quinolone alkaloids, including four racemic mixtures, (+/-)-oxypenicinolines A-D, and two related ones, penicinolines F and G, together with seven known analogues, were isolated from the mangrove-derived fungus Penicillium steckii SCSIO 41025 (Trichocomaceae). The racemates were separated by HPLC using chiral columns. Their structures including absolute configurations were elucidated by extensive spectroscopic analysis, electronic circular dichroism (ECD) experiments, and single-crystal X-ray diffraction analysis. Structurally, (+/-)-oxypenicinolines A-D shared with an unusual 6/6/5/5 tetracyclic system incorporating a rare tetrahydro-pyrrolyl moiety. A plausible biosynthetic pathway for pyrrolyl 4-quinolone alkaloids is proposed. (+/-)-oxypenicinoline A and quinolactacide displayed alpha-glucosidase inhibitory activity with the IC(50) values of 317.8 and 365.9 micro, respectively, which were more potent than that of acarbose (461.0 microM). Additionally, penicinoline and penicinoline E showed weak inhibitions toward acetylcholinesterase (AChE).
ESTHER : Chen_2021_Phytochemistry_186_112730
PubMedSearch : Chen_2021_Phytochemistry_186_112730
PubMedID: 33740577

Title : An Evolving Technology That Integrates Classical Methods with Continuous Technological Developments: Thin-Layer Chromatography Bioautography - Wang_2021_Molecules_26_
Author(s) : Wang M , Zhang Y , Wang R , Wang Z , Yang B , Kuang H
Ref : Molecules , 26 : , 2021
Abstract : Thin-layer chromatography (TLC) bioautography is an evolving technology that integrates the separation and analysis technology of TLC with biological activity detection technology, which has shown a steep rise in popularity over the past few decades. It connects TLC with convenient, economic and intuitive features and bioautography with high levels of sensitivity and specificity. In this study, we discuss the research progress of TLC bioautography and then establish a definite timeline to introduce it. This review summarizes known TLC bioautography types and practical applications for determining antibacterial, antifungal, antitumor and antioxidant compounds and for inhibiting glucosidase, pancreatic lipase, tyrosinase and cholinesterase activity constitutes. Nowadays, especially during the COVID-19 pandemic, it is important to identify original, natural products with anti-COVID potential compounds from Chinese traditional medicine and natural medicinal plants. We also give an account of detection techniques, including in situ and ex situ techniques; even in situ ion sources represent a major reform. Considering the current technical innovations, we propose that the technology will make more progress in TLC plates with higher separation and detection technology with a more portable and extensive scope of application. We believe this technology will be diffusely applied in medicine, biology, agriculture, animal husbandry, garden forestry, environmental management and other fields in the future.
ESTHER : Wang_2021_Molecules_26_
PubMedSearch : Wang_2021_Molecules_26_
PubMedID: 34361800

Title : Synergistic Interaction between the Entomopathogenic Fungus Akanthomyces attenuatus (Zare & Gams) and the Botanical Insecticide Matrine against Megalurothrips usitatus (Bagrall) - Wu_2021_J.Fungi.(Basel)_7_
Author(s) : Wu J , Yang B , Zhang X , Cuthbertson AGS , Ali S
Ref : J Fungi (Basel) , 7 : , 2021
Abstract : The excessive use of synthetic chemicals for Megalurothrips usitatus (Bagrall) management has resulted in the development of insecticide resistance as well as adverse effects to the natural ecosystem. This has driven the need to develop alternative pest control strategies. This study reports a synergistic interaction between the entomopathogenic fungus Akanthomyces attenuatus (Zare & Gams) and the botanical insecticide matrine against M. usitatus. The results revealed that the germination rate and colony growth of A. attenuatus were inhibited by higher matrine concentrations. Percentage mortalities of M. usitatus following application of A. attenuatus and matrine showed a dose mortality effect. After five days of treatment, all concentrations of matrine combined with different concentrations of A. attenuatus, except one combination (matrine 0.25 mg/mL + 1 x 10(7) conidia/mL), showed synergistic effect. The activities of acetylcholinesterase and antioxidant enzymes (superoxide dismutase, catalase and peroxidase) in M. usitatus, in response to individual or combined application of A. attenuatus and matrine at the end of the experimental period, were significantly lower than controls. The findings confirm the synergistic action of A. attenuatus and matrine against M. usitatus along with the biochemical phenomenon possibly regulating the synergistic effect.
ESTHER : Wu_2021_J.Fungi.(Basel)_7_
PubMedSearch : Wu_2021_J.Fungi.(Basel)_7_
PubMedID: 34356915

Title : Bioactive Polyketide and Diketopiperazine Derivatives from the Mangrove-Sediment-Derived Fungus Aspergillus sp. SCSIO41407 - Cai_2021_Molecules_26_
Author(s) : Cai J , Chen C , Tan Y , Chen W , Luo X , Luo L , Yang B , Liu Y , Zhou X
Ref : Molecules , 26 : , 2021
Abstract : Ten polyketide derivatives (1-10), including a new natural product named (E)-2,4-dihydroxy-3-methyl-6-(2-oxopent-3-en-1-yl) benzaldehyde (1), and five known diketopiperazines (11-15), were isolated from the mangrove-sediment-derived fungus Aspergillus sp. SCSIO41407. The structures of 1-15 were determined via NMR and MS spectroscopic analysis. In a variety of bioactivity screening, 3 showed weak cytotoxicity against the A549 cell line, and 2 exhibited weak antibacterial activity against methicillin-resistant Staphylococcus aureus (MRSA). Compounds 3, 5, and 6 showed inhibition against acetylcholinesterase (AChE) with IC(50) values of 23.9, 39.9, and 18.6 microM. Compounds 11, 12, and 14 exhibited obvious inhibitory activities of lipopolysaccharide (LPS)-induced nuclear factor-kappaB (NF-kappaB) with IC(50) values of 19.2, 20.9, and 8.7 microM, and they also suppressed RANKL-induced osteoclast differentiation in bone marrow macrophages cells (BMMCs), with the concentration of 5 microM. In silico molecular docking with AChE and NF-kappaB p65 protein were also performed to understand the inhibitory activities, and 1, 11-14 showed obvious protein/ligand-binding effects to the NF-kappaB p65 protein.
ESTHER : Cai_2021_Molecules_26_
PubMedSearch : Cai_2021_Molecules_26_
PubMedID: 34443439

Title : Fluorometric probe for the lipase level: Design, mechanism and biological imaging application - Guan_2021_Talanta_225_121948
Author(s) : Guan P , Liu Y , Yang B , Wu Y , Chai J , Wen G , Liu B
Ref : Talanta , 225 :121948 , 2021
Abstract : To realize accurate regulation for fluorescent substrate of lipase, two series compounds (I, II) with similar structure were designed and synthesized. The flexible diphenylmethane was permitted I to go deep into the catalytic site of lipase, while rigid structure of 9H-fluoren makes itself difficult to approach the center. Series I could be effectively hydrolyzed by porcine pancreatic lipase (PPL), and the product emitted fluorescence based on aggregation-induced emission (AIE) mechanism, meanwhile different substituent groups (-Br, -Cl, -Ph, -H) on I induced the tunable hydrolysis rate. The limit of detection (LOD) was 0.05 U/mL, and linear calibration range was 0.1-4.0 U/mL, this would be effectively applied to biological detection. This result was well supported by theories calculation and molecular docking. Moreover, substrate 1 was selected to describe the distribution of lipase in many living biology such as zebrafish, Locusta migratoria and Helianthus annuus seeds coat. It was found that lipase and lipid droplets (LDs) coexist in biological systems, but there is no lipase in LDs. The designed probe gives us an opportunity to describe lipase distribution in many important tissues, including biology and medical science.
ESTHER : Guan_2021_Talanta_225_121948
PubMedSearch : Guan_2021_Talanta_225_121948
PubMedID: 33592703

Title : A glyoxylate-containing benzene derivative and butenolides from a marine algicolous fungus Aspergillus sp. SCSIO 41304 - Qi_2021_Nat.Prod.Res__1
Author(s) : Qi X , Chen WH , Lin XP , Liao SR , Yang B , Zhou XF , Liu YH , Wang JF , Li Y
Ref : Nat Prod Res , :1 , 2021
Abstract : A new glyoxylate-containing benzene derivative, methyl 2-(4-hydroxy-3-(3'-methyl-2'-butenyl)phenyl)-2-oxoacetate (1), together with ten known compounds (2-11), were isolated from the marine algicolous fungus, Aspergillus sp. SCSIO 41304. Their planar structures and absolute configurations were elucidated by detailed NMR, MS spectroscopic analysis and comparing with literature data. Compound 1 was isolated as a new fungal secondary metabolite, possessing a methyl glyoxylate moiety R-CO-CO-OCH(3), which is rare in natural sources. All the isolated compounds (1-11) were tested for their antibacterial and enzyme inhibitory activities against acetylcholinesterase (AChE) and pancreatic lipase (PL). Among these compounds, aspulvinone H (4) showed moderate inhibition against AChE and PL with IC(50) values of 25.95 and 47.06 microM, respectively. Further molecular docking simulation exhibited that compound 4 could well bind to the catalytic pockets of the AChE and PL.
ESTHER : Qi_2021_Nat.Prod.Res__1
PubMedSearch : Qi_2021_Nat.Prod.Res__1
PubMedID: 34542359

Title : A Highly Efficient Three-Liquid-Phase-Based Enzymatic One-Pot Multistep Reaction System with Recoverable Enzymes for the Synthesis of Biodiesel - Li_2021_J.Agric.Food.Chem_69_5481
Author(s) : Li Z , Chen H , Fang Y , Ma Y , Yang B , Wang Y
Ref : Journal of Agricultural and Food Chemistry , 69 :5481 , 2021
Abstract : A three-liquid-phase system (TLPS) was developed and used as a novel enzymatic one-pot multistep reaction (EOMR) system. In this system, lipase and phospholipase were enriched in a single liquid phase with a high recovery (ca. 98%) and then used for the simultaneous catalysis of mutually inhibiting and interfering reactions (hydrolysis of phospholipids and glyceride in crude oil). A novel emulsion containing the two dispersed droplets (W(2)/O/W(2) and W(1)/W(2) emulsion structures) could be the key reason for this phenomenon because the emulsion system not only provided a new catalytic interface but also relieved the product inhibition. As a result, the content of free fatty acid (main hydrolysate of the glyceride) and the removal of phospholipid from the crude oil could be increased to 96 and 95%, respectively, within 1 h. The product obtained from the EOMR was directly used in the production of biodiesel via enzymatic esterification, and the content of fatty acid methanol ester could be increased to 93% within 2 h. Furthermore, the enzymes in the middle phase could also be reused, at least for eight rounds without significant loss in catalytic efficiency. Therefore, the TLPS could be considered as an ideal catalytic platform for the EOMR.
ESTHER : Li_2021_J.Agric.Food.Chem_69_5481
PubMedSearch : Li_2021_J.Agric.Food.Chem_69_5481
PubMedID: 33955745

Title : Citrinin and alpha-pyrone derivatives with pancreatic lipase inhibitory activities from Penicillium sp. SCSIO 41302 - Han_2021_J.Asian.Nat.Prod.Res__1
Author(s) : Han WR , Song MM , Hu YW , Pang XY , Liao SR , Yang B , Zhou XF , Liu YH , Liu QC , Wang JF
Ref : J Asian Nat Prod Res , :1 , 2021
Abstract : One new citrinin monomer derivative (1), and two new natural products alpha-pyrone analogues (2a and 2b), were isolated from the sponge derived fungus Penicillium sp. SCSIO 41302. Their structures were determined by extensive spectroscopic analysis, chiral-phase HPLC analysis, modified Mosher's method, ECD calculations, and X-ray single-crystal diffraction. Bioactivity screening showed that compounds 2b and 8 exhibited obvious inhibitory activities against pancreatic lipase and acetyl cholinesterase with IC(50) values of 48.5 and 4.8 microM, respectively, which indicated that different chiral center between enantiomers (2a and 2b) might result in different biological activities (IC(50) value against PL for 2a >100 microg/ml).
ESTHER : Han_2021_J.Asian.Nat.Prod.Res__1
PubMedSearch : Han_2021_J.Asian.Nat.Prod.Res__1
PubMedID: 34762531

Title : Reduced neuropathy target esterase in pre-eclampsia suppresses tube formation of HUVECs via dysregulation of phospholipid metabolism - Li_2021_J.Cell.Physiol_236_4435
Author(s) : Li M , Shen X , Liu H , Yang B , Lu S , Tang M , Ling Y , Li Y , Kuang H
Ref : Journal of Cellular Physiology , 236 :4435 , 2021
Abstract : Recently, studies have shown that neuropathy target esterase (NTE) is essential to placental and normal blood vessel development. However, whether it is involved in abnormal placenta angiogenesis of pre-eclampsia remains unknown. Thus, our aim was to observe the expression of NTE in pre-eclamptic placentas and its effects and mechanism of NTE on the migration and the tube formation of human umbilical vein endothelial cells (HUVECs). Immunohistochemical staining showed that the NTE protein was intensely located in blood vessels of the normal pregnant placenta. However, western blot revealed that the expression level of NTE protein was significantly reduced in pre-eclamptic placenta. The results indicated that overexpression of NTE significantly promoted the migration and the tube formation of HUVECs compared with those of the control and scramble short hairpin RNA (shRNA) group. Conversely, NTE shRNA obviously inhibited the migration and the tube formation of HUVECs. Additionally, chromatography assay evidenced that NTE overexpression significantly reduced the level of phosphatidylcholine (PC) of HUVECs, but NTE shRNA obviously increased the level of PC of HUVECs. Furthermore, exogenous PC and lysophosphatidylcholine (LPC) significantly inhibited the tube formation of HUVECs in a dose-dependent manner. Collectively, our results suggest that reduced NTE in placenta may contribute to abnormal placenta angiogenesis of pre-eclampsia via the dysregulation of PC and LPC metabolism.
ESTHER : Li_2021_J.Cell.Physiol_236_4435
PubMedSearch : Li_2021_J.Cell.Physiol_236_4435
PubMedID: 33184906

Title : A novel sn-1,3 specific lipase from Janibacter sp. as catalysts for the high-yield synthesis of long-medium-long type structured triacylglycerols - Cui_2021_Food.Chem_366_130523
Author(s) : Cui R , Xu L , Lan D , Yang B , Wang Y
Ref : Food Chem , 366 :130523 , 2021
Abstract : Our study offers a novel sn-1,3 specific lipase MAJ1 from marine member Janibacter sp. strain HTCC2649 for preparing long-medium-long (LML) type structured triacylglycerols (TAGs). Firstly, the resin ECR1030 was selected as a suitable support for the immobilization of lipase MAJ1. An efficient synthesis of LML-type structured TAGs by the immobilized lipase MAJ1-catalyzed interesterification of methyl palmitate and tricaprylin was studied in a solvent-free system. The reaction conditions, including substrate molar ratio, temperature and enzyme loading, were optimized. Under the optimum conditions (immobilized lipase MAJ1 of 45 U/g, substrate molar ratio of 4:1, temperature of 35 degreesC, reaction time of 24 h), the structured TAGs with double long chains (DLCST) were obtained in a yield of 44.3 mol%. Secondly, multi-dimensional mass spectrometry-based shotgun lipidomics (MDMS-SL) was employed to quantify each TAG positional isomer in DLCST. The content of 1,3-dipalmitoyl-2-capryloyl-sn-glycerol in DLCST was 97.6% determined by the MDMS-SL technology.
ESTHER : Cui_2021_Food.Chem_366_130523
PubMedSearch : Cui_2021_Food.Chem_366_130523
PubMedID: 34303206
Gene_locus related to this paper: 9mico-a3tmr7

Title : Cyclic Peptides from the Soft Coral-Derived Fungus Aspergillus sclerotiorum SCSIO 41031 - Long_2021_Mar.Drugs_19_
Author(s) : Long J , Chen Y , Chen W , Wang J , Zhou X , Yang B , Liu Y
Ref : Mar Drugs , 19 : , 2021
Abstract : Three novel cyclic hexapeptides, sclerotides C-E (1-3), and a new lipodepsipeptide, scopularide I (4), together with a known cyclic hexapeptide sclerotide A (5), were isolated from fermented rice cultures of a soft coral-derived fungus: Aspergillus sclerotiorum SCSIO 41031. The structures of the new peptides were determined by 1D and 2D NMR spectroscopic analysis, Marfey's method, ESIMS/MS analysis, and single crystal X-ray diffraction analysis. Scopularide I (4) exhibited acetylcholinesterase inhibitory activity with an IC(50) value of 15.6 microM, and weak cytotoxicity against the human nasopharyngeal carcinoma cell line HONE-EBV with IC(50) value of 10.1 microM.
ESTHER : Long_2021_Mar.Drugs_19_
PubMedSearch : Long_2021_Mar.Drugs_19_
PubMedID: 34940700

Title : Lipopeptide Epimers and a Phthalide Glycerol Ether with AChE Inhibitory Activities from the Marine-Derived Fungus Cochliobolus Lunatus SCSIO41401 - Dai_2020_Mar.Drugs_18_
Author(s) : Dai Y , Li K , She J , Zeng Y , Wang H , Liao S , Lin X , Yang B , Wang J , Tao H , Dai H , Zhou X , Liu Y
Ref : Mar Drugs , 18 : , 2020
Abstract : A pair of novel lipopeptide epimers, sinulariapeptides A (1) and B (2), and a new phthalide glycerol ether (3) were isolated from the marine algal-associated fungus Cochliobolus lunatus SCSIO41401, together with three known chromanone derivates (4-6). The structures of the new compounds, including the absolute configurations, were determined by comprehensive spectroscopic methods, experimental and calculated electronic circular dichroism (ECD), and Mo(2) (OAc)(4)-induced ECD methods. The new compounds 1-3 showed moderate inhibitory activity against acetylcholinesterase (AChE), with IC(50) values of 1.3-2.5 M, and an in silico molecular docking study was also performed.
ESTHER : Dai_2020_Mar.Drugs_18_
PubMedSearch : Dai_2020_Mar.Drugs_18_
PubMedID: 33143384

Title : Structurally various sorbicillinoids from the deep-sea sediment derived fungus Penicillium sp. SCSIO06871 - Pang_2020_Bioorg.Chem_107_104600
Author(s) : Pang X , Zhou X , Lin X , Yang B , Tian X , Wang J , Xu S , Liu Y
Ref : Bioorg Chem , 107 :104600 , 2020
Abstract : Two new hybrid sorbicillinoids (1 and 5), three new bisorbicillinoids (2-4), and three monomeric sorbicillinoids (6-8), along with eighteen known sorbicillinoids (9-26) were isolated from cultures of the deep-sea sediment derived fungus Penicillium sp. SCSIO06871. Their structures and absolute configurations were elucidated based upon the extensive spectroscopic analysis, X-ray crystallography analysis and the comparison of the experimental and calculated ECD data. Bisorbicillpyrone A (4) is the first example of bisorbicillinoid containing an alpha-pyrone derivative unit. All of the isolated compounds were evaluated for their antibacterial, antifungal and enzyme inhibitory activities against alpha-glycosidase and acetylcholinesterase (AChE) in vitro. Compound 6 displayed more potent inhibitory activity against alpha-glycosidase than acarbose with IC(50) value of 36.0 microM and compounds 4, 12, 18, 22, 23 exhibited moderate inhibitory activity with IC(50) values ranging from 115.8 to 208.5 microM. Compounds 10 and 22 showed weak enzyme inhibitory activities against AChE with 55.1% and 51.1% inhibitions at concentration of 50 microg/mL, respectively. Besides, compounds 11 and 12 exhibited significant antibacterial activities against Staphylococcus aureus with MIC values of 10.0 and 5.0 microg/mL, respectively. The hypothetical biosynthetic pathway of the isolated sorbicillinoids with three different structural types was discussed.
ESTHER : Pang_2020_Bioorg.Chem_107_104600
PubMedSearch : Pang_2020_Bioorg.Chem_107_104600
PubMedID: 33453645

Title : How To Break the Janus Effect of H2O2 in Biocatalysis? Understanding Inactivation Mechanisms To Generate more Robust Enzymes - Zhao_2019_ACS.Catal_9_2916
Author(s) : Zhao ZX , Lan D , Tan X , Hollmann F , Bornscheuer UT , Yang B , Wang Y
Ref : ACS Catal , 9 :2916 , 2019
Abstract : H2O2, is an attractive oxidant for synthetic chemistry, especially if activated as percarboxylic acid. H2O2, however, is also a potent inactivator of enzymes. Protein engineering efforts to improve enzyme resistance against H2O2 in the past have mostly focused on tedious probabilistic directed evolution approaches. Here we demonstrate that a rational approach combining multiscale MD simulations and Born-Oppenheimer ab initio QM/MM MD simulations is an efficient approach to rapidly identify improved enzyme variants. Thus, the lipase from Penicillium camembertii was redesigned with a single mutation (I260R), leading to drastic improvements in H2O2 resistance while maintaining the catalytic activity. Also the extension of this methodology to other enzymes is demonstrated.
ESTHER : Zhao_2019_ACS.Catal_9_2916
PubMedSearch : Zhao_2019_ACS.Catal_9_2916
Gene_locus related to this paper: penca-mdgli

Title : High-level expression of Thermomyces dupontii thermo-alkaline lipase in Pichia pastoris under the control of different promoters - Wang_2019_3.Biotech_9_33
Author(s) : Wang J , Zhang T , Li Y , Li L , Wang Y , Yang B
Ref : 3 Biotech , 9 :33 , 2019
Abstract : In this study, 15 methanol-inducible and 9 constitutive promoters were used to drive the expression of Thermomyces dupontii lipase (TDL) in Pichia pastoris. Of the 15 methanol-inducible promoters, formaldehyde dehydrogenase promoter (PFLD1) showed the highest efficiency in driving lipase production, followed by alcohol oxidase 1 (PAOX1) and dihydroxyacetone synthase (PDAS1) promoters. The maximum lipase activity of transformants with PFLD1, PAOX1 and PDAS1 promoters in 5-l bioreactor was 27,076, 24,159 and 22,342 U/ml, respectively. For the nine constitutive promoters, glycosyl phosphatidyl inositol-anchored protein promoter (PGCW14) produced the highest amount of lipases in a medium containing glucose or glycerol as the only carbon source, followed by mitochondrial alcohol dehydrogenase isozyme (P0472) and glyceraldehyde-3-phosphate dehydrogenase (PGAP) promoters. The maximum lipase yields in 5-l bioreactors under the control of PGCW14, P0472 and PGAP promoters were 17,353, 15,046 and 14,276 U/ml, respectively. The result of this study not only identifies a few highly efficient promoters for the heterologous expression of TDL in P. pastoris, but also casts some insight into the optimization of protein production in heterologous systems.
ESTHER : Wang_2019_3.Biotech_9_33
PubMedSearch : Wang_2019_3.Biotech_9_33
PubMedID: 30622871
Gene_locus related to this paper: talth-f6lqk7

Title : Structure and characterization of Aspergillus fumigatus lipase B with a unique, oversized regulatory subdomain - Huang_2019_FEBS.J_286_2366
Author(s) : Huang W , Lan D , Popowicz GM , Zak KM , Zhao Z , Yuan H , Yang B , Wang Y
Ref : Febs J , 286 :2366 , 2019
Abstract : Fungal lipases are efficient and environment-friendly biocatalysts for many industrially relevant processes. One of the most widely applied lipases in the manufacturing industry is Candida antarctica lipase B (CALB). Here, we report the biochemical and structural characterization of a novel CALB-like lipase from an important human pathogen-Aspergillus fumigatus (AFLB), which has high sn-1,3-specificity toward triolein. AFLB crystal structure displays a CALB-like catalytic domain and hosts a unique tightly closed 'lid' domain that contains a disulfide bridge, as well as an extra N-terminal subdomain composed of residues 1-128 (including the helix alpha1-alpha5 located above the active site). To gain insight into the function of this novel lid and N-terminal subdomain, we constructed and characterized a series of mutants in these two domains. Deleting the protruding bulk lid's residues, replacing the bulk and tight lid with a small and loose lid from CALB, or breaking the disulfide bridge increased the affinity of CALB for glyceride substrates and improved its catalytic activity, along with the loss of enzyme fold stability and thermostability. N-terminal truncation mutants revealed that the N-terminal peptide (residues 1-59) is a strong inhibitor of AFLB binding to lipid films. This peptide thus limits AFLB's penetration power and specific activity, revealing a unique enzyme activity regulatory mechanism. Our findings on the functional and structural properties of AFLB provide a better understanding of the functions of the CALB-like lipases and pave the way for its future protein engineering. DATABASE: Structural data are available in the Protein Data Bank under the accession numbers 6IDY.
ESTHER : Huang_2019_FEBS.J_286_2366
PubMedSearch : Huang_2019_FEBS.J_286_2366
PubMedID: 30908847
Gene_locus related to this paper: aspfu-q4wg73

Title : Insight into the Modification of Phosphatidylcholine with n-3 Polyunsaturated Fatty Acids-Rich Ethyl Esters by Immobilized MAS1 Lipase - Wang_2019_Molecules_24_
Author(s) : Wang X , Qin X , Li X , Zhao Z , Yang B , Wang Y
Ref : Molecules , 24 : , 2019
Abstract : This study reported the modification of phosphatidylcholine (PC) with n-3 polyunsaturated fatty acids (PUFA)-rich ethyl esters (EE) by immobilized MAS1 lipase-catalyzed transesterification in the solvent-free system. Effects of n-3 PUFA-rich EE/PC mass ratio, enzyme loading, reaction temperature, and water dosage on the incorporation of n-3 PUFA into PC were investigated, respectively. The results indicate that the maximum incorporation of n-3 PUFA into PC reached 33.5% (24 h) under the following conditions: n-3 PUFA-rich EE/PC mass ratio of 6:1, enzyme loading of 20%, reaction temperature of 55 degrees C, and water dosage of 1.0%. After 72 h of reaction, the incorporation of n-3 PUFA into PC was 43.55% and the composition of the reaction mixture was analyzed by (31)P nuclear magnetic resonance (NMR). The results show that the reaction product consisted of 32.68% PC, 28.76% 1-diacyl-sn-glycero-3-lysophosphatidylcholine (sn-1 LPC), 4.90% 2-diacyl-sn-glycero-3-lysophosphatidylcholine (sn-2 LPC), and 33.60% sn-glycero-3-phosphatidylcholine (GPC). This study offers insight into the phospholipase activity of immobilized MAS1 lipase and suggests the extended applications of immobilized MAS1 lipase in the modification of phospholipids for industrial purpose.
ESTHER : Wang_2019_Molecules_24_
PubMedSearch : Wang_2019_Molecules_24_
PubMedID: 31569526
Gene_locus related to this paper: 9actn-h0b8d4

Title : Exploring the influence of phospholipid monolayer conformation and environmental conditions on the interfacial binding of Gibberella Zeae lipase - Wang_2019_Int.J.Biol.Macromol_132_1051
Author(s) : Wang F , Chen W , Abousalham A , Yang B , Wang Y
Ref : Int J Biol Macromol , 132 :1051 , 2019
Abstract : The involvement of different parameters on Gibberella zeae lipase (GZEL) membrane binding were characterized by using monomolecular film technology and circular dichroism spectroscopy. Among four kinds of phospholipid monolayers, 1,2dimyristoylsnglycero3phosphoethanolamine have the highest maximum insertion pressure (MIP) value. Comparing the GZEL adsorption to phosphatidylcholine monolayers with different acyl chains in sn-1 and sn-2 positions, the higher MIP values were found for 1,2dilauroylsnglycero3phosphocholine. Significantly improvement between 1,2dioleoylsnglycero3phosphocholine and 1,2distearoylsnglycero3phosphocholine suggested that the presence of fatty acid unsaturation may affect protein adsorption by changing the chemical structure in each phospholipid. The MIP value was shown higher (48.6mNm(-1)) at pH5 and pH6 (47.5+/-1.9mNm(-1)) but decreased significantly (34.2mNm(-1)) at pH9. This may indicate that the proportion of helices in the protein decreases with the alteration of the catalytic center, thus affecting the binding of the protein to its substrate. The MIP values obviously decreased with increasing salt ion concentration, suggesting that excessive salt ion concentration may destabilize the secondary and tertiary structures of the protein, thereby affecting the characteristics of its adsorption at the interfaces. Present studies improve our understanding on the protein-membrane interaction of this enzyme.
ESTHER : Wang_2019_Int.J.Biol.Macromol_132_1051
PubMedSearch : Wang_2019_Int.J.Biol.Macromol_132_1051
PubMedID: 30922913
Gene_locus related to this paper: gibze-q6wer3

Title : Epigenetic mechanisms underlying the effects of triptolide and tripchlorolide on the expression of neuroligin-1 in the hippocampus of APP\/PS1 transgenic mice - Lu_2019_Pharm.Biol_57_453
Author(s) : Lu X , Yang B , Yu H , Hu X , Nie J , Wan B , Zhang M , Lu C
Ref : Pharm Biol , 57 :453 , 2019
Abstract : Context: Neuroligin-1 (NLGN1) is a cell adhesion protein located on the excitatory postsynaptic membrane. beta-Amyloid (Abeta)-induced neuroinflammation decreases NLGN1 expression through epigenetic mechanisms. Triptolide (T10) and tripchlorolide (T4) exert protective effects on synapses in Alzheimer's disease (AD) mice, but the mechanisms remain unclear. Objective: The effects of T10 and T4 on hippocampal NLGN1 expression in AD mice and the epigenetic mechanisms were assessed using chromatin immunoprecipitation and methylated DNA immunoprecipitation. Materials and methods: Sixty APP/PS1 transgenic mice were randomly divided into an AD model group, a T10-treated group and a T4-treated group (n = 20); 20 wild-type littermates served as the control group. APP/PS1 transgenic mice were intraperitoneally injected with T10 (0.1 mg/kg) and T4 (25 mug/kg) once per day for 60 days. NLGN1 expression was examined using western blotting and quantitative PCR. Results: T10 and T4 increased the levels of the NLGN1 protein and mRNA in hippocampus of AD mice. T10 and T4 inhibited the binding of HDAC2 (p< 0.01) and MeCP2 (p< 0.01 and p< 0.05, respectively) to the NLGN1 promoter, and cytosine methylation (1.2305 +/- 0.1482/1.2554 +/- 0.3570 vs. 1.6578 +/- 0.1818, p< 0.01) at the NLGN1 promoter in the hippocampus of AD mice. T10 and T4 increased the level of acetylated histone H3 (0.7733 +/- 0.1611/0.8241 +/- 0.0964 vs. 0.5587 +/- 0.0925, p< 0.01) at the NLGN1 promoter in the hippocampus of AD mice. Conclusions: T10 and T4 may increase hippocampal NLGN1 expression in AD mice through epigenetic mechanisms, providing a new explanation for the mechanism underlying the protective effects of T10 and T4 on synapses.
ESTHER : Lu_2019_Pharm.Biol_57_453
PubMedSearch : Lu_2019_Pharm.Biol_57_453
PubMedID: 31311385

Title : A novel strategy to improve the thermostability of Penicillium camembertii mono- and di-acylglycerol lipase - Liu_2018_Biochem.Biophys.Res.Commun_500_639
Author(s) : Liu Y , Yuan D , Zhao Z , Lan D , Yang B , Wang Y
Ref : Biochemical & Biophysical Research Communications , 500 :639 , 2018
Abstract : Penicillium camembertii (PCL), a mono- and di-acylglycerol lipase (DGL), has the vital potential in the oil chemistry for food industry. However, known DGLs are mesophilic enzymes which restricts its application in the industry. To improve thermostability of PCL, we used amino acid substitution by comparison of amino acids compositions of PCL and protein sequences from typical thermophilic bacteria. Then, some conservative residues around active center were avoided to mutate according to homologous alignment analyses. Furthermore, the list was narrowed down to 28 candidate mutational sites of PCL by analyzing the hydrophobic interaction of amino acids in the structure. And among them only the mutant PCL-D25R had formed an additional salt bridge between R25-D32 and increased more hydrogen bonds interaction. Therefore, mutant PCL-D25R were constructed and expressed. Thermal inactivation assay showed that the half-life of mutant PCL-D25R at 45 degrees C increased 4-fold compared to that of PCL-WT. Melting temperature of mutant PCL-D25R increased to 49.5 degrees C from 46.5 degrees C by fluorescence-based thermal stability assay. This study provides a valuable strategy for engineering DGL thermostability.
ESTHER : Liu_2018_Biochem.Biophys.Res.Commun_500_639
PubMedSearch : Liu_2018_Biochem.Biophys.Res.Commun_500_639
PubMedID: 29679572
Gene_locus related to this paper: penca-mdgli

Title : Function of C-terminal peptides on enzymatic and interfacial adsorption properties of lipase from Gibberella zeae - Wang_2018_Biochim.Biophys.Acta.Gen.Subj_1862_2623
Author(s) : Wang F , Zhang H , Czarna A , Chen W , Yang B , Wang Y
Ref : Biochimica & Biophysica Acta Gen Subj , 1862 :2623 , 2018
Abstract : BACKGROUND: The crystal structure of lipase from Gibberella zeae (GZEL) indicates that its C-terminal extension is composed of a loop and a alpha-helix. This structure is unique, possibly providing novel evidence on lipase mechanisms. METHODS: Two C-terminally truncated mutants (GZEL-Delta(alpha-helix) and GZEL-Delta(alpha-helix+loop)) were constructed. The role of these secondary structure segments on enzymatic activities and interfacial binding properties of GZEL was investigated by using conventional pH-stat method and monomolecular film techniques. In addition, inactive variants (Ser144Ala) of wild-type GZEL and two truncated mutants were constructed and produced specifically for interfacial binding experiments. RESULTS: Compared to the wild-type GZEL, lipase and phospholipase activities were significantly decreased in the two mutants. Deletion of the alpha-helix had great influence on the lipase activity of GZEL, resulting in residual 7.3% activity; the additional deletion of the loop led to 8.1% lipase activity. As for the phospholipase function, residual activities of 63.0% and 35.4% were maintained for GZEL-Delta(alpha-helix) and GZEL-Delta(alpha-helix+loop), respectively. Findings obtained with monomolecular film experiments further indicated that the reduction in phospholipase activity occurred with the anionic phospholipid as substrate, but was not seen with zwitterionic phospholipid. Results of the maximum insertion pressure, synergy factor and binding kinetic parameters documented that the alpha-helix structure of GZEL strongly influence the binding and insertion of enzyme to the phospholipid monolayer. Moreover, the interfacial binding function of alpha-helix was partly conformed by connecting to the C-terminal of Aspergillus oryzae lipase. GENERAL SIGNIFICANCE: Our results provide important information on the understanding of the structure-function relationship of GZEL.
ESTHER : Wang_2018_Biochim.Biophys.Acta.Gen.Subj_1862_2623
PubMedSearch : Wang_2018_Biochim.Biophys.Acta.Gen.Subj_1862_2623
PubMedID: 30025859

Title : Highly Efficient Deacidification of High-Acid Rice Bran Oil Using Methanol as a Novel Acyl Acceptor - Li_2018_Appl.Biochem.Biotechnol_184_1061
Author(s) : Li D , Faiza M , Ali S , Wang W , Tan CP , Yang B , Wang Y
Ref : Appl Biochem Biotechnol , 184 :1061 , 2018
Abstract : A highly efficient process for reducing the fatty acid (FA) content of high-acid rice bran oil (RBO) was developed by immobilized partial glycerides-selective lipase SMG1-F278N-catalyzed esterification/transesterification using methanol as a novel acyl acceptor. Molecular docking simulation indicated that methanol was much closer to the catalytic serine (Ser-171) compared with ethanol and glycerol, which might be one of the reasons for its high efficiency in the deacidification of high-acid RBO. Additionally, the reaction parameters were optimized to minimize the FA content of high-acid RBO. Under the optimal conditions (substrate molar ratio of methanol to FAs of 1.8:1, enzyme loading of 40sU/g, and at 30s degreesC), FA content decreased from 25.14 to 0.03% after 6sh of reaction. Immobilized SMG1-F278N exhibited excellent methanol tolerance and retained almost 100% of its initial activity after being used for ten batches. After purification by molecular distillation, the final product contained 97.86% triacylglycerol, 2.10% diacylglycerol, and 0.04% FA. The acid value of the final product was 0.09smg KOH/g, which reached the grade one standard of edible oil. Overall, methanol was a superior acyl acceptor for the deacidification of high-acid RBO and the high reusability of immobilized SMG1-F278N indicates an economically attractive process.
ESTHER : Li_2018_Appl.Biochem.Biotechnol_184_1061
PubMedSearch : Li_2018_Appl.Biochem.Biotechnol_184_1061
PubMedID: 28948493
Gene_locus related to this paper: malgo-a8puy1

Title : Effects of acute and chronic exposures of fluoxetine on the Chinese fish, topmouth gudgeon Pseudorasbora parva - Chen_2018_Ecotoxicol.Environ.Saf_160_104
Author(s) : Chen H , Zeng X , Mu L , Hou L , Yang B , Zhao J , Schlenk D , Dong W , Xie L , Zhang Q
Ref : Ecotoxicology & Environmental Safety , 160 :104 , 2018
Abstract : Fluoxetine is a selective serotonin reuptake inhibitor used as an antidepressant and has been frequently detected in aquatic environments. However, its effects in fish from Asia remain relatively less studied. In this study, the topmouth gudgeon Pseudorasbora parva was exposed to 0, 50, and 200microg/L of fluoxetine for 4h and 42 d. The effects of fluoxetine on biometrics were compared to biochemical endpoints indicative of stress in different fish tissues (brain, liver, gills and intestine) following exposures. In fish exposed for 42 d, lipid peroxidation endpoints were enhanced 80% in the liver and gills. Acetylcholinesterase (AChE) activity was increased 40% after exposure to 50microg/L and 55% at 200microg/L following 4h exposure. In contrast AChE was increased 26% (at 50microg/L) after 42 d of exposures. Enhanced ethoxyresorufin-O-deethylase activity (EROD) was detected only in fish exposed to 50microg/L of fluoxetine for 4h. The activity of alpha-glucosidase (alpha-Glu) was also induced (at 200microg/L) after 4h of exposure. After 4h of exposure, the activities of proteases in the intestine were generally inhibited at 200microg/L. Both 4h and 42 d exposures resulted in an increased hepatosomatic index (HSI) but did not affect the condition factor (CF). Our results demonstrate that fluoxetine significantly altered biochemical endpoints in P. parva after acute exposure and the morphological changes in liver size were not observed until 42d of exposure.
ESTHER : Chen_2018_Ecotoxicol.Environ.Saf_160_104
PubMedSearch : Chen_2018_Ecotoxicol.Environ.Saf_160_104
PubMedID: 29793199

Title : Inhibitory Influence of Panax notoginseng Saponins on Aspirin Hydrolysis in Human Intestinal Caco-2 Cells - Sun_2018_Molecules_23_
Author(s) : Sun Z , Wu Y , Yang B , Zhu B , Hu S , Lu Y , Zhao B , Du S
Ref : Molecules , 23 : , 2018
Abstract : Herb-drug interactions are important safety concerns in clinical practice. The interactions occur firstly in the intestinal absorption for orally administered drugs. Aspirin and Panax notoginseng saponins (PNS)-based drugs are often combined in China to prevent larger-artery atherosclerosis. Here, we aimed to characterize the aspirin transport across Caco-2 cell monolayers, a model of the intestinal absorption, and further to evaluate the influence of PNS on aspirin hydrolysis and the relating mechanisms. Transcellular transport of aspirin and the influence of PNS were explored using Caco-2 cell monolayers. The protein expression of human carboxylesterase 1 (hCE1) and hCE2 in Caco-2 cells after PNS treatment was analyzed by ELISA, and the mRNA level were determined by qRT-PCR. In the study, Caco-2 cells showed high level of hydrolase activity, and most aspirin was hydrolyzed inside the cells during the transport process. Interestingly, PNS were demonstrated to inhibit the esterase activities responsible for aspirin hydrolysis in Caco-2 cells. PNS could also decrease the protein expression of hCE1 and hCE2, whereas exhibited minor effect on the mRNA expression. These results indicated that oral administration of PNS-based drugs might inhibit the hydrolysis of aspirin during intestinal absorption thus promoting its bioavailability.
ESTHER : Sun_2018_Molecules_23_
PubMedSearch : Sun_2018_Molecules_23_
PubMedID: 29463025

Title : A comparative study on kinetics and substrate specificities of Phospholipase A1 with Thermomyces lanuginosus lipase - Xin_2017_J.Colloid.Interface.Sci_488_149
Author(s) : Xin R , Khan FI , Zhao Z , Zhang Z , Yang B , Wang Y
Ref : J Colloid Interface Sci , 488 :149 , 2017
Abstract : The mechanism of lipase binding to the lipid-water interface is crucial for substrate specificity and kinetic properties. In this study, the chain-length specificity, regiospecificity and substrate specificity of Phospholipase A1 (PLA1) and its parent enzyme Thermomyces lanuginosus lipase (TLL) have been investigated using a classical emulsion system. The results show that both PLA1 and TLL are 1,3-regioselective lipases. Additionally, the hydrolytic activity of PLA1 is comparatively lower on short-chain triacylglyceride (TAG) and higher on phosphatidylcholine (PC) than the hydrolytic activity of TLL. Further, the results obtained with monolayer film techniques demonstrate that the C-terminal region regulates the binding of PLA1 to PC. A hypothesis is presented according to which the alpha9 helix of C-terminal region in PLA1 not only controls the opening of lid but also serves as a membrane anchor that assists in binding to PC. These findings bring new insight into rational design of novel lipases with intriguing functionalities.
ESTHER : Xin_2017_J.Colloid.Interface.Sci_488_149
PubMedSearch : Xin_2017_J.Colloid.Interface.Sci_488_149
PubMedID: 27821336

Title : Molecular interaction studies of acetylcholinesterase with potential acetylcholinesterase inhibitors from the root of Rhodiola crenulata using molecular docking and isothermal titration calorimetry methods - Li_2017_Int.J.Biol.Macromol_104_527
Author(s) : Li FJ , Liu Y , Yuan Y , Yang B , Liu ZM , Huang LQ
Ref : Int J Biol Macromol , 104 :527 , 2017
Abstract : (-)-Epicatechin gallate ((-)-ECG), 1,2,3,4,6-O-pentagalloylglucose (PGG), rhodionin, herbacetin and rhodiosin isolated from the root of Rhodiola crenulata exhibited potent, dose-dependent inhibitory effects on acetylcholinesterase (AChE) with IC50 ranged from 57.50+/-5.83 to 2.43+/-0.34mug/mL. With the aim of explaining the differences in activity of these active ingredients and clarifying how they inhibit AChE, the AChE-inhibitor interactions were further explored using molecular docking and isothermal titration calorimetry (ITC) methods in the present study. Molecular docking studies revealed that all compounds except PGG showed binding energy values ranging from -10.30 to -8.00kcal/mol while the binding energy of galantamine, a known AChE inhibitor, was -9.53kcal/mol; they inhibited the AChE by binding into the ligand pocket with the similar binding pattern to that of galantamine by interacting with Glu199 of AChE. Inhibition constant of these active ingredients had a positive correlation with binding energy. The interaction between AChE and PGG was further evaluated with the ITC method and the results indicated that the PGG-AChE interaction was relevant to AChE concentration. The results revealed a possible mechanism for the AChE inhibition activity of these bioactive ingredients, which may provide some help in lead compounds optimization in the future.
ESTHER : Li_2017_Int.J.Biol.Macromol_104_527
PubMedSearch : Li_2017_Int.J.Biol.Macromol_104_527
PubMedID: 28625836

Title : Point mutations in acetylcholinesterase 1 associated with chlorpyrifos resistance in the brown planthopper, Nilaparvata lugens Stal - Zhang_2017_Insect.Mol.Biol_26_453
Author(s) : Zhang Y , Yang B , Li J , Liu M , Liu Z
Ref : Insect Molecular Biology , 26 :453 , 2017
Abstract : Insecticide resistance frequently results from target-site insensitivity, such as point mutations in acetylcholinesterases (AChEs) for resistance to organophosphates and carbamates. From a field-originated population of Nilaparvata lugens, a major rice pest, a resistant population (R9) was obtained by nine-generation continuous selection with chlorpyrifos. From the same field population, a relatively susceptible population (S9) was also constructed through rearing without any insecticides. Compared to the susceptible strain, Sus [medium lethal dose (LC50 ) = 0.012 mg/l], R9 had a resistance ratio (RR) of 253.08-fold, whereas the RR of S9 was only 2.25-fold. Piperonyl butoxide and triphenyl phosphate synergized chlorpyrifos in R9 less than three-fold, indicating other important mechanisms for high resistance. The target-site insensitivity was supported by the key property differences of crude AChEs between R9 and S9. Compared to S9, three mutations (G119S, F331C and I332L) were detected in NlAChE1 from individuals of the R9 and field populations, but no mutation was detected in NlAChE2. G119S and F331C could decreased insecticide sensitivities in recombinant NlAChE1, whereas I332L took effect through increasing the influence of F331C on target insensitivity. F331C might be deleterious because of its influence on the catalytic efficiency of NlAChE1, whereas I332L would decrease these adverse effects and maintain the normal functions of AChEs.
ESTHER : Zhang_2017_Insect.Mol.Biol_26_453
PubMedSearch : Zhang_2017_Insect.Mol.Biol_26_453
PubMedID: 28407384

Title : Immobilized MAS1 lipase showed high esterification activity in the production of triacylglycerols with n-3 polyunsaturated fatty acids - Wang_2017_Food.Chem_216_260
Author(s) : Wang X , Li D , Qu M , Durrani R , Yang B , Wang Y
Ref : Food Chem , 216 :260 , 2017
Abstract : Immobilization of lipase MAS1 from marine Streptomyces sp. strain W007 and its application in catalyzing esterification of n-3 polyunsaturated fatty acids (PUFA) with glycerol were investigated. The resin XAD1180 was selected as a suitable support for the immobilization of lipase MAS1, and its absorption ability was 75mg/g (lipase/resin ratio) with initial buffer pH value of 8.0. The thermal stability of immobilized MAS1 was improved significantly compared with that of the free lipase. Immobilized MAS1 had no regiospecificity in the hydrolysis of triolein. The highest esterification degree (99.31%) and TAG content (92.26%) by immobilized MAS1-catalyzed esterification were achieved under the optimized conditions, which were significantly better than those (82.16% and 47.26%, respectively) by Novozym 435. More than 92% n-3 PUFA was incorporated into TAG that had similar fatty acids composition to the substrate (n-3 PUFA). The immobilized MAS1 exhibited 50% of its initial activity after being used for five cycles.
ESTHER : Wang_2017_Food.Chem_216_260
PubMedSearch : Wang_2017_Food.Chem_216_260
PubMedID: 27596418
Gene_locus related to this paper: 9actn-h0b8d4

Title : Juvenile Hormone Epoxide Hydrolase: a Promising Target for Hemipteran Pest Management - Tusun_2017_Sci.Rep_7_789
Author(s) : Tusun A , Li M , Liang X , Yang T , Yang B , Wang G
Ref : Sci Rep , 7 :789 , 2017
Abstract : Juvenile hormone epoxide hydrolase (JHEH) has attracted great interest because of its critical role in the regulation of juvenile hormone (JH) in insects. In this study, one JHEH gene from Apolygus lucorum (AlucJHEH) was characterized in terms of deduced amino acid sequence, phylogeny, homology modeling and docking simulation. The results reveals a conserved catalytic mechanism of AlucJHEH toward JH. Our study also demonstrates that the mRNA of AlucJHEH gene was detectable in head, thorax and abdomen from all life stages. To functionally characterize the AlucJHEH gene, three fragments of double-stranded RNAs (dsRNAs) were designed to target different regions of the sequence. Injection of 3rd nymphs with dsRNA fragments successfully knocked down the target gene expression, and a significantly decreased survival rate was observed, together with a molting block, These findings confirm the important regulatory roles of AlucJHEH in A. lucorum and indicate this gene as a promising target for future hemipterans pest control.
ESTHER : Tusun_2017_Sci.Rep_7_789
PubMedSearch : Tusun_2017_Sci.Rep_7_789
PubMedID: 28400585

Title : Recombinant Lipase from Gibberella zeae Exhibits Broad Substrate Specificity: A Comparative Study on Emulsified and Monomolecular Substrate - Wang_2017_Int.J.Mol.Sci_18_
Author(s) : Wang F , Zhang H , Zhao Z , Wei R , Yang B , Wang Y
Ref : Int J Mol Sci , 18 : , 2017
Abstract : Using the classical emulsified system and the monomolecular film technique, the substrate specificity of recombinant Gibberella zeae lipase (rGZEL) that originates from Gibberella zeae was characterized in detail. Under the emulsified reaction system, both phospholipase and glycolipid hydrolytic activities were observed, except for the predominant lipase activity. The optimum conditions for different activity exhibition were also determined. Compared with its lipase activity, a little higher ratio of glycolipid hydrolytic activity (0.06) than phospholipase activity (0.02) was found. rGZEL preferred medium chain-length triglycerides, while lower activity was found for the longer-chain triglyceride. Using the monomolecular film technique, we found that the preference order of rGZEL to different phospholipids was 1,2-diacyl-sn-glycero-3-phospho-l-serine (PS) > 1,2-dioleoyl-sn-glycero-3-phospho-rac-(1-glycerol) sodium salt (PG) > 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) > l-alpha-phosphatidylinositol (PI) > cardiolipin (CL) > 3-sn-phosphatidic acid sodium salt (PA) > l-alpha-phosphatidylethanolamine (PE), while no hydrolytic activity was detected for sphingomyelin (SM). Moreover, rGZEL showed higher galactolipase activity on 1,2-distearoyimonoglactosylglyceride (MGDG). A kinetic study on the stereo- and regioselectivity of rGZEL was also performed by using three pairs of pseudodiglyceride enantiomers (DDGs). rGZEL presented higher preference for distal DDG enantiomers than adjacent ester groups, however, no hydrolytic activity to the sn-2 position of diglyceride analogs was found. Furthermore, rGZEL preferred the R configuration of DDG enantiomers. Molecular docking results were in concordance with in vitro tests.
ESTHER : Wang_2017_Int.J.Mol.Sci_18_
PubMedSearch : Wang_2017_Int.J.Mol.Sci_18_
PubMedID: 28718792
Gene_locus related to this paper: gibze-q6wer3

Title : Engineering a lipase B from Candida antactica with efficient perhydrolysis performance by eliminating its hydrolase activity - Wang_2017_Sci.Rep_7_44599
Author(s) : Wang XP , Zhou PF , Li ZG , Yang B , Hollmann F , Wang YH
Ref : Sci Rep , 7 :44599 , 2017
Abstract : A Ser105Ala mutant of the lipase B from Candida antarctica enables 'perhydrolase-only' reactions. At the example of the chemoenzymatic Baeyer-Villiger oxidation of cyclohexanone, we demonstrate that with this mutant selective oxidation can be achieved in deep eutectic solvent while essentially eliminating the undesired hydrolysis reaction of the product.
ESTHER : Wang_2017_Sci.Rep_7_44599
PubMedSearch : Wang_2017_Sci.Rep_7_44599
PubMedID: 28317884

Title : Hirschsprung disease is associated with an L286P mutation in the fifth transmembrane domain of the endothelin-B receptor in the N-ethyl-N-nitrosourea-induced mutant line - Chen_2016_Exp.Anim_65_245
Author(s) : Chen B , Ouyang HL , Wang WH , Yin YH , Yan LN , Yang B , Xue ZF
Ref : Exp Anim , 65 :245 , 2016
Abstract : Hirschsprung disease (HSCR), or colonic aganglionosis, is a congenital disorder characterized by the absence of intramural ganglia along variable lengths of the colon, resulting in intestinal obstruction. It is the most common cause of congenital intestinal obstruction, with an incidence of 1 in 5,000 live births. N-ethyl-N-nitrosourea (ENU)-induced mutagenesis is a powerful tool for the study of gene function and the generation of human disease models. In the current study, a novel mutant mouse with aganglionic megacolon and coat color spotting was generated by ENU-induced mutagenesis. Histological and acetylcholinesterase (AChE) whole-mount staining analysis showed a lack of ganglion cells in the colon in mutant mice. The mutation was mapped to chromosome 14 between markers rs30928624 and D14Mit205 (Chr 14 positions 103723921 bp and 105054651 bp). The Ednrb (Chr 14 position 103814625-103844173 bp) was identified as a potential candidate gene in this location. Mutation analysis revealed a T>C missense mutation at nucleotide 857 of the cDNA encoding endothelin receptor B (EDNRB) in which a proline was substituted for the highly conserved Lys-286 residue (L286P) in the fifth transmembrane (TM V) domain of this G protein-coupled receptor. The mutant mouse was named Ednrb(m1yzcm) (Ednrb; mutation 1, Yangzhou University Comparative Medicine Center). The results of the present study implicate the structural importance of the TM V domain in Ednrb function, and the Ednrb(m1yzcm) mouse represents a valuable model for the study of HSCR in humans.
ESTHER : Chen_2016_Exp.Anim_65_245
PubMedSearch : Chen_2016_Exp.Anim_65_245
PubMedID: 26923755

Title : Screening and characterization of a thermostable lipase from marine Streptomyces sp. strain W007 - Yuan_2016_Biotechnol.Appl.Biochem_63_41
Author(s) : Yuan D , Lan D , Xin R , Yang B , Wang Y
Ref : Biotechnol Appl Biochem , 63 :41 , 2016
Abstract : A screening method along with the combination of genome sequence of microorganism, pairwise alignment, and lipase classification was used to search the thermostable lipase. Then, a potential thermostable lipase (named MAS1) from marine Streptomyces sp. strain W007 was expressed in Pichia pastoris X-33, and the biochemical properties were characterized. Lipase MAS1 belongs to the subfamily I.7, and it has 38% identity to the well-characterized Bacillus subtilis thermostable lipases in the subfamily I.4. The purified enzyme was estimated to be 29 kDa. The enzyme showed optimal temperature at 40 degrees C, and retained more than 80% of initial activity after 1 H incubation at 60 degrees C, suggesting that MAS1 was a thermostable lipase. MAS1 was an alkaline enzyme with optimal pH value at 7.0 and had stable activity for 12 H of incubation at pH 6.0-9.0. It was stable and retained about 90% of initial activity in the presence of Cu(2+) , Ca(2+) , Ni(2+) , and Mg(2+) , whereas 89.05% of the initial activity was retained when ethylene diamine tetraacetic acid was added. MAS1 showed the tolerance to organic solvents, but was inhibited by various surfactants. MAS1 was verified to be a triglyceride lipase and could hydrolyze triacylglycerol and diacylglycerol. The result represents a good example for researchers to discover thermostable lipase for industrial application.
ESTHER : Yuan_2016_Biotechnol.Appl.Biochem_63_41
PubMedSearch : Yuan_2016_Biotechnol.Appl.Biochem_63_41
PubMedID: 25639796
Gene_locus related to this paper: 9actn-h0b8d4

Title : Simplified Enzymatic Upgrading of High-Acid Rice Bran Oil Using Ethanol as a Novel Acyl Acceptor - Li_2016_J.Agric.Food.Chem_64_6730
Author(s) : Li D , Wang W , Durrani R , Li X , Yang B , Wang Y
Ref : Journal of Agricultural and Food Chemistry , 64 :6730 , 2016
Abstract : One of the major challenges in the upgrading of high-acid rice bran oil (RBO) is to efficiently reduce the amount of free fatty acids. Here we report a novel method for upgrading high-acid RBO using ethanol as a novel acyl acceptor in combination with a highly selective lipase from Malassezia globosa (SMG1-F278N). This process enabled an unprecedented deacidification efficiency of up to 99.80% in a short time (6 h); the immobilized SMG1-F278N used in deacidification exhibited excellent operational stability and could be used for at least 10 consecutive batches without detectable loss in activity. Scale-up was performed under optimized conditions to verify the applicability of this process, and low-acid (0.08%) RBO with a high level of gamma-oryzanol (27.8 g/kg) and gamma-oryzanol accumulation fold (1.5) was obtained after molecular distillation at lower temperature (120 degreesC). Overall, we report a simplified and efficient procedure for the production of edible RBO from high-acid RBO.
ESTHER : Li_2016_J.Agric.Food.Chem_64_6730
PubMedSearch : Li_2016_J.Agric.Food.Chem_64_6730
PubMedID: 27571030
Gene_locus related to this paper: malgo-a8puy1

Title : A Novel Process for the Synthesis of Highly Pure n-3 Polyunsaturated Fatty Acid (PUFA)-Enriched Triglycerides by Combined Transesterification and Ethanolysis - Li_2016_J.Agric.Food.Chem_64_6533
Author(s) : Li D , Wang W , Qin X , Li X , Yang B , Wang Y
Ref : Journal of Agricultural and Food Chemistry , 64 :6533 , 2016
Abstract : In this study, a novel two-step enzymatic reaction was developed for the synthesis of highly pure triacylglycerols (TAGs) with a high content of n-3 polyunsaturated fatty acids (PUFAs). Glyceride mixtures were primarily synthesized by Novozym 435-catalyzed transesterification of glycerol and DHA/EPA-rich ethyl esters (EEs), followed by removal of partial glycerides, for the first time, by immobilized mono- and diacylglycerol lipase SMG1-F278N-catalyzed ethanolysis. TAG yield as high as 98.66% was achieved under the optimized conditions, and highly pure (98.75%) n-3 PUFA-enriched TAGs with 88.44% of n-3 PUFA was obtained after molecular distillation at lower temperature (140 degreesC). In addition, the EEs produced during ethanolysis had a FA composition similar to that of the original EEs, making them feasible for cyclic utilization. This was the first study reporting removal of partial glycerides by ethanolysis. Through ethanolysis, a higher purity product could be easily obtained at a relatively low temperature compared with the conventional high-temperature molecular distillation.
ESTHER : Li_2016_J.Agric.Food.Chem_64_6533
PubMedSearch : Li_2016_J.Agric.Food.Chem_64_6533
PubMedID: 27540752
Gene_locus related to this paper: malgo-a8puy1

Title : Time Course Analysis of Skeletal Muscle Pathology of GDE5 Transgenic Mouse - Hashimoto_2016_PLoS.One_11_e0163299
Author(s) : Hashimoto T , Yang B , Okazaki Y , Yoshizawa I , Kajihara K , Kato N , Wada M , Yanaka N
Ref : PLoS ONE , 11 :e0163299 , 2016
Abstract : Glycerophosphodiesterase 5 (GDE5) selectively hydrolyses glycerophosphocholine to choline and is highly expressed in type II fiber-rich skeletal muscles. We have previously generated that a truncated mutant of GDE5 (GDE5dC471) that lacks phosphodiesterase activity and shown that transgenic mice overexpressing GDE5dC471 in skeletal muscles show less skeletal muscle mass than control mice. However, the molecular mechanism and pathophysiological features underlying decreased skeletal muscle mass in GDE5dC471 mice remain unclear. In this study, we characterized the skeletal muscle disorder throughout development and investigated the primary cause of muscle atrophy. While type I fiber-rich soleus muscle mass was not altered in GDE5dC471 mice, type II fiber-rich muscle mass was reduced in 8-week-old GDE5dC471 mice. Type II fiber-rich muscle mass continued to decrease irreversibly in 1-year-old transgenic mice with an increase in apoptotic cell. Adipose tissue weight and blood triglyceride levels in 8-week-old and 1-year-old transgenic mice were higher than those in control mice. This study also demonstrated compensatory mRNA expression of neuromuscular junction (NMJ) components, including nicotinic acetylcholine receptors (alpha1, gamma, and epsilon subunits) and acetylcholinesterase in type II fiber-rich quadriceps muscles in GDE5dC471 mice. However, we did not observe morphological changes in NMJs associated with skeletal muscle atrophy in GDE5dC471 mice. We also found that HSP70 protein levels are significantly increased in the skeletal muscles of 2-week-old GDE5dC471 mice and in mouse myoblastic C2C12 cells overexpressing GDE5dC471. These findings suggest that GDE5dC471 mouse is a novel model of early-onset irreversible type II fiber-rich myopathy associated with cellular stress.
ESTHER : Hashimoto_2016_PLoS.One_11_e0163299
PubMedSearch : Hashimoto_2016_PLoS.One_11_e0163299
PubMedID: 27658304

Title : [Safety and efficacy of human umbilical cord derived-mesenchymal stem cell transplantation for treating patients with HBV-related decompensated cirrhosis] - Yu_2016_Zhonghua.Gan.Zang.Bing.Za.Zhi_24_51
Author(s) : Yu SJ , Chen LM , Lyu S , Li YY , Yang B , Geng H , Lin H , Wang SY , Xu RN , Wang LF , Shi M , Wang FS
Ref : Zhonghua Gan Zang Bing Za Zhi , 24 :51 , 2016
Abstract : OBJECTIVE: To retrospectively investigate the efficacy of human umbilical cord-derived mesenchymal stem cells (UC-MSC) as clinical treatment for HBV-related decompensated liver cirrhosis (HBV-DLC)*D.
METHODS: Sixty patients with HBV-DLC were given standard medical treatment combined with a 3-month regimen of UC-MSC at a dose of 0.5-1.0x10(6) cells/kg/month. Another group of patients with HBV-DLC (n=120; control group) that was matched (2:1) to the case group by age, sex, diagnosis, and follow-up period was given the standard medical treatment only. We reviewed all patients' data of biochemical tests, imaging examinations, Child-Pugh scores, and adverse reactions. Comparisons of continuous data between the two groups were made by independent-sample t-test, and comparisons of categorical data were made by chi-square test.
RESULTS: Compared with the control group, the group that received the combination UC-MSC treatment showed a significant rise in cholinesterase, globulin and alkaline phosphatase, and reduced Child-Pugh scores during the follow-up period. However, there was no significant difference between the groups of patients for levels of alanine transaminase, total bilirubin, albumin, total cholesterol, or prothrombin activity.
CONCLUSIONS: Addition of the UC-MSC treatment to the standard therapy could help to improve liver function in patients with HBV-DLC.
ESTHER : Yu_2016_Zhonghua.Gan.Zang.Bing.Za.Zhi_24_51
PubMedSearch : Yu_2016_Zhonghua.Gan.Zang.Bing.Za.Zhi_24_51
PubMedID: 26983390

Title : Reduction in mRNA and protein expression of a nicotinic acetylcholine receptor alpha8 subunit is associated with resistance to imidacloprid in the brown planthopper, Nilaparvata lugens - Zhang_2015_J.Neurochem_135_686
Author(s) : Zhang Y , Wang X , Yang B , Hu Y , Huang L , Bass C , Liu Z
Ref : Journal of Neurochemistry , 135 :686 , 2015
Abstract : Target-site resistance is commonly caused by qualitative changes in insecticide target-receptors and few studies have implicated quantitative changes in insecticide targets in resistance. Here we show that resistance to imidacloprid in a selected strain of Nilaparvata lugens is associated with a reduction in expression levels of the nicotinic acetylcholine receptor (nAChR) subunit Nlalpha8. Synergism bioassays of the selected strain suggested resistance was conferred, in part, by a target-site mechanism. Sequencing of N. lugens nAChR subunit genes identified no mutations associated with resistance, however, a decrease in mRNA and protein levels of Nlalpha8 was observed during selection. RNA interference knockdown of Nlalpha8 decreased the sensitivity of N. lugens to imidacloprid, demonstrating that a decrease in Nlalpha8 expression is sufficient to confer resistance in vivo. Radioligand binding assays revealed that the affinity of the high-affinity imidacloprid-binding site of native nAChRs was reduced by selection, and reducing the amount of Nlalpha8 cRNA injected into Xenopus oocytes significantly decreased imidacloprid potency on recombinant receptors. Taken together, these results provide strong evidence that a decrease in Nlalpha8 levels confers resistance to imidacloprid in N. lugens, and thus provides a rare example of target-site resistance associated with a quantitative rather than qualitative change. In insects, target-site mutations often cause high resistance to insecticides, such as neonicotinoids acting on nicotinic acetylcholine receptors (nAChRs). Here we found that a quantitative change in target-protein level, decrease in mRNA and protein levels of Nlalpha8, contributed importantly to imidacloprid resistance in Nilaparvata lugens. This finding provides a new target-site mechanism of insecticide resistance.
ESTHER : Zhang_2015_J.Neurochem_135_686
PubMedSearch : Zhang_2015_J.Neurochem_135_686
PubMedID: 26259922

Title : Melatonin attenuates intestinal ischemia--reperfusion-induced lung injury in rats by upregulating N-myc downstream-regulated gene 2 - Yang_2015_J.Surg.Res_194_273
Author(s) : Yang B , Ni YF , Wang WC , Du HY , Zhang H , Zhang L , Zhang WD , Jiang T
Ref : J Surg Res , 194 :273 , 2015
Abstract : BACKGROUND: Successful drug treatment for ischemia--reperfusion-induced lung injury remains a major clinical problem. Melatonin (MT) is a hormone that is principally synthesized in the pineal gland. It has been shown to exhibit a variety of functions including anti-inflammatory and antioxidant effects. Previous reports on N-myc downstream-regulated gene (NDRG)2 have suggested that it is involved in cellular differentiation, development, antiapoptosis, anti-inflammatory cytokine, and antioxidant. The objective of this study was to test whether MT, a novel NDRG2 activator, can protect against intestinal ischemia-reperfusion-induced lung injury (IIRI). MATERIALS AND
METHODS: IIRI was induced in rats by occlusion of the superior mesenteric artery for 60 min, and the occlusion was then released for reperfusion. Rats were randomly divided into six groups as follows: control group; MT group; IIRI group; IIRI+5 mg/kg MT group; IIRI+15 mg/kg MT group; and IIRI+25 mg/kg MT group. The effects of MT on intestinal ischemia-reperfusion-induced lung pathologic changes, inflammatory cytokines release, myeloperoxidase and superoxide dismutase activities, and malondialdehyde level were examined. In addition, the NDRG2 activation in lung tissues was detected by Western blot analysis.
RESULTS: MT pretreatment attenuated edema and the pathologic changes in the lung. MT also decreased the levels of tumor necrosis factor-alpha, interleukin-1beta, and interleukin-8 in bronchoalveolar lavage fluid. In addition, MT markedly prevented IIRI-induced elevation of malondialdehyde and myeloperoxidase levels, as well as reduction of superoxide dismutase activity. Furthermore, the expression of NDRG2 was activated by MT pretreatment in lung tissues.
CONCLUSIONS: The present study demonstrates that MT exerted protection against IIRI-induced oxidative stress. The potential mechanism of this action may attribute partly to the activation of NDRG2 expression.
ESTHER : Yang_2015_J.Surg.Res_194_273
PubMedSearch : Yang_2015_J.Surg.Res_194_273
PubMedID: 25491174

Title : Biochemical Properties and Structure Analysis of a DAG-Like Lipase from Malassezia globosa - Xu_2015_Int.J.Mol.Sci_16_4865
Author(s) : Xu H , Lan D , Yang B , Wang Y
Ref : Int J Mol Sci , 16 :4865 , 2015
Abstract : Diacylglycerol (DAG)-like lipases are found to play an important role in the life sciences and industrial fields. A putative DAG-like lipase (MgMDL2) from Malassezia globosa was cloned and expressed in recombinant Pichia pastoris. The recombinant MgMDL2 was expressed as a glycosylated protein and purified into homogeneity by anion exchange chromatography. The activity of recombinant MgMDL2 was optimal at 15 degrees C and pH 6.0, and it keeps over 50% of relative activity at 5 degrees C, suggesting that MgMDL2 was a cold active lipase. MgMDL2 retained over 80% of initial activity after incubation at 30 and 40 degrees C for 2.5 h, but it was not stable at 50 degrees C. Incubation of methanol and ethanol at a concentration of 30% for 2 h did not affect the recombinant enzyme activity, while metal ions, including Ca2+, Mn2+ and Ni2+, sharply inhibited the MgMDL2 activity at 5 mM by 42%, 35% and 36%, respectively. MgMDL2 exhibited a preference for medium chain-length esters with highest activity toward p-nitrophenyl caprylate, while it was active on mono- and diacylglycerol but not on triacylglycerol, indicating that it was a typical DAG-like lipase. By homology modeling, Phe278 was predicted to be involved in the preference of MgMDL2 for monoacyl- and diacyl-glyceride substrates, but not triglycerides.
ESTHER : Xu_2015_Int.J.Mol.Sci_16_4865
PubMedSearch : Xu_2015_Int.J.Mol.Sci_16_4865
PubMedID: 25749469
Gene_locus related to this paper: malgo-a8puy5

Title : Residue Asn277 Affects the Stability and Substrate Specificity of the SMG1 Lipase from Malassezia globosa - Lan_2015_Int.J.Mol.Sci_16_7273
Author(s) : Lan D , Wang Q , Xu J , Zhou P , Yang B , Wang Y
Ref : Int J Mol Sci , 16 :7273 , 2015
Abstract : Thermostability and substrate specificity are important characteristics of enzymes for industrial application, which can be improved by protein engineering. SMG1 lipase from Malassezia globosa is a mono- and diacylglycerol lipase (MDL) that shows activity toward mono- and diacylglycerols, but no activity toward triacylglycerols. SMG1 lipase is considered a potential biocatalyst applied in oil/fat modification and its crystal structure revealed that an interesting residue-Asn277 may contribute to stabilize loop 273-278 and the 3104 helix which are important to enzyme characterization. In this study, to explore its role in affecting the stability and catalytic activity, mutagenesis of N277 with Asp (D), Val (V), Leu (L) and Phe (F) was conducted. Circular dichroism (CD) spectral analysis and half-life measurement showed that the N277D mutant has better thermostability. The melting temperature and half-life of the N277D mutant were 56.6 degrees C and 187 min, respectively, while that was 54.6 degrees C and 121 min for SMG1 wild type (WT). Biochemical characterization of SMG1 mutants were carried out to test whether catalytic properties were affected by mutagenesis. N277D had similar enzymatic properties as SMG1 WT, but N277F showed a different substrate selectivity profile as compared to other SMG1 mutants. Analysis of the SMG1 3D model suggested that N277D formed a salt bridge via its negative charged carboxyl group with a positively charged guanidino group of R227, which might contribute to confer N277D higher temperature stability. These findings not only provide some clues to understand the molecular basis of the lipase structure/function relationship but also lay the framework for engineering suitable MDL lipases for industrial applications.
ESTHER : Lan_2015_Int.J.Mol.Sci_16_7273
PubMedSearch : Lan_2015_Int.J.Mol.Sci_16_7273
PubMedID: 25837472
Gene_locus related to this paper: malgo-a8puy1

Title : Enzymatic selective synthesis of 1,3-DAG based on deep eutectic solvent acting as substrate and solvent - Zeng_2015_Bioprocess.Biosyst.Eng_38_2053
Author(s) : Zeng CX , Qi SJ , Xin RP , Yang B , Wang YH
Ref : Bioprocess Biosyst Eng , 38 :2053 , 2015
Abstract : In this study, enzymatic selective esterification of oleic acid with glycerol based on deep eutectic solvent acting as substrate and solvent was studied. As choline chloride (ChCl) or betaine can effectively change the chemical reaction characteristics of glycerol when they are mixed with a certain molar ratio of glycerol, several factors crucial to the lipase catalytic esterification of glycerol with oleic acid was investigated. Results showed that, betaine had more moderate effects than ChCl on the lipase, and water content had an important influence of the esterification and the enzyme selectivity. Significant changes of the glyceride compositions and enzyme selectivity were found in ChCl adding system compared with pure glycerol system; optimum accumulation of DAG especially 1,3-DAG because of the eutectic effect of ChCl was found in this system. Furthermore, in a model 1,3-DAG esterification synthesis system catalyzed by Novozym 435, high content (42.9 mol%) of the 1,3-DAG could be obtained in ChCl adding system within 1 h.
ESTHER : Zeng_2015_Bioprocess.Biosyst.Eng_38_2053
PubMedSearch : Zeng_2015_Bioprocess.Biosyst.Eng_38_2053
PubMedID: 26210852

Title : The Role of Residues 103, 104, and 278 in the Activity of SMG1 Lipase from Malassezia globosa: A Site-Directed Mutagenesis Study - Lan_2015_J.Microbiol.Biotechnol_25_1827
Author(s) : Lan D , Wang Q , Popowicz GM , Yang B , Tang Q , Wang Y
Ref : J Microbiol Biotechnol , 25 :1827 , 2015
Abstract : The SMG1 lipase from Malassezia globosa is a newly found mono- and diacylglycerol (DAG) lipase that has a unique lid in the loop conformation that differs from the common alpha-helix lid. In the present study, we characterized the contribution of three residues, L103 and F104 in the lid and F278 in the rim of the binding site groove, on the function of SMG1 lipase. Sitedirected mutagenesis was conducted at these sites, and each of the mutants was expressed in the yeast Pichia pastoris, purified, and characterized for their activity toward DAG and pnitrophenol (pNP) ester. Compared with wild-type SMG1, F278A retained approximately 78% of its activity toward DAG, but only 11% activity toward pNP octanoate (pNP-C8). L103G increased its activity on pNP-C8 by approximately 2-fold, whereas F104G showed an approximate 40% decrease in pNP-C8 activity, and they both showed decreased activity on the DAG emulsion. The deletion of 103-104 retained approximately 30% of its activity toward the DAG emulsion, with an almost complete loss of pNP-C8 activity. The deletion of 103-104 showed a weaker penetration ability to a soybean phosphocholine monolayer than wild-type SMG1. Based on the modulation of the specificity and activity observed, a pNP-C8 binding model for the ester (pNP-C8, N102, and F278 form a flexible bridge) and a specific lipidanchoring mechanism for DAG (L103 and F104 serve as "anchors" to the lipid interface) were proposed.
ESTHER : Lan_2015_J.Microbiol.Biotechnol_25_1827
PubMedSearch : Lan_2015_J.Microbiol.Biotechnol_25_1827
PubMedID: 26239010
Gene_locus related to this paper: malgo-a8puy1

Title : A mechanistic study into the epoxidation of carboxylic acid and alkene in a mono, di-acylglycerol lipase - Wang_2015_Biochem.Biophys.Res.Commun_460_392
Author(s) : Wang X , Tang Q , Popowicz GM , Yang B , Wang Y
Ref : Biochemical & Biophysical Research Communications , 460 :392 , 2015
Abstract : More and more industrial chemistry reactions rely on green technologies. Enzymes are finding increasing use in diverse chemical processes. Epoxidized vegetable oils have recently found applications as plasticizers and additives for PVC production. We report here an unusual activity of the Malassezia globosa lipase (SMG1) that is able to catalyze epoxidation of alkenes. SMG1 catalyzes formation of peroxides from long chain carboxylic acids that subsequently react with double bonds of alkenes to produce epoxides. The SMG1 is selective towards carboxylic acids and active also as a mutant lacking hydrolase activity. Moreover we present previously unobserved mechanism of catalysis that does not rely on acyl-substrate complex nor tetrahedral intermediate. Since SMG1 lipase is activated by allosteric change upon binding to the lipophilic-hydrophilic phase interface we reason that it can be used to drive the epoxidation in the lipophilic phase exclusively.
ESTHER : Wang_2015_Biochem.Biophys.Res.Commun_460_392
PubMedSearch : Wang_2015_Biochem.Biophys.Res.Commun_460_392
PubMedID: 25783054
Gene_locus related to this paper: malgo-a8puy1

Title : Expression of a novel epoxide hydrolase of Aspergillus usamii E001 in Escherichia coli and its performance in resolution of racemic styrene oxide - Hu_2015_J.Ind.Microbiol.Biotechnol_42_671
Author(s) : Hu D , Tang CD , Yang B , Liu JC , Yu T , Deng C , Wu MC
Ref : J Ind Microbiol Biotechnol , 42 :671 , 2015
Abstract : The full-length cDNA sequence of Aueh2, a gene encoding an epoxide hydrolase of Aspergillus usamii E001 (abbreviated to AuEH2), was amplified from the total RNA. Synchronously, the complete DNA sequence containing 5', 3' flanking regions, eight exons and seven introns was cloned from the genomic DNA. In addition, a cDNA fragment of Aueh2 encoding a 395-aa AuEH2 was expressed in Escherichia coli. The catalytic activity of recombinant AuEH2 (re-AuEH2) was 1.44 U/ml using racemic styrene oxide (SO) as the substrate. The purified re-AuEH2 displayed the maximum activity at pH 7.0 and 35 degrees C. It was highly stable at a pH range of 5.0-7.5, and at 40 degrees C or below. Its activity was not obviously influenced by beta-mercaptoethanol, EDTA and most of metal ions tested, but was inhibited by Hg(2+), Sn(2+), Cu(2+), Fe(3+) and Zn(2+). The K m and V max of re-AuEH2 were 5.90 mM and 20.1 U/mg towards (R)-SO, while 7.66 mM and 3.19 U/mg towards (S)-SO. Its enantiomeric ratio (E) for resolution of racemic SO was 24.2 at 10 degrees C. The experimental result of re-AuEH2 biasing towards (R)-SO was consistent with the analytical one by molecular docking (MD) simulation.
ESTHER : Hu_2015_J.Ind.Microbiol.Biotechnol_42_671
PubMedSearch : Hu_2015_J.Ind.Microbiol.Biotechnol_42_671
PubMedID: 25733186
Gene_locus related to this paper: aspng-q1ktb5

Title : In vitro and in vivo metabolism and inhibitory activities of vasicine, a potent acetylcholinesterase and butyrylcholinesterase inhibitor - Liu_2015_PLoS.One_10_e0122366
Author(s) : Liu W , Shi X , Yang Y , Cheng X , Liu Q , Han H , Yang B , He C , Wang Y , Jiang B , Wang Z , Wang C
Ref : PLoS ONE , 10 :e0122366 , 2015
Abstract : Vasicine (VAS), a potential natural cholinesterase inhibitor, exhibited promising anticholinesterase activity in preclinical models and has been in development for treatment of Alzheimer's disease. This study systematically investigated the in vitro and in vivo metabolism of VAS in rat using ultra performance liquid chromatography combined with electrospray ionization quadrupole time-of-flight mass spectrometry. A total of 72 metabolites were found based on a detailed analysis of their 1H- NMR and 13C NMR data. Six key metabolites were isolated from rat urine and elucidated as vasicinone, vasicinol, vasicinolone, 1,2,3,9-tetrahydropyrrolo [2,1-b] quinazolin-3-yl hydrogen sulfate, 9-oxo-1,2,3,9-tetrahydropyrrolo [2,1-b] quinazolin-3-yl hydrogen sulfate, and 1,2,3,9-tetrahydropyrrolo [2,1-b] quinazolin-3-beta-D-glucuronide. The metabolic pathway of VAS in vivo and in vitro mainly involved monohydroxylation, dihydroxylation, trihydroxylation, oxidation, desaturation, sulfation, and glucuronidation. The main metabolic soft spots in the chemical structure of VAS were the 3-hydroxyl group and the C-9 site. All 72 metabolites were found in the urine sample, and 15, 25, 45, 18, and 11 metabolites were identified from rat feces, plasma, bile, rat liver microsomes, and rat primary hepatocyte incubations, respectively. Results indicated that renal clearance was the major excretion pathway of VAS. The acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) inhibitory activities of VAS and its main metabolites were also evaluated. The results indicated that although most metabolites maintained potential inhibitory activity against AChE and BChE, but weaker than that of VAS. VAS undergoes metabolic inactivation process in vivo in respect to cholinesterase inhibitory activity.
ESTHER : Liu_2015_PLoS.One_10_e0122366
PubMedSearch : Liu_2015_PLoS.One_10_e0122366
PubMedID: 25849329

Title : Identification of candidate odorant receptors in Asian corn borer Ostrinia furnacalis - Yang_2015_PLoS.One_10_e0121261
Author(s) : Yang B , Ozaki K , Ishikawa Y , Matsuo T
Ref : PLoS ONE , 10 :e0121261 , 2015
Abstract : In lepidopteran insects, odorant receptors are involved in the perception of sex pheromones and general odorants. In the Asian corn borer, Ostrinia furnacalis, although several pheromone receptors have been identified, no general odorant receptor has been reported. In this study, an RNA sequencing analysis was carried out to identify the whole repertoire of the odorant receptors expressed in the antennae of O. furnacalis. Among 12 million reads obtained from the antennae of male and female moths, 52 candidate odorant receptors were identified, including 45 novel ones. Expression levels of candidate odorant receptors were estimated by read mapping and quantitative reverse transcription PCR. These analyses confirmed that the expression of the previously identified pheromone receptors was highly male biased. In contrast, none of the newly identified odorant receptors showed male-biased expression. Three of the newly identified odorant receptors showed female-biased expression. Two of them were the most highly expressed odorant receptors in the female antennae, suggesting that they may be involved in the detection of odorants important for the induction of female-specific behaviors such as oviposition site selection. In addition, candidate genes of 21 ionotropic receptors, 5 gustatory receptors, 2 sensory neuron membrane proteins, and 26 odorant degrading enzymes were identified. Our results provide a basis for further analysis of the chemosensory system in the Ostrinia species.
ESTHER : Yang_2015_PLoS.One_10_e0121261
PubMedSearch : Yang_2015_PLoS.One_10_e0121261
PubMedID: 25803580
Gene_locus related to this paper: ostfu-a0a0f7qea8 , ostfu-a0a0f7qeb1 , ostfu-a0a0f7qec9 , ostfu-a0a0f7qee1 , ostfu-a0a0f7qee5 , ostfu-a0a0f7qhk9 , ostfu-a0a0f7qhl7 , ostfu-a0a0f7qhl9 , ostfu-a0a0f7qie8 , ostfu-a0a0f7qif1 , ostfu-a0a0f7qif3 , ostfu-a0a0f7qjw7 , ostfu-a0a0f7qjx1 , ostfu-a0a0f7qjy8

Title : Fatty acid specificity of T1 lipase and its potential in acylglycerol synthesis - Qin_2014_J.Sci.Food.Agric_94_1614
Author(s) : Qin XL , Lan DM , Zhong JF , Liu L , Wang YH , Yang B
Ref : J Sci Food Agric , 94 :1614 , 2014
Abstract : BACKGROUND: T1 lipase has received considerable attention due to its thermostability. Fatty acid specificity of T1 lipase (crude and purified) was investigated, and its potential in the synthesis of acylglycerols was also evaluated.
RESULTS: Fatty acid specificity of T1 lipase (crude and purified) was investigated in the esterification of fatty acids (C6:0 to C18:3), suggesting that crude and purified T1 lipase had the lowest preference for C18:0 [specificity constant (1/alpha) = 0.08] followed by C18:1 (1/alpha = 0.12) and showed the highest preference for C8:0 (1/alpha = 1). A structural model was constructed to briefly explore interactions between the lipase and its substrate. Furthermore, crude T1 lipase-catalysed synthesis of diacylglycerols (DAGs) and monoacylglycerols (MAGs) by esterification of glycerol with C18:1 was studied for evaluating its potential in acylglycerols synthesis. The optimal conditions were glycerol/oleic acid molar ratio 5:1, the lipase concentration 9.7 U g(-1) of substrates, water content 50 g kg(-1) of substrates and temperature 50 degrees C, which yielded 42.25% DAGs, 26.34% MAGs and 9.18% triacylglycerols at 2 h. CONCLUSION: DAGs and MAGs were synthesised in good yields although C18:1 (a much poorer substrate) was used. Our work demonstrates that T1 lipase, which was discovered to show 1,3-regio-selectivity, is a promising biocatalyst for lipids modification.
ESTHER : Qin_2014_J.Sci.Food.Agric_94_1614
PubMedSearch : Qin_2014_J.Sci.Food.Agric_94_1614
PubMedID: 24338705
Gene_locus related to this paper: bacsp-lip

Title : Functional study on the mutations in the silkworm (Bombyx mori) acetylcholinesterase type 1 gene (ace1) and its recombinant proteins - Wang_2014_Mol.Biol.Rep_41_429
Author(s) : Wang JM , Wang BB , Xie Y , Sun SS , Gu ZY , Ma L , Li FC , Zhao YF , Yang B , Shen WD , Li B
Ref : Mol Biol Rep , 41 :429 , 2014
Abstract : The acetylcholinesterase of Lepidoptera insects is encoded by two genes, ace1 and ace2. The expression of the ace1 gene is significantly higher than that of the ace2 gene, and mutations in ace1 are one of the major reasons for pesticide resistance in insects. In order to investigate the effects of the mutations in ace1's characteristic sites on pesticide resistance, we generated mutations for three amino acids using site-directed mutagenesis, which were Ala(GCG)303Ser(TCG), Gly(GGA)329Ala(GCA) and Leu (TCT)554Ser(TTC). The Baculovirus expression system was used for the eukaryotic expression of the wild type ace1 (wace1) and the mutant ace1 (mace1). SDS-PAGE and Western blotting were used to detect the targeting proteins with expected sizeof about 76 kDa. The expression products were purified for the determination of AChE activity and the inhibitory effects of physostigmine and phoxim. We observed no significant differences in the overall activity of the wild type and mutant AChEs. However, with 10 min of physostigmine (10 muM) inhibition, the remaining activity of the wild type AChE was significantly lower than that of the mutant AChE. Ten min inhibition with 33.4 muM phoxim also resulted in significantly lower remaining activity of the wild type AChE than that of the mutant AChE. These results indicated that mutations for the three amino acids reduced the sensitivity of AChE to physostigmine and phoxim, which laid the foundation for future in vivo studies on AChE's roles in pesticide resistance.
ESTHER : Wang_2014_Mol.Biol.Rep_41_429
PubMedSearch : Wang_2014_Mol.Biol.Rep_41_429
PubMedID: 24323194
Gene_locus related to this paper: bommo-ACHE1

Title : Site-directed mutagenesis studies of the aromatic residues at the active site of a lipase from Malassezia globosa - Gao_2014_Biochimie_102_29
Author(s) : Gao C , Lan D , Liu L , Zhang H , Yang B , Wang Y
Ref : Biochimie , 102 :29 , 2014
Abstract : The lipase from Malassezia globosa (SMG1) has specific activity on mono- and diacylglycerol but not on triacylglycerol. The structural analysis of SMG1 structure shows that two bulky aromatic residues, W116 and W229, lie at the entrance of the active site. To study the functions of these two residues in the substrate recognition and the catalytic reaction, they were mutated to a series of amino acids. Subsequently, biochemical properties of these mutants were investigated. Although the activities decrease, W229L and W116A show a significant shift in substrate preference. W229L has an increased preference for short-chain substrates whereas W116A has preference for long-chain substrates. Besides, the half-lives of W116A and W116H at 45 degrees C are 346.6 min and 115.5 min respectively, which improve significantly compared to that of native enzyme. Moreover, the optimum substrate of W116A, W116F and W229F mutants shifted from p-nitrophenyl caprylate to p-nitrophenyl myristate. These findings not only shed light onto the lipase structure/function relationship but also lay the framework for the potential industrial applications.
ESTHER : Gao_2014_Biochimie_102_29
PubMedSearch : Gao_2014_Biochimie_102_29
PubMedID: 24556587
Gene_locus related to this paper: malgo-a8puy1

Title : Enhanced therapeutic efficacy of combined use of sorafenib and transcatheter arterial chemoembolization for treatment of advanced hepatocellular carcinoma - Zhou_2014_Jpn.J.Clin.Oncol_44_711
Author(s) : Zhou L , Li J , Ai DL , Fu JL , Peng XM , Zhang LZ , Wang JY , Zhao Y , Yang B , Yu Q , Liu CZ , Wang HM
Ref : Japanese Journal of Clinical Oncology , 44 :711 , 2014
Abstract : OBJECTIVE: Clinical trials suggest that combining transcatheter arterial chemoembolization with sorafenib in patients with advanced hepatocellular carcinoma shows a superior safety and tolerability profile. Our study aimed to retrospectively analyze the utility and prognostic factors of this combined therapy in these patients.
METHODS: Patients with advanced hepatocellular carcinoma, treated by transcatheter arterial chemoembolization and sorafenib subsequently, between February 2010 and September 2012 in our hospital, were retrospectively analyzed. After sorafenib treatment for 12 weeks, abdominal enhanced computed tomography or magnetic resonance imaging was used to evaluate short-term outcomes and clinical benefit rate. Overall survival and adverse events were recorded during follow-up. Univariate and multivariate analyses were used to identify relationships between baseline characteristics and overall survival.
RESULTS: Fifty-one advanced hepatocellular carcinoma patients were included. Common adverse events for sorafenib were hand-foot skin reaction, alopecia, diarrhea, anorexia and fatigue. The clinical benefit rate was 64% and the median survival time was 7.5 months. Median survival of patients with and without portal vein tumor thrombi was 6.0 months and 10.3 months (P < 0.001), respectively. Median survival of patients with cholinesterase >/=5000 U/l and < 5000 U/l was 10.6 months and 6.1 months (P < 0.001), respectively. Multivariate analysis identified the presence of portal vein tumor thrombi and low cholinesterase level as independent negative predictors of survival.
CONCLUSIONS: Combining sorafenib and transcatheter arterial chemoembolization was safe and effective for advanced hepatocellular carcinoma patients with extrahepatic spread but without portal vein tumor thrombi. Portal vein tumor thrombi and cholinesterase level are independent predictors of prognosis following this combined therapy.
ESTHER : Zhou_2014_Jpn.J.Clin.Oncol_44_711
PubMedSearch : Zhou_2014_Jpn.J.Clin.Oncol_44_711
PubMedID: 24855686

Title : Biochemical properties of a new cold-active mono- and diacylglycerol lipase from marine member Janibacter sp. strain HTCC2649 - Yuan_2014_Int.J.Mol.Sci_15_10554
Author(s) : Yuan D , Lan D , Xin R , Yang B , Wang Y
Ref : Int J Mol Sci , 15 :10554 , 2014
Abstract : Mono- and di-acylglycerol lipase has been applied to industrial usage in oil modification for its special substrate selectivity. Until now, the reported mono- and di-acylglycerol lipases from microorganism are limited, and there is no report on the mono- and di-acylglycerol lipase from bacteria. A predicted lipase (named MAJ1) from marine Janibacter sp. strain HTCC2649 was purified and biochemical characterized. MAJ1 was clustered in the family I.7 of esterase/lipase. The optimum activity of the purified MAJ1 occurred at pH 7.0 and 30 degrees C. The enzyme retained 50% of the optimum activity at 5 degrees C, indicating that MAJ1 is a cold-active lipase. The enzyme activity was stable in the presence of various metal ions, and inhibited in EDTA. MAJ1 was resistant to detergents. MAJ1 preferentially hydrolyzed mono- and di-acylglycerols, but did not show activity to triacylglycerols of camellia oil substrates. Further, MAJ1 is low homologous to that of the reported fungal diacylglycerol lipases, including Malassezia globosa lipase 1 (SMG1), Penicillium camembertii lipase U-150 (PCL), and Aspergillus oryzae lipase (AOL). Thus, we identified a novel cold-active bacterial lipase with a sn-1/3 preference towards mono- and di-acylglycerides for the first time. Moreover, it has the potential, in oil modification, for special substrate selectivity.
ESTHER : Yuan_2014_Int.J.Mol.Sci_15_10554
PubMedSearch : Yuan_2014_Int.J.Mol.Sci_15_10554
PubMedID: 24927145
Gene_locus related to this paper: 9mico-a3tmr7

Title : Association of polymorphisms in prolylcarboxypeptidase and chymase genes with essential hypertension in the Chinese Han population - Wu_2013_J.Renin.Angiotensin.Aldosterone.Syst_14_263
Author(s) : Wu Y , Yang H , Yang B , Yang K , Xiao C
Ref : J Renin Angiotensin Aldosterone Syst , 14 :263 , 2013
Abstract : INTRODUCTION: The prolylcarboxypeptidase (PRCP) gene encodes a membrane protein that acts on angiotensin II (Ang II) and kallikrein to release vasoactive peptides. The chymase (CMA1) gene is important for Ang II generation. Therefore, the two genes might be involved in the pathogenesis of essential hypertension (EH). MATERIALS AND METHODS: Eleven tag single nucleotide polymorphisms (SNPs) in the PRCP gene and four tag SNPs and G-1903A (rs1800875) polymorphism in the CMA1 gene were genotyped in the Chinese Han population (n=1020) using a polymerase chain reaction-restriction fragment length polymorphism method. RESULTS: In the PRCP gene, single site analyses indicated that the rs7104980 G allele was a susceptible factor for EH (adjusted odds ratio (OR)=1.98, 95% confidence interval (CI) 1.62-2.43, p=0.3x10(-10)). The protective effect of Hap3 GAGCACTAACA was observed without carrying the susceptible rs7104908 G allele (OR=0.67, 95% CI 0.56-0.81, p=0.3x10(-4)) by haplotype analyses. In the case of the CMA1 gene, no associations with EH were found through single site analyses. However, haplotype analyses showed that Hap16 TTTA significantly increased the risk of EH with OR=3.15 (p=0.0002) which may be driven by interaction with a nearby SNP combination. CONCLUSIONS: The present results indicated PRCP rs7104980 can be considered as a marker for EH and Hap3 GAGCACTAACA (PRCP) and Hap16 TTTA (CMA1) might be associated with EH in Chinese Han population.
ESTHER : Wu_2013_J.Renin.Angiotensin.Aldosterone.Syst_14_263
PubMedSearch : Wu_2013_J.Renin.Angiotensin.Aldosterone.Syst_14_263
PubMedID: 22679278
Gene_locus related to this paper: human-PRCP

Title : Enzymatic synthesis of extremely pure triacylglycerols enriched in conjugated linoleic acids - Cao_2013_Molecules_18_9704
Author(s) : Cao Y , Wang W , Xu Y , Yang B , Wang Y
Ref : Molecules , 18 :9704 , 2013
Abstract : This work was objectively targeted to synthesize extremely pure triacylglycerols (TAG) enriched in conjugated linoleic acids (CLAs) for medical and dietetic purposes. Extremely pure CLA-enriched TAG was successfully synthesized by using the multi-step process: TAG was primarily synthesized by lipase-catalyzed esterification of CLA and glycerol and then the lower glycerides [monoacylglycerol (MAG) and diacylglycerol (DAG)] in the esterification mixtures was hydrolyzed to free fatty acids (FFAs) by a mono- and di-acylglycerol lipase (lipase SMG1), finally, the FFAs were further separated from TAG by low temperature (150 degreesC) molecular distillation. The operation parameters for the lipase SMG1-catalyzed hydrolysis were optimized using response surface methodology based on the central composite rotatable design (CCRD). The operation parameters included water content, pH and reaction temperature and all of these three parameters showed significant effects on the hydrolysis of lower glycerides. The optimal conditions were obtained with a water content of 66.4% (w/w, with respect to oil mass), pH at 5.7 and 1 h of reaction time at 19.6 degreesC. Under these conditions, the content of lower glycerides in the reaction mixture decreased from 45.2% to 0.3% and the purity of CLA-enriched TAG reached 99.7%. Further purification of TAG was accomplished by molecular distillation and the final CLA-enriched TAG product yielded 99.8% of TAG. These extremely pure CLA-enriched TAG would be used for in vivo studies in animals and humans in order to get specic information concerning CLA metabolism.
ESTHER : Cao_2013_Molecules_18_9704
PubMedSearch : Cao_2013_Molecules_18_9704
PubMedID: 23945644

Title : Synthesis of structured lipids by lipase-catalyzed interesterification of triacetin with camellia oil methyl esters and preliminary evaluation of their plasma lipid-lowering effect in mice - Cao_2013_Molecules_18_3733
Author(s) : Cao Y , Qi S , Zhang Y , Wang X , Yang B , Wang Y
Ref : Molecules , 18 :3733 , 2013
Abstract : Structured lipids (SLCTs triacylglycerols with short- and long-chain acyl residues) were synthesized by interesterification of triacetin and fatty acid methyl esters (FAMEs) from camellia oil, followed by molecular distillation for purification. Different commercial immobilized lipases (Lipozyme RM IM and Novozyme 435), the substrate molar ratios of FAMEs to triacetin, the reaction temperatures and the lipase amounts were studied for their efficiency in producing SLCTs. Results showed that Novozyme 435 was more suitable for this reaction system. Moreover, the optimal reaction conditions for the highest conversion of FAMEs and the highest LLS-TAGs (triacylglycerols with one short- and two long-chain acyl residues) yields were achieved at a molar ratio of FAMEs to triacetin of 3:1, 50 degreeC of reaction temperature and a lipase amount of 4% (w/v). Scale-up was conducted based on the optimized reaction conditions. Results showed that after 24 h of reaction , the conversion rate of FAMEs was 82.4% and the rate of disubstituted triacetin was 52.4 mol%. The final product yield rate was 94.6%. The effects of the synthesized SLCTs on the plasma lipid level of fasting mice were also studied. The SLCTs could effectively lessen the total triacylglycerol levels in plasma compared to the triacylglycerol group in fasting NIH mice. It suggested that this type of structured lipid might be beneficial for human health, especially for the prevention of obesity.
ESTHER : Cao_2013_Molecules_18_3733
PubMedSearch : Cao_2013_Molecules_18_3733
PubMedID: 23529033

Title : Crystal structure of a mono- and diacylglycerol lipase from Malassezia globosa reveals a novel lid conformation and insights into the substrate specificity - Xu_2012_J.Struct.Biol_178_363
Author(s) : Xu T , Liu L , Hou S , Xu J , Yang B , Wang Y , Liu J
Ref : J Struct Biol , 178 :363 , 2012
Abstract : Most lipases contain a lid domain to shield the hydrophobic binding site from the water environment. The lid, mostly in helical form, can undergo a conformational change to expose the active cleft during the interfacial activation. Here we report the crystal structures of Malassezia globosa LIP1 (SMG1) at 1.45 and 2.60 resolution in two crystal forms. The structures present SMG1 in its closed form, with a novel lid in loop conformation. SMG1 is one of the few members in the fungal lipase family that has been found to be strictly specific for mono- and diacylglycerol. To date, the mechanism for this substrate specificity remains largely unknown. To investigate the substrate binding properties, we built a model of SMG1 in open conformation. Based on this model, we found that the two bulky hydrophobic residues adjacent to the catalytic site and the N-terminal hinge region of the lid both may act as steric hindrances for triacylglycerols binding. These unique structural features of SMG1 will provide a better understanding on the substrate specificity of mono- and diacylglycerol lipases and a platform for further functional study of this enzyme.
ESTHER : Xu_2012_J.Struct.Biol_178_363
PubMedSearch : Xu_2012_J.Struct.Biol_178_363
PubMedID: 22484238
Gene_locus related to this paper: malgo-a8puy1

Title : Lipase-catalyzed incorporation of different Fatty acids into tripalmitin-enriched triacylglycerols: effect of reaction parameters - Qin_2012_J.Agric.Food.Chem_60_2377
Author(s) : Qin XL , Yang B , Huang HH , Wang YH
Ref : Journal of Agricultural and Food Chemistry , 60 :2377 , 2012
Abstract : Tripalmitin-enriched triacylglycerols were concentrated from palm stearin by acetone fractionation and as the substrate reacted with a mixture of equimolar quantities of fatty acids (C8:0-C18:3). The incorporation degree and acyl migration level of the fatty acids and acylglycerols composition were investigated, providing helpful information for the production of human milk fat substitutes. Higher incorporation degrees of the fatty acids were obtained with lipase PS IM, Lipozyme TL IM, and Lipozyme RM IM followed by porcine pancreatic lipase and Novozym 435-catalyzed acidolysis. During reactions catalyzed by Lipozyme TL IM, Lipozyme RM IM, and lipase PS IM, incorporation degrees of C12:0, C14:0, C18:1, and C18:2 were higher than those of other fatty acids at operated variables (molar ratio, temperature, and time), and the triacylglycerols content reached the highest (82.09%) via Lipozyme RM IM-catalyzed acidolysis. On the basis of significantly different levels of acyl migration to the sn-2 position, lipases were in the order of lipase PS IM < Lipozyme TL IM < Lipozyme RM IM.
ESTHER : Qin_2012_J.Agric.Food.Chem_60_2377
PubMedSearch : Qin_2012_J.Agric.Food.Chem_60_2377
PubMedID: 22360498

Title : Molecular basis for substrate selectivity of a mono- and diacylglycerol lipase from Malassezia globosa - Liu_2012_Biochem.Biophys.Res.Commun_424_285
Author(s) : Liu L , Gao C , Lan D , Yang B , Wang Y
Ref : Biochemical & Biophysical Research Communications , 424 :285 , 2012
Abstract : The lipase from Malassezia globosa (SMG1) was identified to be strictly specific for mono- and diacylglycerol but not triacylglycerol. The crystal structures of SMG1 were solved in the closed conformation, but they failed to provide direct evidence of factors responsible for this unique selectivity. To address this problem, we constructed a structure in the open, active conformation and modeled a diacylglycerol analogue into the active site. Molecular dynamics simulations were performed on this enzyme-analogue complex to relax steric clashes. This bound diacylglycerol analogue unambiguously identified the position of two pockets which accommodated two alkyl chains of substrate. The structure of SMG1-analogue complex revealed that Leu103 and Phe278 divided the catalytic pocket into two separated moieties, an exposed groove and a narrow tunnel. Analysis of the binding model suggested that the unique selectivity of this lipase mainly resulted from the shape and size of this narrow tunnel, in which there was no space for the settlement of the third chain of triacylglycerol. These results expand our understanding on the mechanism underlying substrate selectivity of enzyme, and could pave the way for site-directed mutagenesis experiments to improve the enzyme for application.
ESTHER : Liu_2012_Biochem.Biophys.Res.Commun_424_285
PubMedSearch : Liu_2012_Biochem.Biophys.Res.Commun_424_285
PubMedID: 22750000
Gene_locus related to this paper: malgo-a8puy1

Title : Draft genome sequence of pigeonpea (Cajanus cajan), an orphan legume crop of resource-poor farmers - Varshney_2011_Nat.Biotechnol_30_83
Author(s) : Varshney RK , Chen W , Li Y , Bharti AK , Saxena RK , Schlueter JA , Donoghue MT , Azam S , Fan G , Whaley AM , Farmer AD , Sheridan J , Iwata A , Tuteja R , Penmetsa RV , Wu W , Upadhyaya HD , Yang SP , Shah T , Saxena KB , Michael T , McCombie WR , Yang B , Zhang G , Yang H , Wang J , Spillane C , Cook DR , May GD , Xu X , Jackson SA
Ref : Nat Biotechnol , 30 :83 , 2011
Abstract : Pigeonpea is an important legume food crop grown primarily by smallholder farmers in many semi-arid tropical regions of the world. We used the Illumina next-generation sequencing platform to generate 237.2 Gb of sequence, which along with Sanger-based bacterial artificial chromosome end sequences and a genetic map, we assembled into scaffolds representing 72.7% (605.78 Mb) of the 833.07 Mb pigeonpea genome. Genome analysis predicted 48,680 genes for pigeonpea and also showed the potential role that certain gene families, for example, drought tolerance-related genes, have played throughout the domestication of pigeonpea and the evolution of its ancestors. Although we found a few segmental duplication events, we did not observe the recent genome-wide duplication events observed in soybean. This reference genome sequence will facilitate the identification of the genetic basis of agronomically important traits, and accelerate the development of improved pigeonpea varieties that could improve food security in many developing countries.
ESTHER : Varshney_2011_Nat.Biotechnol_30_83
PubMedSearch : Varshney_2011_Nat.Biotechnol_30_83
PubMedID: 22057054
Gene_locus related to this paper: cajca-a0a151r9d2 , cajca-a0a151u2m0 , cajca-a0a151tes0 , cajca-a0a151u784 , cajca-a0a151sf79 , cajca-a0a151qu18 , cajca-a0a151sz37 , cajca-a0a151ss18 , cajca-a0a151rb44 , cajca-a0a151ryr0 , cajca-a0a151qzm6 , cajca-a0a151rsm6 , cajca-a0a151rsn1 , cajca-a0a151tig2 , cajca-a0a151rwt3 , cajca-a0a151rx08 , cajca-a0a151rws4 , cajca-a0a151r0b7

Title : Optimal production and biochemical properties of a lipase from Candida albicans - Lan_2011_Int.J.Mol.Sci_12_7216
Author(s) : Lan D , Hou S , Yang N , Whiteley C , Yang B , Wang Y
Ref : Int J Mol Sci , 12 :7216 , 2011
Abstract : Lipases from microorganisms have multi-faceted properties and play an important role in ever-growing modern biotechnology and, consequently, it is of great significance to develop new ones. In the present work, a lipase gene from Candida albicans (CaLIP10) was cloned and two non-unusual CUG serine codons were mutated into universal codons, and its expression in Pichia pastoris performed optimally, as shown by response surface methodology. Optimal conditions were: initial pH of culture 6.86, temperature 25.53 degrees C, 3.48% of glucose and 1.32% of yeast extract. The corresponding maximal lipolytic activity of CaLIP10 was 8.06 U/mL. The purified CaLIP10 showed maximal activity at pH 8.0 and 25 degrees C, and a good resistance to non-ionic surfactants and polar organic solvent was noticed. CaLIP10 could effectively hydrolyze coconut oil, but exhibited no obvious preference to the fatty acids with different carbon length, and diacylglycerol was accumulated in the reaction products, suggesting that CaLIP10 is a potential lipase for the oil industry.
ESTHER : Lan_2011_Int.J.Mol.Sci_12_7216
PubMedSearch : Lan_2011_Int.J.Mol.Sci_12_7216
PubMedID: 22072943

Title : A novel cold-active lipase from Candida albicans: cloning, expression and characterization of the recombinant enzyme - Lan_2011_Int.J.Mol.Sci_12_3950
Author(s) : Lan DM , Yang N , Wang WK , Shen YF , Yang B , Wang YH
Ref : Int J Mol Sci , 12 :3950 , 2011
Abstract : A novel lipase gene lip5 from the yeast Candida albicans was cloned and sequenced. Alignment of amino acid sequences revealed that 86-34% identity exists with lipases from other Candida species. The lipase and its mutants were expressed in the yeast Pichia pastoris, where alternative codon usage caused the mistranslation of 154-Ser and 293-Ser as leucine. 154-Ser to leucine resulted in loss of expression of Lip5, and 293-Ser to leucine caused a marked reduction in the lipase activity. Lip5-DM, which has double mutations that revert 154 and 293 to serine residues, showed good lipase activity, and was overexpressed and purified by (NH(4))(2)SO(4) precipitation and ion-exchange chromatography. The pure Lip5-DM was stable at low temperatures ranging from 15-35 degrees C and pH 5-9, with the optimal conditions being 15-25 degrees C and pH 5-6. The activation energy of recombinant lipase was 8.5 Kcal/mol between 5 and 25 degrees C, suggesting that Lip5-DM was a cold-active lipase. Its activity was found to increase in the presence of Zn(2+), but it was strongly inhibited by Fe(2+), Fe(3+), Hg(2+) and some surfactants. In addition, the Lip5-DM could not tolerate water-miscible organic solvents. Lip5-DM exhibited a preference for the short-and medium-chain length p-nitrophenyl (C4 and C8 acyl group) esters rather than the long chain length p-nitrophenyl esters (C12, C16 and C18 acyl group) with highest activity observed with the C8 derivatives. The recombinant enzyme displayed activity toward triacylglycerols, such as olive oil and safflower oil.
ESTHER : Lan_2011_Int.J.Mol.Sci_12_3950
PubMedSearch : Lan_2011_Int.J.Mol.Sci_12_3950
PubMedID: 21747717
Gene_locus related to this paper: canal-LIP5

Title : Preparation and characterization of 1,3-dioleoyl-2-palmitoylglycerol - Qin_2011_J.Agric.Food.Chem_59_5714
Author(s) : Qin XL , Wang YM , Wang YH , Huang HH , Yang B
Ref : Journal of Agricultural and Food Chemistry , 59 :5714 , 2011
Abstract : 1,3-Dioleoyl-2-palmitoylglycerol, an important triacylglycerol in infant formulas, was effectively enriched by a two-step process: (a) dry fractionation of leaf lard and (b) enzymatic acidolysis of the fractionated leaf lard. In step a, the 1,3-dioleoyl-2-palmitoylglycerol content was increased from 16.77 to 30.73% after programmed temperature treatment of the leaf lard at 60 degreeC for 20 min followed by 34 degreeC for 10 h. In step b, 43.72% of the 1,3-dioleoyl-2-palmitoylglycerol content was obtained at the optimal conditions of enzymatic acidolysis: a substrate molar ratio of 1:4 (the fractionated leaf lard/camellia oil fatty acids), 6% (w/w) of enzyme loading, and 6 h of reaction time at 45 degreeC. On the basis of gas chromatography determination and "deducting score" principle, a model was properly established for characterizing the quality of triacylglycerols enriched with 1,3-dioleoyl-2-palmitoylglycerol. This approach would be a valuable contribution in structured lipids industries because only gas chromatography determination was involved.
ESTHER : Qin_2011_J.Agric.Food.Chem_59_5714
PubMedSearch : Qin_2011_J.Agric.Food.Chem_59_5714
PubMedID: 21510711

Title : Complete genome sequence of Staphylococcus aureus T0131, an ST239-MRSA-SCCmec type III clone isolated in China - Li_2011_J.Bacteriol_193_3411
Author(s) : Li Y , Cao B , Zhang Y , Zhou J , Yang B , Wang L
Ref : Journal of Bacteriology , 193 :3411 , 2011
Abstract : We report here the complete genome sequence of Staphylococcus aureus T0131, which is a multiresistant clinical isolate recovered in China and the first sequenced epidemic ST239-MRSA-SCCmec type III strain obtained in Asia. Comparison with two published genomes of ST239 reveals the polymorphism among strains of this type from different continents.
ESTHER : Li_2011_J.Bacteriol_193_3411
PubMedSearch : Li_2011_J.Bacteriol_193_3411
PubMedID: 21551295
Gene_locus related to this paper: staau-SA0897

Title : Bioequivalence evaluation of two brands of rivastigmine of different salt forms, an acetylcholinesterase inhibitor for the treatment of Alzheimer's disease, in healthy Beagle dogs - Shen_2011_Pharmazie_66_590
Author(s) : Shen C , Yang B , Zhou T , Duan G , Yu Y
Ref : Pharmazie , 66 :590 , 2011
Abstract : The bioequivalence of two brands of rivastigmine capsules, of different salt forms, was demonstrated in six healthy beagle dogs after a single oral dose in a randomized cross-over study. Reference (Rivastigmine hydrochloride, Sunve, CN) and test (Rivastigmine tartrate, Novartis, CH) products were administered to fasting beagles on two treatment days separated by a two-day washout period; blood samples were collected at specified time intervals, and the plasma was separated and analyzed for rivastigmine using a validated GC-MS method. The pharmacokinetic parameters AUC(0-t), AUC(0-infinity), C(max), T(max) and t1/2 were compared statistically to evaluate bioequivalence between the two brands, using the statistical modules recommended by the State Food and Drug Administration (SFDA) of China. The analysis of variance (ANOVA) did not show any significant difference between the two formulations and 90% confidence intervals fell within the acceptable ranges for bioequivalence. Based on these statistical inferences it was concluded that the two brands exhibited comparable pharmacokinetic profiles and that Sanwei's Rivastigmine hydrochloride was bioequivalent to Rivastigmine tartrate of Novartis, CH.
ESTHER : Shen_2011_Pharmazie_66_590
PubMedSearch : Shen_2011_Pharmazie_66_590
PubMedID: 21901981

Title : Production of extremely pure diacylglycerol from soybean oil by lipase-catalyzed glycerolysis - Wang_2011_Enzyme.Microb.Technol_49_192
Author(s) : Wang W , Li T , Ning Z , Wang Y , Yang B , Yang X
Ref : Enzyme Microb Technol , 49 :192 , 2011
Abstract : Research work was objectively targeted to synthesize highly pure diacylglycerol (DAG) with glycerolysis of soybean oil in a solvent medium of t-butanol. Three commercial immobilized lipases (Lipozyme RM IM, Lipozyme TL IM and Novozym 435) were screened, and Novozym 435 was the best out of three candidates. Batch reaction conditions of the enzymatic glycerolysis, the substrate mass ratio, the reaction temperature and the substrate concentration, were studied. The optimal reaction conditions were achieved as 6.23:1 mass ratio of soybean oil to glycerol, 40% (w/v) of substrate concentration in t-butanol and reaction temperature of 50 degreeC. A two-stage molecular distillation was employed for purification of DAG from reaction products. Scale-up was attempted based on the optimized reaction conditions, 98.7% (24 h) for the conversion rate of soybean oil, 48.5% of DAG in the glycerolysis products and 96.1% for the content of DAG in the final products were taken in account as the results.
ESTHER : Wang_2011_Enzyme.Microb.Technol_49_192
PubMedSearch : Wang_2011_Enzyme.Microb.Technol_49_192
PubMedID: 22112408

Title : Brominated aliphatic hydrocarbons and sterols from the sponge Xestospongia testudinaria with their bioactivities - Zhou_2011_Chem.Phys.Lipids_164_703
Author(s) : Zhou X , Lu Y , Lin X , Yang B , Yang X , Liu Y
Ref : Chemistry & Physic of Lipids , 164 :703 , 2011
Abstract : Four brominated aliphatic hydrocarbons (1-4), including a novel brominated ene-tetrahydrofuran named as mutafuran H (1), and five sterols (5-9) were isolated from the South China Sea sponge Xestospongia testudinaria. The structure of 1 was determined on the basis of NMR ((1)H, (13)C NMR, HSQC, HMBC, (1)H-(1)H COSY, and NOESY), MS, and optical rotation analysis. Known compounds were identified by comparison of their NMR data with those reported in the literature. Compounds 1-4, and 6-9 were evaluated for their toxicity against Artemia salina larvae, and anti-acetylcholinesterase activity.
ESTHER : Zhou_2011_Chem.Phys.Lipids_164_703
PubMedSearch : Zhou_2011_Chem.Phys.Lipids_164_703
PubMedID: 21864515

Title : Computational determination of binding structures and free energies of phosphodiesterase-2 with benzo[1,4]diazepin-2-one derivatives - Yang_2010_J.Phys.Chem.B_114_16020
Author(s) : Yang B , Hamza A , Chen G , Wang Y , Zhan CG
Ref : J Phys Chem B , 114 :16020 , 2010
Abstract : Phosphodiesterase-2 (PDE2) is a key enzyme catalyzing hydrolysis of both cyclic adenosine monophosphate (cAMP) and cyclic guanosine monophosphate (cGMP) that serve as intracellular second messengers. PDE2 has been recognized as an attractive drug target, and selective inhibitors of PDE2 are expected to be promising candidates for the memory enhancer, antidepressant, and anxiolytic agent. In the present study, we examined the detailed binding structures and free energies for PDE2 interacting with a promising series of inhibitors, i.e., benzo[1,4]diazepin-2-one derivatives, by carrying out molecular docking, molecular dynamics (MD) simulations, binding free energy calculations, and binding energy decompositions. The computational results provide valuable insights into the detailed enzyme-inhibitor binding modes including important intermolecular interactions, e.g., the pi-pi stacking interactions with the common benzo[1,4]diazepin-2-one scaffold of the inhibitors, hydrogen bonding and hydrophobic interactions with the substituents on the benzo[1,4]diazepin-2-one scaffold. Future rational design of new, more potent inhibitors of PDE2 should carefully account for all of these favorable intermolecular interactions. By use of the MD-simulated binding structures, the calculated binding free energies are in good agreement with the experimental activity data for all of the examined benzo[1,4]diazepin-2-one derivatives. The enzyme-inhibitor binding modes determined and the agreement between the calculated and experimental results are expected to be valuable for future rational design of more potent inhibitors of PDE2.
ESTHER : Yang_2010_J.Phys.Chem.B_114_16020
PubMedSearch : Yang_2010_J.Phys.Chem.B_114_16020
PubMedID: 21077589

Title : Wheat germ lipase catalyzed kinetic resolution of secondary alcohols in non-aqueous media - Xia_2009_Biotechnol.Lett_31_83
Author(s) : Xia X , Wang YH , Yang B , Wang X
Ref : Biotechnol Lett , 31 :83 , 2009
Abstract : The lipase from wheat germ was used for the kinetic resolution of secondary alcohols. It has the opposite enantioselectivity against the Kazlauskas rule and acts as an anti-Kazlauskas catalyst. The effect of initial water activity, organic solvent, acyl donor and temperature were investigated. Wheat germ lipase had a high activity and enantioselectivity only in n-hexane with a high initial water activity (alpha(w) = 0.97), especially with 1-phenylethanol (C 32%, E > 200). Its performance changed little with the chain length of acyl donor and temperature.
ESTHER : Xia_2009_Biotechnol.Lett_31_83
PubMedSearch : Xia_2009_Biotechnol.Lett_31_83
PubMedID: 18777014

Title : Design, synthesis and evaluation of galanthamine derivatives as acetylcholinesterase inhibitors - Jia_2009_Eur.J.Med.Chem_44_772
Author(s) : Jia P , Sheng R , Zhang J , Fang L , He Q , Yang B , Hu Y
Ref : Eur Journal of Medicinal Chemistry , 44 :772 , 2009
Abstract : A new series of galanthamine derivatives have been designed, synthesized and evaluated as acetylcholinesterase inhibitors. All of the new compounds prepared showed high AChE inhibitory activities, with compound 3e that has an N-hexyl-benzyl piperidine substituent on the nitrogen atom reaching the best inhibitory activity for AChE (IC(50)=5.62 nM). The docking study performed with AutoDock demonstrated that 3e was nicely accommodated by AChE.
ESTHER : Jia_2009_Eur.J.Med.Chem_44_772
PubMedSearch : Jia_2009_Eur.J.Med.Chem_44_772
PubMedID: 18550228

Title : Synthesis and biological evaluation of novel flavonoid derivatives as dual binding acetylcholinesterase inhibitors - Shen_2009_J.Enzyme.Inhib.Med.Chem_24_372
Author(s) : Shen Y , Zhang J , Sheng R , Dong X , He Q , Yang B , Hu Y
Ref : J Enzyme Inhib Med Chem , 24 :372 , 2009
Abstract : A new series of flavonoid derivatives have been designed, synthesised and evaluated as acetylcholinesterase inhibitors that could bind simultaneously to the peripheral and catalytic sites of the enzyme. Among them, fifteen derivatives were found to inhibit the enzyme in the micromolar range and isoflavone derivatives possessed more potent inhibitory activity than other flavonoid derivatives. The best compound 9a had its inhibitory activity (IC(50) = 0.093 microM) in the same range as the reference compound, donepezil (IC(50) = 0.025 microM). Preliminary structure-activity relationships and a molecular modeling study for 9a have revealed that the isoflavone moiety plays a key role in the interaction of this series of derivatives with AChE by acting as an anchor in its peripheral anionic site.
ESTHER : Shen_2009_J.Enzyme.Inhib.Med.Chem_24_372
PubMedSearch : Shen_2009_J.Enzyme.Inhib.Med.Chem_24_372
PubMedID: 18830885

Title : Water activity dependence of lipases in non-aqueous biocatalysis - Xia_2009_Appl.Biochem.Biotechnol_159_759
Author(s) : Xia X , Wang C , Yang B , Wang YH , Wang X
Ref : Appl Biochem Biotechnol , 159 :759 , 2009
Abstract : Eleven lipases are tested and it was found that lipases can be divided into three types according to water activity dependence. The first type is lipase that has low water activity dependence and works in a low water activity, its performance changes little with the change of water activity. The optimum water activity is 0.19 and Newlase F (Rhizopus niveus), lipase FAP-15 (Rhizopus oryzae) belong to this type. The second type is lipase that has medium water activity dependence and its performance changes with the change of water activity. Most lipases belong to this type and the optimum water activity in this type is about 0.60. The third type is lipase that has a high water activity dependence and works only in a high water activity (a ( w ) > 0.75). WGL (wheat germ) belongs to this type and the optimum water activity is 0.90. The relationship between enantioselectivity and water activity is also discussed and the enantioselectivity seems to be independent of water activity. And we also compared the two control methods of water activity, it was found that the method which add solid salt hydrates to the reaction mixture (method II) is more stable and effective throughout the reaction than the method that pre-equilibrate via the vapor phase (method I). The addition concentration of salt hydrates is also investigated and the optimum concentration is 1 g/l.
ESTHER : Xia_2009_Appl.Biochem.Biotechnol_159_759
PubMedSearch : Xia_2009_Appl.Biochem.Biotechnol_159_759
PubMedID: 19455434

Title : BZYX, a novel acetylcholinesterase inhibitor, significantly improved chemicals-induced learning and memory impairments on rodents and protected PC12 cells from apoptosis induced by hydrogen peroxide - Zhang_2009_Eur.J.Pharmacol_613_1
Author(s) : Zhang J , Zhu D , Sheng R , Wu H , Hu Y , Wang F , Cai T , Yang B , He Q
Ref : European Journal of Pharmacology , 613 :1 , 2009
Abstract : BZYX was designed as a dual-binding-site acetylcholinesterase (AChE) inhibitor and selected from series of indanone derivatives. The present study was designed to examine the cognition-enhanced, anti-cholinesterase, and neuroprotective effects of BZYX. In the passive avoidance performance and radial arm maze, BZYX showed a comparable effect to donepezil and rivastigmine on memory deficits in different stages induced by scopolamine, NaNO(2) and ethanol, respectively. Ellman's assay indicated BZYX exhibited high inhibition on AChE activity. IC(50) values for BZYX: 0.058+/-0.022 microM; donepezil: 0.019+/-0.004 microM; rivastigmine: 3.81+/-2.81 microM; glantamine: 3.01+/-1.85 microM and huperzine A: 0.053+/-0.016 microM. BZYX also presented great neuroprotecive function from apoptosis induced by hydrogen peroxide(H(2)O(2)) in PC12 cells. MTT assay and Annexin V-FITC Apoptosis Detection showed the viability of PC12 cells remarkably decreased with 400 microM H(2)O(2), while it significantly increased when the cells were pretreated with 0.1-1.0 microM BZYX. BZYX pretreatment remarkably reversed the loss of mitochondria membrane potential (DeltaPsim), scavenged reactive oxygen species formation induced by H(2)O(2) and resulted in up-regulation of procaspase3 and xIAP protein level and down-regulation of phosphorylated JNK protein, p53 protein level and cleavage of caspase 3. It is speculated that the mitochondrial pathway, mediated by Bcl-2 family and Mitogen-Activated Protein Kinases (MAPKs), might involved in the neuroprotection of BZYX. These results first demonstrated that BZYX had neuroprotective effects as well as cognition enhancement and acetylcholinesterase inhibition. It is hopeful that BZYX becomes a potential candidate for use in the intervention for neurodegenerative diseases.
ESTHER : Zhang_2009_Eur.J.Pharmacol_613_1
PubMedSearch : Zhang_2009_Eur.J.Pharmacol_613_1
PubMedID: 19345205

Title : Molecular cloning and characterization of a juvenile hormone esterase gene from brown planthopper, Nilaparvata lugens - Liu_2008_J.Insect.Physiol_54_1495
Author(s) : Liu S , Yang B , Gu J , Yao X , Zhang Y , Song F , Liu Z
Ref : J Insect Physiol , 54 :1495 , 2008
Abstract : Juvenile hormone (JH) plays key roles in the regulation of growth, development, diapause and reproduction in insects, and juvenile hormone esterase (JHE) plays an important role in regulating JH titers. We obtained a full-length cDNA encoding JHE in Nilaparvata lugens (NlJHE), the first JHE gene cloned from the hemipteran insects. The deduced protein sequence of Nljhe contains the five conserved motifs identified in JHEs of other insect species, including a consensus GQSAG motif that is required for the enzymatic activity of JHE proteins. Nljhe showed high amino acid similarities with Athalia rosae JHE (40%) and Apis mellifera JHE (39%). Recombinant NlJHE protein expressed in the baculovirus expression system hydrolyzed [3H] JH III at high activity and yielded the specificity constants (kcat/KM=4.28x10(6) M(-1) s(-1)) close to those of the validated JHEs from other insect species, indicating that Nljhe cDNA encodes a functional JH esterase. The Nljhe transcript was expressed mainly in the fat body and the expression level reached a peak at 48 h after ecdysis of the 5th instar nymphs. In the 5th instar, macropterous insects showed significantly higher Nljhe mRNA levels and JHE activities, but much lower JH III levels, than those detected in the brachypterous insects soon after ecdysis and at 48 h after ecdysis. These data suggest that NlJHE might play important roles in regulation of JH levels and wing form differentiation.
ESTHER : Liu_2008_J.Insect.Physiol_54_1495
PubMedSearch : Liu_2008_J.Insect.Physiol_54_1495
PubMedID: 18804476
Gene_locus related to this paper: nillu-b8q962

Title : 2-Phenoxy-indan-1-one derivatives as acetylcholinesterase inhibitors: a study on the importance of modifications at the side chain on the activity - Shen_2008_Bioorg.Med.Chem_16_7646
Author(s) : Shen Y , Sheng R , Zhang J , He Q , Yang B , Hu Y
Ref : Bioorganic & Medicinal Chemistry , 16 :7646 , 2008
Abstract : As a part of our project aimed at developing new agents of potential application in AD, a new series of 2-phenoxy-indan-1-one derivatives which possess alkylamine side chain were designed, synthesized, and evaluated for their inhibitory activity against AChE and BuChE. Most of the compounds were found to inhibit AChE in the nanomolar range. The optimum inhibitor 3g exhibited 34-fold increase in AChE inhibition than donepezil and displayed neuroprotective effect against H(2)O(2)-induced cell death.
ESTHER : Shen_2008_Bioorg.Med.Chem_16_7646
PubMedSearch : Shen_2008_Bioorg.Med.Chem_16_7646
PubMedID: 18662884

Title : [Separation and purification of recombinant Nippostrongylus brasiliensis acetylcholinesterase from culture medium of genetic engineering Pichia pastoris] - Zhang_2006_Se.Pu_24_39
Author(s) : Zhang Y , Yang B
Ref : Se Pu , 24 :39 , 2006
Abstract : To develop a simple, fast and highly efficient method for the separation and purification of recombinant Nippostrongylus brasiliensis acetylcholinesterase (NbAChE) from culture medium of genetic engineering Pichia pastoris, Q-Sepharose Fast Flow chromatographic medium was used. The chromatographic column was 20 cm x 3.5 cm i. d. The elution buffer A was 20 mmol/L NaH2PO4-Na2HPO4 (pH 8) and buffer B was 1 mol/L NaCl + 20 mmol/L NaH2PO4- Na2HPO4(pH 8). The elution gradient was nonlinear. It was firstly eluted with 10% B for 300 min, then with 30% B for 300 min, finally with 100% B for 300 min. The flow rate of mobile phase was 6 mL/min. The obtained recombinant NbAChE was proved to be homogeneous on sodium-dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and its relative molecular mass was estimated to be approximately 66 000, which was consistent with that reported in literature. The total activity recovery of this purification method was 52.6% and the purification factor was 3.87. The final specific activity of recombinant NbAChE was 2 837 U/mg. This chromatographic process is simple and highly efficient. It can be used to separate and purify recombinant NbAChE from culture medium of Pichia pastoris harboring NbAChE gene.
ESTHER : Zhang_2006_Se.Pu_24_39
PubMedSearch : Zhang_2006_Se.Pu_24_39
PubMedID: 16827308

Title : Disposable biosensor test for organophosphate and carbamate insecticides in milk - Zhang_2005_J.Agric.Food.Chem_53_5110
Author(s) : Zhang Y , Muench SB , Schulze H , Perz R , Yang B , Schmid RD , Bachmann TT
Ref : Journal of Agricultural and Food Chemistry , 53 :5110 , 2005
Abstract : A highly sensitive and rapid biosensor test based on disposable screen-printed thick-film electrodes was developed, which is suitable for monitoring organophosphate and carbamate residues in foods of animal origin with increased fat contents such as milk. The wild-type enzyme was combined with three engineered variants of Nippostrongylus brasiliensis acetylcholinesterase (NbAChE), to obtain enhanced sensitivity. The sample pretreatment could be reduced to a minimum. There was no extraction or fat removal necessary. With the biosensor test paraoxon concentrations down to 1 microg/L could be detected in milk. The detection limit for carbaryl was 20 microg/L. Recovery rates for paraoxon and carbaryl in milk samples lay between 89 and 107%. Ten milk samples from local markets were tested both with the biosensor test and with standard chromatographic multiresidue methods. Two milk samples caused AChE inhibition rates of >50%. Accordingly, 4 microg/L tebufenpyrad, 4 microg/L tetraconazole, and 2 microg/L bifenthrin were detected in one of these milk samples. The other milk sample contained 2 microg/L tebufenpyrad.
ESTHER : Zhang_2005_J.Agric.Food.Chem_53_5110
PubMedSearch : Zhang_2005_J.Agric.Food.Chem_53_5110
PubMedID: 15969483

Title : Excessive expression of acetylcholinesterase impairs glutamatergic synaptogenesis in hippocampal neurons - Dong_2004_J.Neurosci_24_8950
Author(s) : Dong H , Xiang YY , Farchi N , Ju W , Wu Y , Chen L , Wang Y , Hochner B , Yang B , Soreq H , Lu WY
Ref : Journal of Neuroscience , 24 :8950 , 2004
Abstract : Acetylcholinesterase (AChE) exerts noncatalytic activities on neural cell differentiation, adhesion, and neuritogenesis independently of its catalytic function. The noncatalytic functions of AChE have been attributed to its peripheral anionic site (PAS)-mediated protein-protein interactions. Structurally, AChE is highly homologous to the extracellular domain of neuroligin, a postsynaptic transmembrane molecule that interacts with presynaptic beta-neurexins, thus facilitating synaptic formation and maturation. Potential effects of AChE expression on synaptic transmission, however, remain unknown. Using electrophysiology, immunocytochemistry, and molecular biological approaches, this study investigated the role of AChE in the regulation of synaptic formation and functions. We found that AChE was highly expressed in cultured embryonic hippocampal neurons at early culture days, particularly in dendritic compartments including the growth cone. Subsequently, the expression level of AChE declined, whereas synaptic activity and synaptic proteins progressively increased. Chronic blockade of the PAS of AChE with specific inhibitors selectively impaired glutamatergic functions and excitatory synaptic structures independently of cholinergic activation, while inducing AChE overexpression. Moreover, the PAS blockade-induced glutamatergic impairments were associated with a depressed expression of beta-neurexins and an accumulation of other synaptic proteins, including neuroligins, and were mostly preventable by antisense suppression of AChE expression. Our findings demonstrate that interference with the nonenzymatic features of AChE alters AChE expression, which impairs excitatory synaptic structure and functions.
ESTHER : Dong_2004_J.Neurosci_24_8950
PubMedSearch : Dong_2004_J.Neurosci_24_8950
PubMedID: 15483114

Title : Overexpression of cytochrome P450 CYP2J2 protects against hypoxia-reoxygenation injury in cultured bovine aortic endothelial cells - Yang_2001_Mol.Pharmacol_60_310
Author(s) : Yang B , Graham L , Dikalov S , Mason RP , Falck JR , Liao JK , Zeldin DC
Ref : Molecular Pharmacology , 60 :310 , 2001
Abstract : CYP2J2 is abundant in human heart and its arachidonic acid metabolites, the epoxyeicosatrienoic acids (EETs), have potent vasodilatory, antiinflammatory and cardioprotective properties. This study was designed to examine the role of CYP2J2 in hypoxia-reoxygenation-induced injury in cultured bovine aortic endothelial cells (BAECs). Early passage BAECs were exposed to 24-h hypoxia followed by 4-h reoxygenation (HR). HR resulted in cell injury, as indicated by significant increases in lactate dehydrogenase (LDH) release and trypan blue stained cells (p < 0.01) and was associated with a decrease in CYP2J2 protein expression. Transfection of BAECs with the CYP2J2 cDNA resulted in increased CYP2J2 expression and arachidonic acid epoxygenase activity, compared with cells transfected with an irrelevant green fluorescent protein (GFP) cDNA. HR induced significant injury in GFP-transfected BAECs, as indicated by increases in LDH release and trypan blue-stained cells (p < 0.01); however, the HR-induced injury was markedly attenuated in CYP2J2-transfected cells (p < 0.01). HR increased cellular 8-iso-prostaglandin F(2alpha) (p < 0.05), and decreased eNOS expression, L-arginine uptake and conversion, and nitrite production (p < 0.01) in GFP-transfected BAECs. CYP2J2 transfection attenuated the HR-induced increase in 8-iso-prostaglandin F(2alpha) (p < 0.05) and decreased the amount of extracellular superoxide detected by cytochrome c reduction under normoxic conditions (p < 0.05) but did not significantly affect HR-induced decreases in eNOS expression, L-arginine uptake and conversion, and nitrite production. Treatment of BAECs with synthetic EETs and/or epoxide hydrolase inhibitors also showed protective effects against HR injury (p < 0.05). These observations suggest: (1) HR results in endothelial injury and decreased CYP2J2 expression; (2) transfection with the CYP2J2 cDNA protects against HR injury; and (3) the cytoprotective effects of CYP2J2 may be mediated, at least in part, by antioxidant effects.
ESTHER : Yang_2001_Mol.Pharmacol_60_310
PubMedSearch : Yang_2001_Mol.Pharmacol_60_310
PubMedID: 11455018

Title : Asymmetric Syntheses of 2-Substituted and 2,5-Disubstituted Pyrrolidines from (3S,5R,7aR)-5-(Benzotriazol-1-yl)-3-phenyl[2,1-b]oxazolopyrrolidine - Katritzky_1999_J.Org.Chem_64_1979
Author(s) : Katritzky AR , Cui XL , Yang B , Steel PJ
Ref : J Org Chem , 64 :1979 , 1999
Abstract : Benzotriazole, 2,5-dimethoxytetrahydrofuran, and (S)-phenylglycinol in one step gave 80% of (3S, 5R,7aR)-5-(benzotriazol-1-yl)-3-phenyl-[2,1-b]oxazolopyrrolidine (6), whose crystal structure was confirmed by X-ray crystallography. Novel chiral pyrrolidine synthon 6 reacts with organosilicon (allyltrimethylsilanes and vinyloxytrimethylsilanes), organophosphorus, organozinc, and Grignard reagents to afford chiral 2-substituted and 2,5-disubstituted pyrrolidines.
ESTHER : Katritzky_1999_J.Org.Chem_64_1979
PubMedSearch : Katritzky_1999_J.Org.Chem_64_1979
PubMedID: 11674292