Cai M

References (11)

Title : Association Lp-PLA2 Gene Polymorphisms with Coronary Heart Disease - Ma_2022_Dis.Markers_2022_9775699
Author(s) : Ma S , Ding L , Cai M , Chen L , Yan B , Yang J
Ref : Dis Markers , 2022 :9775699 , 2022
Abstract : OBJECTIVES: The study evaluated the association between lipoprotein-associated phospholipase A2 (Lp-PLA2) gene polymorphisms and coronary heart disease (CHD), in order to explore the molecular genetics of CHD. METHODS: Groups of CHD patients (n = 283) and healthy controls (n = 261) were involved in this study. R92H, V279F, and A379V polymorphisms of LP-PLA2 gene were confirmed using polymerase chain reaction (PCR) and direct DNA sequencing. These polymorphisms and their interaction were also analyzed as potential risk factors of CHD. RESULTS: In this study population, the genotypes of R92H (GG, GA, and AA), V279F (CC, AC, and AA) and A379V (GG, GA, and AA) were studied. There was a significantly difference in frequencies of R92H between CHD patients and controls (P < 0.05). In contrast, no significant difference in frequencies of V279F and A379V existed between CHD patients and controls. Furthermore, R92H and A379V were in strong linkage disequilibrium. CONCLUSIONS: These results suggested that R92H polymorphism might contribute to increased risk of CHD.
ESTHER : Ma_2022_Dis.Markers_2022_9775699
PubMedSearch : Ma_2022_Dis.Markers_2022_9775699
PubMedID: 35818585
Gene_locus related to this paper: human-PLA2G7

Title : The Aptamer Ob2, a novel AChE inhibitor, restores cognitive deficits and alleviates amyloidogenesis in 5FAD transgenic mice - Liang_2022_Mol.Ther.Nucleic.Acids_28_114
Author(s) : Liang Z , Li X , Luo X , Luo H , Chen Y , Cai M , Zhong X , Fang Y , Guo T , Shi Y , Zhang X
Ref : Mol Ther Nucleic Acids , 28 :114 , 2022
Abstract : Loss of cerebral cholinergic neurons and decreased levels of acetylcholine (ACh) are considered to be major factors causing cognitive dysfunction in Alzheimer's disease (AD). Abnormally elevated levels of acetylcholinesterase (AChE) resulting in decreased levels of ACh are common in AD patients; thus, AChE inhibitors (AChEIs) are widely used for the treatment of AD. In our previous work, we acquired DNA aptamers Ob1, Ob2, and Ob3 against human brain AChE from systematic evolution of ligands by exponential enrichment (SELEX). In this study, we investigated the effect of these aptamers on learning and memory abilities, as well as the underlying mechanism in a 5xFAD transgenic AD mouse model. Here, we showed that only aptamer Ob2 exhibits a good inhibitory effect on both mouse and human AChE activity. In addition, chronic treatment with aptamer Ob2 significantly improved cognitive ability of 5xFAD mice in the Morris water maze. Moreover, the mechanism of aptamer Ob2 in 5xFAD mice may be associated with its inhibition of AChE activity, alleviation of the levels of Abeta by lowering the expression of beta-secretase (BACE1), and activation of astrocytes in the brains of 5xFAD mice. These results indicate that aptamer Ob2 exhibits potential as an effective AChEI for the treatment of AD.
ESTHER : Liang_2022_Mol.Ther.Nucleic.Acids_28_114
PubMedSearch : Liang_2022_Mol.Ther.Nucleic.Acids_28_114
PubMedID: 35402070

Title : Attenuation of virulence in multiple serotypes (M1, M3, and M28) of Group A Streptococcus after the loss of secreted esterase - Zhang_2021_J.Microbiol.Immunol.Infect__
Author(s) : Zhang X , Zhao Y , Wang Y , Cai M , Song Y , Zhu H
Ref : J Microbiol Immunol Infect , : , 2021
Abstract : INTRODUCTION: Group A Streptococcus (GAS) can produce streptococcal secreted esterase (Sse), which inhibits neutrophil recruitment to the site of infection and is crucial for GAS pathogenesis. As an effective esterase, Sse hydrolyzes the sn-2 ester bond of human platelet-activating factor, inactivating it and abolishing its ability to recruit neutrophils. OBJECTIVES: The purpose of this study was to investigate the effects of sse deletion on the virulence of multiple serotypes of GAS. METHODS: Isogenic strains that lack the sse gene (deltasse) were derived from the parent strains MGAS5005 (serotype M1, CovRS mutant), MGAS2221 (serotype M1, wild-type CovRS), MGAS315 (serotype M3, CovRS mutant) and MGAS6180 (serotype M28, wild-type CovRS) and were used to study the differences in virulence and pathogenicity of GAS serotypes. RESULTS: In a subcutaneous infection model, mice infected with MGAS5005(deltasse) exhibited higher survival rates but decreased dissemination to the organs compared with mice infected with MGAS5005. When mice were infected with the four deltasse mutants, the MPO activity and IFN-gamma, TNF-alpha, IL-2 and IL-6 levels increased, but the skin lesion sizes decreased. In an intraperitoneal infection model, the absence of Sse significantly reduced the virulence of GAS, leading to increased mouse survival rates and decreased GAS burdens in the organs in most of the challenge experiments. In addition, the numbers of the four deltasse mutants were greatly reduced 60 min after incubation with isolated rat neutrophils. CONCLUSION: Our results suggest that Sse participates in the pathogenesis of multiple GAS serotypes (MGAS5005, MGAS2221, MGAS315 and MGAS6180), particularly the hypervirulent CovS mutant strains MGAS5005 and MGAS315. These strain differences were positively correlated with the virulence of the serotype.
ESTHER : Zhang_2021_J.Microbiol.Immunol.Infect__
PubMedSearch : Zhang_2021_J.Microbiol.Immunol.Infect__
PubMedID: 34674958

Title : Tailoring Particle-Enzyme Nanoconjugates for Biocatalysis at the Organic-Organic Interface - Sun_2020_ChemSusChem_13_6523
Author(s) : Sun Z , Cai M , Hubner R , Ansorge-Schumacher MB , Wu C
Ref : ChemSusChem , 13 :6523 , 2020
Abstract : Nonaqueous Pickering emulsions (PEs) are a powerful platform for catalysis design, offering both a large interface contact and a preferable environment for water-sensitive synthesis. However, up to now, little progress has been made to incorporate insoluble enzymes into the nonaqueous system for biotransformation. Herein, we present biocatalytically active nonaqueous PEs, stabilized by particle-enzyme nanoconjugates, for the fast transesterification and esterification, and eventually for biodiesel synthesis. Our nanoconjugates are the hybrid biocatalysts tailor-made by loading hydrophilic Candida antarctica lipase B onto hydrophobic silica nanoparticles, resulting in not only catalytically active but highly amphiphilic particles for stabilization of a methanol-decane emulsion. The enzyme activity in these PEs is significantly enhanced, ca. 375-fold higher than in the nonaqueous biphasic control. Moreover, the PEs can be multiply reused without significant loss of enzyme performance. With this proof-of-concept, this system can be expanded for many advanced syntheses using different enzymes in the future.
ESTHER : Sun_2020_ChemSusChem_13_6523
PubMedSearch : Sun_2020_ChemSusChem_13_6523
PubMedID: 33078882

Title : Methylotrophic yeast Pichia pastoris as a chassis organism for polyketide synthesis via the full citrinin biosynthetic pathway - Xue_2017_J.Biotechnol_242_64
Author(s) : Xue Y , Kong C , Shen W , Bai C , Ren Y , Zhou X , Zhang Y , Cai M
Ref : J Biotechnol , 242 :64 , 2017
Abstract : With the rapid development of synthetic biology, exploring various chassis organisms has become necessary to improve the heterologous biosynthesis of natural products and pharmaceuticals. In this study, we tested the potential of the industrial methylotrophic yeast strain Pichia pastoris for the heterologous synthesis of polyketides. A recombinant P. pastoris GS-pksCT-npgA carrying the Monascus purpureus citrinin polyketide synthase gene pksCT and the Aspergillus nidulans phosphopantetheinyl transferase gene npgA was constructed. Subsequently, a specific compound was isolated and identified as citrinin intermediate trimethylated pentaketide aldehyde. On account of the hypothetic functions of the genes in the citrinin gene cluster, mpl1 encoding serine hydrolase, mpl2 encoding oxygenase, and mpl4 encoding dehydrogenase were gradually expressed. Proteins were also normally expressed, but a new compound was undetected. Basing on the recently reported citrinin gene cluster in Monascus ruber, we obtained two other genes (mpl6 and mpl7) participating in citrinin biosynthesis by genome walking in M. purpureus. Then, we co-transformed intron-removed mpl6 and mpl7 into the P. pastoris strain carrying pksCT, npgA, mpl1, mpl2, and mpl4. All genes were activated by the methanol-induced AOX1 promoter, and a complete biosynthetic pathway of citrinin was assembled. Finally, citrinin was successfully produced under methanol induction in P. pastoris. These results prove that P. pastoris is a promising chassis organism for polyketide production.
ESTHER : Xue_2017_J.Biotechnol_242_64
PubMedSearch : Xue_2017_J.Biotechnol_242_64
PubMedID: 27913218
Gene_locus related to this paper: monpu-cita

Title : The memory-ameliorating effects of Artemisia princeps var. orientalis against cholinergic dysfunction in mice - Liu_2012_Am.J.Chin.Med_40_993
Author(s) : Liu X , Kim DH , Kim JM , Park SJ , Cai M , Jang DS , Ryu JH
Ref : Am J Chin Med , 40 :993 , 2012
Abstract : Artemisia princeps var. orientalis (Compositae) is widely distributed in China, Japan and Korea and is known to have anti-inflammatory and anti-oxidative activities. The ethyl acetate fraction of ethanolic extract of A. princeps var. orientalis (AEA) was found to inhibit acetylcholinesterase activity in a dose-dependent manner in vitro (IC(50) value: 541.4 +/- 67.5 mug/ml). Therefore, we investigated the effects of AEA on scopolamine-induced learning and memory impairment using the passive avoidance, the Y-maze, and the Morris water maze tasks in mice. AEA (100 or 200 mg/kg, p.o.) significantly ameliorated scopolamine-induced cognitive impairments in the passive avoidance and Y-maze tasks (p < 0.05). In the Morris water maze task, AEA (200 mg/kg, p.o.) significantly shortened escape latencies in training trials and increased both swimming time spent in the target zone and probe crossing numbers during the probe trial as compared with scopolamine-treated mice (p < 0.05). Additionally, the ameliorating effect of AEA on scopolamine-induced memory impairment was antagonized by a subeffective dose of MK-801. These results suggest that AEA could be an effective treatment against cholinergic dysfunction and its effect is mediated by the enhancement of the cholinergic neurotransmitter system via NMDA receptor signaling or acetylcholinesterase inhibition.
ESTHER : Liu_2012_Am.J.Chin.Med_40_993
PubMedSearch : Liu_2012_Am.J.Chin.Med_40_993
PubMedID: 22928830

Title : Genetic, molecular, and biochemical basis of fungal tropolone biosynthesis - Davison_2012_Proc.Natl.Acad.Sci.U.S.A_109_7642
Author(s) : Davison J , al Fahad A , Cai M , Song Z , Yehia SY , Lazarus CM , Bailey AM , Simpson TJ , Cox RJ
Ref : Proc Natl Acad Sci U S A , 109 :7642 , 2012
Abstract : A gene cluster encoding the biosynthesis of the fungal tropolone stipitatic acid was discovered in Talaromyces stipitatus (Penicillium stipitatum) and investigated by targeted gene knockout. A minimum of three genes are required to form the tropolone nucleus: tropA encodes a nonreducing polyketide synthase which releases 3-methylorcinaldehyde; tropB encodes a FAD-dependent monooxygenase which dearomatizes 3-methylorcinaldehyde via hydroxylation at C-3; and tropC encodes a non-heme Fe(II)-dependent dioxygenase which catalyzes the oxidative ring expansion to the tropolone nucleus via hydroxylation of the 3-methyl group. The tropA gene was characterized by heterologous expression in Aspergillus oryzae, whereas tropB and tropC were successfully expressed in Escherichia coli and the purified TropB and TropC proteins converted 3-methylorcinaldehyde to a tropolone in vitro. Finally, knockout of the tropD gene, encoding a cytochrome P450 monooxygenase, indicated its place as the next gene in the pathway, probably responsible for hydroxylation of the 6-methyl group. Comparison of the T. stipitatus tropolone biosynthetic cluster with other known gene clusters allows clarification of important steps during the biosynthesis of other fungal compounds including the xenovulenes, citrinin, sepedonin, sclerotiorin, and asperfuranone.
ESTHER : Davison_2012_Proc.Natl.Acad.Sci.U.S.A_109_7642
PubMedSearch : Davison_2012_Proc.Natl.Acad.Sci.U.S.A_109_7642
PubMedID: 22508998
Gene_locus related to this paper: talsn-tropf , talsn-tropi

Title : Complete genome sequence of Polymorphum gilvum SL003B-26A1T, a crude oil-degrading bacterium from oil-polluted saline soil - Li_2011_J.Bacteriol_193_2894
Author(s) : Li SG , Tang YQ , Nie Y , Cai M , Wu XL
Ref : Journal of Bacteriology , 193 :2894 , 2011
Abstract : Polymorphum gilvum SL003B-26A1(T) is a type strain of a newly published novel species in the novel genus Polymorphum. It was isolated from a crude oil-polluted saline soil in Shengli Oilfield, China, and was able to use the crude oil as the sole carbon source. Here we report the complete genome of SL003B-26A1(T) and the genes likely to be involved in oil degradation and ecological adaption.
ESTHER : Li_2011_J.Bacteriol_193_2894
PubMedSearch : Li_2011_J.Bacteriol_193_2894
PubMedID: 21478361
Gene_locus related to this paper: polgs-f2iwi7 , polgs-f2j4a9 , polgs-f2j5z8 , polgs-f2j578 , polgs-f2iy78

Title : Complete genome sequence of Amycolicicoccus subflavus DQS3-9A1T, an actinomycete isolated from crude oil-polluted soil - Cai_2011_J.Bacteriol_193_4538
Author(s) : Cai M , Chen WM , Nie Y , Chi CQ , Wang YN , Tang YQ , Li GY , Wu XL
Ref : Journal of Bacteriology , 193 :4538 , 2011
Abstract : Amycolicicoccus subflavus DQS3-9A1(T), isolated from crude oil-polluted soil in the Daqing Oilfield in China, is a type strain of a newly published novel species in the novel genus Amycolicicoccus. Here we report the complete genome of DQS3-9A1(T)and genes associated with oil-polluted environment.
ESTHER : Cai_2011_J.Bacteriol_193_4538
PubMedSearch : Cai_2011_J.Bacteriol_193_4538
PubMedID: 21725023
Gene_locus related to this paper: amysd-f6en24 , amysd-f6es27 , amysd-f6esh4 , amysd-f6eeb4 , amysd-f6es28 , amysd-f6ep66 , amysd-f6ehy7 , hoysd-f6eii9 , hoysd-f6ejm7

Title : Candida antarctica lipase B chemically immobilized on epoxy-activated micro- and nanobeads: catalysts for polyester synthesis - Chen_2008_Biomacromolecules_9_463
Author(s) : Chen B , Hu J , Miller EM , Xie W , Cai M , Gross RA
Ref : Biomacromolecules , 9 :463 , 2008
Abstract : Candida antarctica Lipase B (CALB) was covalently immobilized onto epoxy-activated macroporous poly(methyl methacrylate) Amberzyme beads (235 microm particle size, 220 A pore size) and nanoparticles (nanoPSG, diameter 68 nm) with a poly(glycidyl methacrylate) outer region. Amberzyme beads allowed CALB loading up to 0.16 g of enzyme per gram of support. IR microspectroscopy generated images of Amberzyme-CALB beads showed CALB is localized within a 50 microm thick loading front. IR microspectroscopy images, recorded prior to and after treatment of Amberzyme-CALB with DMSO/aqueous Triton X-100, are similar, confirming that CALB is largely chemically linked to Amberzyme. The activity of CALB immobilized on Amberzyme, Lewatit (i.e., Novozym 435 catalyst), and nanoPSG was assessed for lactone ring-opening and step-condensation polymerizations. For example, the percent conversion of -caprolactone using the same amount of enzyme catalyzed by Amberzym-CALB, Novozym 435, and nanoPSG-CALB for 20 min was 7.0, 16, and 65%, respectively. Differences in CALB reactivity were discussed based on resin physical parameters and availability of active sites determined by active site titrations. Regardless of the matrix used and chemical versus physical immobilization, -CL ring-opening polymerizations occur by a chain growth mechanism without chain termination. To test Amberzyme-CALB stability, the catalyst was reused over three reaction cycles for -CL ring-opening polymerization (70 degrees C, 70 min reactions) and glycerol/1,8-octanediol/adipic acid polycondensation reactions (90 degrees C, 64 h). Amberzyme-CALB was found to have far better stability for reuse relative to Novozym 435 for the polycondensation reaction.
ESTHER : Chen_2008_Biomacromolecules_9_463
PubMedSearch : Chen_2008_Biomacromolecules_9_463
PubMedID: 18197630
Gene_locus related to this paper: canar-LipB

Title : Organization and regulation of pentachlorophenol-degrading genes in Sphingobium chlorophenolicum ATCC 39723 - Cai_2002_J.Bacteriol_184_4672
Author(s) : Cai M , Xun L
Ref : Journal of Bacteriology , 184 :4672 , 2002
Abstract : The first three enzymes of the pentachlorophenol (PCP) degradation pathway in Sphingobium chlorophenolicum (formerly Sphingomonas chlorophenolica) ATCC 39723 have been characterized, and the corresponding genes, pcpA, pcpB, and pcpC, have been individually cloned and sequenced. To search for new genes involved in PCP degradation and map the physical locations of the pcp genes, a 24-kb fragment containing pcpA and pcpC was completely sequenced. A putative LysR-type transcriptional regulator gene, pcpM, and a maleylacetate reductase gene, pcpE, were identified upstream of pcpA. pcpE was found to play a role in PCP degradation. pcpB was not found on the 24-kb fragment. The four gene products PcpB, PcpC, PcpA, and PcpE were responsible for the metabolism of PCP to 3-oxoadipate in ATCC 39723, and inactivational mutation of each gene disrupted the degradation pathway. The organization of the pcp genes is unusual because the four PCP-degrading genes, pcpA, pcpB, pcpC, and pcpE, were found to be located at four discrete locations. Two hypothetical LysR-type regulator genes, pcpM and pcpR, have been identified; pcpM was not required, but pcpR was essential for the induction of pcpB, pcpA, and pcpE. The coinducers of PcpR were PCP and other polychlorinated phenols. The expression of pcpC was constitutive. Thus, the organization and regulation of the genes involved in PCP degradation to 3-oxoadipate were documented.
ESTHER : Cai_2002_J.Bacteriol_184_4672
PubMedSearch : Cai_2002_J.Bacteriol_184_4672
PubMedID: 12169590
Gene_locus related to this paper: flasp-Q8KN41