Gu L

References (11)

Title : Sugammadex enhances recovery after abdominal surgery in cancer patients: a real-world, observational study - Gu_2021_Ann.Palliat.Med_10_12566
Author(s) : Gu X , Gao R , Li P , Jiao D , Song T , Li T , Gu L
Ref : Ann Palliat Med , 10 :12566 , 2021
Abstract : BACKGROUND: Sugammadex, a modified gamma-cyclodextrin that selectively binds to muscle relaxants, is increasingly being used to reverse neuromuscular blockade after surgery, but the potential benefits for cancer patients in the real-world setting are obscure. METHODS: This was a real-world, retrospective study. Adult cancer patients (<=18 years) undergoing abdominal surgery at Jiangsu Cancer Hospital, a tertiary care cancer hospital in China, between 2 March 2018 and 25 November 2019, were included in the analysis. Patients received 2 mg/kg (maximally 200 mg) sugammadex based on the discretion of the attending anesthetists. Patients were extubated as soon as they were awake and able to follow commands. The endpoint measures included extubation time, bowel function recovery and length of hospital stay. RESULTS: A total of 1,615 patients were included in the analysis: 795 participants received sugammadex at a dosage of 2 mg/kg (maximum 200 mg) upon completion of surgery; the remaining 820 participants did not receive sugammadex or neostigmine (another antidote for neuromuscular blockade). Despite several biases that clearly favored patients not receiving sugammadex [younger, better American Society of Anesthesiologists (ASA) status, and fewer comorbidities], the extubation time was significantly shorter in patients receiving sugammadex [median: 14 (range, 0-121) vs. 30.5 (range, 0-183) min; P<0.001]. In multivariate linear regression analysis, sugammadex use was associated with a significantly shorter extubation time (P<0.05). Patients who received sugammadex also had accelerated bowel function recovery and shorter postoperative hospital stay. CONCLUSIONS: Sugammadex shortens extubation time and accelerates postoperative recovery in cancer patients undergoing abdominal surgery.
ESTHER : Gu_2021_Ann.Palliat.Med_10_12566
PubMedSearch : Gu_2021_Ann.Palliat.Med_10_12566
PubMedID: 35016451

Title : Rapid screening for natural lipase inhibitors from Alisma orientale combining high-performance thin-layer chromatography-bioautography with mass spectrometry - Yang_2021_J.Chromatogr.B.Analyt.Technol.Biomed.Life.Sci_1170_122599
Author(s) : Yang F , Gu L , Han Z , Wang Z
Ref : Journal of Chromatography B Analyt Technol Biomed Life Sciences , 1170 :122599 , 2021
Abstract : Lipase inhibitors are an attractive class of hypolipidemic compounds, which inhibit the activity of human pancreatic lipase, thereby preventing the absorption of triglycerides in vivo. As a library of promising lead compounds for drug development, traditional Chinese medicine (TCM) has gained growing attention in quick discovery and identification of enzyme inhibitors of natural-origin. The purpose of this work was to discover unknown lipase inhibitors from Alisma orientale by the activity oriented analysis method thin-layer chromatography-bioautography, then use electrospray ionization mass spectrometry technology via the elution based TLC-MS interface to identify their structures. As a result, eleven natural lipase inhibitors from Alisma orientale extracts were identified based on molecular mass and fragment ions obtained by HPTLC-MS, and further confirmed by a series of complementary means including UV spectra, (1)H NMR characteristic proton signals and polarity of compounds, eleven lipase inhibitors were tentatively assigned as triterpenoids: alisol B (m/z 495.50 [M + Na](+)), alisol B 23-acetate (m/z 537.58 [M + Na](+)), 11-deoxy-alisol B (m/z 479.50 [M + Na](+)), 11-deoxy-alisol B 23-acetate (m/z 521.50 [M + Na](+)), alisol A/epialisol A (m/z 513.50 [M + Na](+)), 16-oxo-11-deoxy-alisol A (m/z 511.50 [M + Na](+)), 16-oxo-alisol A (527.50 [M + Na] (+)), alisol C (m/z 509.58 [M + Na](+)), alisol C 23-acetate (m/z 551.50 [M + Na](+)), alisol M 23-acetate (m/z 567.50 [M + Na](+)), and alismanol Q/neoalisol (m/z 493.42 [M + Na](+)). The integrated approach is an efficient method for rapid screening lipase inhibitors from complex plant extracts and provides a reasonable and favorable basis for the identification and separation of other enzymatic system and other important compounds with therapeutic values.
ESTHER : Yang_2021_J.Chromatogr.B.Analyt.Technol.Biomed.Life.Sci_1170_122599
PubMedSearch : Yang_2021_J.Chromatogr.B.Analyt.Technol.Biomed.Life.Sci_1170_122599
PubMedID: 33713950

Title : Cascade Reaction System Integrating Single-Atom Nanozymes with Abundant Cu Sites for Enhanced Biosensing - Wu_2020_Anal.Chem__
Author(s) : Wu Y , Wu J , Jiao L , Xu W , Wang H , Wei X , Gu W , Ren G , Zhang N , Zhang Q , Huang L , Gu L , Zhu C
Ref : Analytical Chemistry , : , 2020
Abstract : Single-atom nanozymes (SAzymes), as novel nanozymes with atomically dispersed active sites, are of great importance in the de-velopment of nanozymes for their high catalytic activities, the maximum utilization efficiency of metal atoms, and the simple mod-el of active sites. Herein, the peroxidase-like SAzymes with high-concentration Cu sites on carbon nanosheets (Cu-N-C) were syn-thesized through a salt-template strategy. With the densely distributed active Cu atoms (~5.1 wt%), the Cu-N-C SAzymes exhibit remarkable activity to mimic natural peroxidase. Integrating Cu-N-C SAzymes with natural acetylcholinesterase and choline oxi-dase, three-enzyme-based cascade reaction system was constructed for the colorimetric detection of acetylcholine and organo-phosphorus pesticides. This work not only provides a strategy to synthesize SAzymes with abundant active sites but also gives some new insights for robust nanozyme biosensing systems.
ESTHER : Wu_2020_Anal.Chem__
PubMedSearch : Wu_2020_Anal.Chem__
PubMedID: 31941278

Title : The histone demethylase Jarid1b mediates angiotensin II-induced endothelial dysfunction by controlling the 3'UTR of soluble epoxide hydrolase - Vasconez_2019_Acta.Physiol.(Oxf)_225_e13168
Author(s) : Vasconez AE , Janetzko P , Oo JA , Pfluger-Muller B , Ratiu C , Gu L , Helin K , Geisslinger G , Fleming I , Schroder K , Fork C , Brandes RP , Leisegang MS
Ref : Acta Physiol (Oxf) , 225 :e13168 , 2019
Abstract : AIM: The histone demethylase Jarid1b limits gene expression by removing the active methyl mark from histone3 lysine4 at gene promoter regions. A vascular function of Jarid1b is unknown, but a vasoprotective function to inflammatory and hypertrophic stimuli, like angiotensin II (AngII) could be inferred. This hypothesis was tested using Jarid1b knockout mice and the inhibitor PBIT. METHODS: Mice or aortic segments were treated with AngII to induce endothelial dysfunction. Aortae from WT and Jarid1b knockout were studied in organ chambers and endothelium-dependent dilator responses to acetylcholine and endothelium-independent responses to DetaNONOate were recorded after pre-constriction with phenylephrine in the presence or absence of the NO-synthase inhibitor nitro-L-arginine. Molecular mechanisms were investigated with chromatin immunoprecipitation, RNA-Seq, RNA-3'-adaptor-ligation, actinomycin D and RNA-immunoprecipitation. RESULTS: Knockout or inhibition of Jarid1b prevented the development of endothelial dysfunction in response to AngII. This effect was not a consequence of altered nitrite oxide availability but accompanied by a loss of the inflammatory response to AngII. As Jarid1b mainly inhibits gene expression, an indirect effect should account for this observation. AngII induced the soluble epoxide hydrolase (sEH), which degrades anti-inflammatory lipids, and thus promotes inflammation. Knockout or inhibition of Jarid1b prevented the AngII-mediated sEH induction. Mechanistically, Jarid1b maintained the length of the 3'untranslated region of the sEH mRNA, thereby increasing its stability and thus sEH protein expression. Loss of Jarid1b activity therefore resulted in sEH mRNA destabilization. CONCLUSION: Jarid1b contributes to the pro-inflammatory effects of AngII by stabilizing sEH expression. Jarid1b inhibition might be an option for future therapeutics against cardiovascular dysfunction.
ESTHER : Vasconez_2019_Acta.Physiol.(Oxf)_225_e13168
PubMedSearch : Vasconez_2019_Acta.Physiol.(Oxf)_225_e13168
PubMedID: 30076673

Title : High-level expression of Humicola insolens cutinase in Pichia pastoris without carbon starvation and its use in cotton fabric bioscouring - Hong_2019_J.Biotechnol_304_10
Author(s) : Hong R , Sun Y , Su L , Gu L , Wang F , Wu J
Ref : J Biotechnol , 304 :10 , 2019
Abstract : Huimcola insolens cutinase (HiC) was heterologously expressed in Pichia pastoris. To avoid a carbon starvation step, fermentation was conducted using combinations of sorbitol with glycerol and methanol in the cell growth and induction phases, respectively. The cutinase productivity (27.71 U mL(-1) h(-1)) was 9.93 U mL(-1) h(-1) greater than that achieved using traditional two-phase methods, and a cutinase activity of 2660 U mL(-1), using p-nitrophenyl butyrate as substrate, was achieved after only 96 h in a 3-L bioreactor. Subsequently, the combination of HiC with Thermobifida fusca cutinase (TfC) in cotton fabric bioscouring was evaluated by monitoring the wettability and dyeability of the fabric. Treatment with 20 U mL(-1) of HiC at 80 degrees C for 5 min followed by 30 U mL(-1) of TfC at 50 degrees C for 1 h gave the best results. The total treatment time was shorter and performance was better than those seen with the alkali method.
ESTHER : Hong_2019_J.Biotechnol_304_10
PubMedSearch : Hong_2019_J.Biotechnol_304_10
PubMedID: 31400343

Title : [Elementary research of constructive feature and three-dimensional reconstruction of nerve bundles of C7 anterior and posterior division end] - Qin_2012_Zhongguo.Xiu.Fu.Chong.Jian.Wai.Ke.Za.Zhi_26_97
Author(s) : Qin B , Gu L , Xiang J , Fu G , Qi J , Wang H , Zhang D , Zheng J , Liu X , Zhu J
Ref : Zhongguo Xiu Fu Chong Jian Wai Ke Za Zhi , 26 :97 , 2012
Abstract : OBJECTIVE: To observe the distribution feature of nerve bundles in C7 nerve anterior and posterior division end. METHODS: The brachial plexus specimen was harvested from 1 fresh adult cadaver. After C7 nerve was confirmed, the distal end of anterior and posterior division was dissected and embedded by OCT. Then the samples were serially horizontally sliced with each 10 microm deep. After acetylcholinesterase (AChE) histochemical staining, the stain characteristics of different nerve fiber bundles were observed and amount of the nerve fiber bundles were counted under optic-microscope. At last, the imaging which were collected were three-dimensional (3-D) reconstructed by using Amira 4.1 software. RESULTS: There was no obvious difference in the stain between the anterior and posterior divisions. The running of the nerve fiber bundles were dispersive from proximal end of nerve to distal end of nerve. Nerve fiber bundles of anterior division were mainly sensor nerve fiber bundles, which located in medial side. Nerve fiber bundles of posterior division were mainly moter nerve fiber bundles, having no regularity in the distribution of nerve fiber bundles. The total number of nerve fiber bundles in distal end of anterior division was 7.85 +/- 1.04, the number of motor nerve fiber bundles was 2.85 +/- 0.36, and the number of sensor nerve fiber bundles was 5.13 +/- 1.01. The total number of nerve fiber bundles in distal end of posterior division was 9.79 +/- 1.53, the number of motor nerve fiber bundles was 6.00 +/- 0.69, and the number of sensor nerve fiber bundles was 3.78 +/- 0.94. There were significant differences in the numbers of motor and sensor nerve fiber bundles between anterior and posterior divisions (P < 0.05). The microstructure 3-D model was reconstructed based on serial slice through Amira 4.1. The intercross and recombination process of nerves bundles could be observed obviously. The nerve bundle distribution showed cross and combination. CONCLUSION: Nerve fiber bundles of anterior division are mainly sensor nerve fiber bundles and locate in medial side. Nerve fiber bundles of posterior division are mainly motor nerve fiber bundles, which has no regularity in the distribution of nerve fiber bundles. The 3-D reconstruction can display the internal structure feature of the C7 division end.
ESTHER : Qin_2012_Zhongguo.Xiu.Fu.Chong.Jian.Wai.Ke.Za.Zhi_26_97
PubMedSearch : Qin_2012_Zhongguo.Xiu.Fu.Chong.Jian.Wai.Ke.Za.Zhi_26_97
PubMedID: 22332529

Title : Structure and activity of DmmA, a marine haloalkane dehalogenase - Gehret_2012_Protein.Sci_21_239
Author(s) : Gehret JJ , Gu L , Geders TW , Brown WC , Gerwick L , Gerwick WH , Sherman DH , Smith JL
Ref : Protein Science , 21 :239 , 2012
Abstract : DmmA is a haloalkane dehalogenase (HLD) identified and characterized from the metagenomic DNA of a marine microbial consortium. Dehalogenase activity was detected with 1,3-dibromopropane as substrate, with steady-state kinetic parameters typical of HLDs (K(m) = 0.24 +/- 0.05 mM, k(cat) = 2.4 +/- 0.1 s(-1) ). The 2.2-A crystal structure of DmmA revealed a fold and active site similar to other HLDs, but with a substantially larger active site binding pocket, suggestive of an ability to act on bulky substrates. This enhanced cavity was shown to accept a range of linear and cyclic substrates, suggesting that DmmA will contribute to the expanding industrial applications of HLDs.
ESTHER : Gehret_2012_Protein.Sci_21_239
PubMedSearch : Gehret_2012_Protein.Sci_21_239
PubMedID: 22124946
Gene_locus related to this paper: 9cyan-q6dnd9

Title : Terminal alkene formation by the thioesterase of curacin A biosynthesis: structure of a decarboxylating thioesterase - Gehret_2011_J.Biol.Chem_286_14445
Author(s) : Gehret JJ , Gu L , Gerwick WH , Wipf P , Sherman DH , Smith JL
Ref : Journal of Biological Chemistry , 286 :14445 , 2011
Abstract : Curacin A is a polyketide synthase (PKS)-non-ribosomal peptide synthetase-derived natural product with potent anticancer properties generated by the marine cyanobacterium Lyngbya majuscula. Type I modular PKS assembly lines typically employ a thioesterase (TE) domain to off-load carboxylic acid or macrolactone products from an adjacent acyl carrier protein (ACP) domain. In a striking departure from this scheme the curacin A PKS employs tandem sulfotransferase and TE domains to form a terminal alkene moiety. Sulfotransferase sulfonation of beta-hydroxy-acyl-ACP is followed by TE hydrolysis, decarboxylation, and sulfate elimination (Gu, L., Wang, B., Kulkarni, A., Gehret, J. J., Lloyd, K. R., Gerwick, L., Gerwick, W. H., Wipf, P., Hakansson, K., Smith, J. L., and Sherman, D. H. (2009) J. Am. Chem. Soc. 131, 16033-16035). With low sequence identity to other PKS TEs (<15%), the curacin TE represents a new thioesterase subfamily. The 1.7-A curacin TE crystal structure reveals how the familiar alpha/beta-hydrolase architecture is adapted to specificity for beta-sulfated substrates. A Ser-His-Glu catalytic triad is centered in an open active site cleft between the core domain and a lid subdomain. Unlike TEs from other PKSs, the lid is fixed in an open conformation on one side by dimer contacts of a protruding helix and on the other side by an arginine anchor from the lid into the core. Adjacent to the catalytic triad, another arginine residue is positioned to recognize the substrate beta-sulfate group. The essential features of the curacin TE are conserved in sequences of five other putative bacterial ACP-ST-TE tridomains. Formation of a sulfate leaving group as a biosynthetic strategy to facilitate acyl chain decarboxylation is of potential value as a route to hydrocarbon biofuels.
ESTHER : Gehret_2011_J.Biol.Chem_286_14445
PubMedSearch : Gehret_2011_J.Biol.Chem_286_14445
PubMedID: 21357626
Gene_locus related to this paper: 9cyan-d0e8e2

Title : Polyketide decarboxylative chain termination preceded by o-sulfonation in curacin a biosynthesis - Gu_2009_J.Am.Chem.Soc_131_16033
Author(s) : Gu L , Wang B , Kulkarni A , Gehret JJ , Lloyd KR , Gerwick L , Gerwick WH , Wipf P , Hakansson K , Smith JL , Sherman DH
Ref : Journal of the American Chemical Society , 131 :16033 , 2009
Abstract : Biosynthetic innovation in natural product systems is driven by the recruitment of new genes and enzymes into these complex pathways. Here, an unprecedented decarboxylative chain termination mechanism is described for the polyketide synthase of curacin A, an anticancer lead compound isolated from the marine cyanobacterium Lyngbya majuscula. The unusual chain termination module containing adjacent sulfotransferase (ST) and thioesterase (TE) catalytic domains embedded in CurM was biochemically characterized. The TE was proved to catalyze a hydrolytic chain release of the polyketide chain elongation intermediate. Moreover, a selective ST-mediated sulfonation of the (R)-beta-hydroxyl group was found to precede TE-mediated hydrolysis, triggering a successive decarboxylative elimination and resulting in the formation of a rare terminal olefin in the final metabolite.
ESTHER : Gu_2009_J.Am.Chem.Soc_131_16033
PubMedSearch : Gu_2009_J.Am.Chem.Soc_131_16033
PubMedID: 19835378
Gene_locus related to this paper: 9cyan-d0e8e2

Title : Synthesis and biological evaluation of functionalized coumarins as acetylcholinesterase inhibitors - Shen_2005_Eur.J.Med.Chem_40_1307
Author(s) : Shen Q , Peng Q , Shao J , Liu X , Huang Z , Pu X , Ma L , Li YM , Chan AS , Gu L
Ref : Eur Journal of Medicinal Chemistry , 40 :1307 , 2005
Abstract : Three series of functionalized coumarin compounds were designed and prepared as cholinesterase (AChE and BuChE) inhibitors. The biological profile against AChE and BuChE of the prepared compounds was determined. Compound 7b exhibited a mixed-type of AChE inhibitor with IC50 value for the AChE inhibition of 0.19+/-0.01 microM and a high selectivity for AChE/BuChE, and compound 6b acted as non-competitive AChE inhibitor with IC50 value of 0.43+/-0.02 microM. Structure-activity relationships (SARs) of prepared compounds were discussed.
ESTHER : Shen_2005_Eur.J.Med.Chem_40_1307
PubMedSearch : Shen_2005_Eur.J.Med.Chem_40_1307
PubMedID: 16182411

Title : Mice lacking serum paraoxonase are susceptible to organophosphate toxicity and atherosclerosis - Shih_1998_Nature_394_284
Author(s) : Shih DM , Gu L , Xia YR , Navab M , Li WF , Hama S , Castellani LW , Furlong CE , Costa LG , Fogelman AM , Lusis AJ
Ref : Nature , 394 :284 , 1998
Abstract : Serum paraoxonase (PON1) is an esterase that is associated with high-density lipoproteins (HDLs) in the plasma; it is involved in the detoxification of organophosphate insecticides such as parathion and chlorpyrifos. PON1 may also confer protection against coronary artery disease by destroying pro-inflammatory oxidized lipids present in oxidized low-density lipoproteins (LDLs). To study the role of PON1 in vivo, we created PON1-knockout mice by gene targeting. Compared with their wild-type littermates, PON1-deficient mice were extremely sensitive to the toxic effects of chlorpyrifos oxon, the activated form of chlorpyrifos, and were more sensitive to chlorpyrifos itself. HDLs isolated from PON1-deficient mice were unable to prevent LDL oxidation in a co-cultured cell model of the artery wall, and both HDLs and LDLs isolated from PON1-knockout mice were more susceptible to oxidation by co-cultured cells than the lipoproteins from wild-type littermates. When fed on a high-fat, high-cholesterol diet, PON1-null mice were more susceptible to atherosclerosis than their wild-type littermates.
ESTHER : Shih_1998_Nature_394_284
PubMedSearch : Shih_1998_Nature_394_284
PubMedID: 9685159