Zhong Q

References (6)

Title : Microbial-host-isozyme analyses reveal microbial DPP4 as a potential antidiabetic target - Wang_2023_Science_381_eadd5787
Author(s) : Wang K , Zhang Z , Hang J , Liu J , Guo F , Ding Y , Li M , Nie Q , Lin J , Zhuo Y , Sun L , Luo X , Zhong Q , Ye C , Yun C , Zhang Y , Wang J , Bao R , Pang Y , Wang G , Gonzalez FJ , Lei X , Qiao J , Jiang C
Ref : Science , 381 :eadd5787 , 2023
Abstract : A mechanistic understanding of how microbial proteins affect the host could yield deeper insights into gut microbiota-host cross-talk. We developed an enzyme activity-screening platform to investigate how gut microbiota-derived enzymes might influence host physiology. We discovered that dipeptidyl peptidase 4 (DPP4) is expressed by specific bacterial taxa of the microbiota. Microbial DPP4 was able to decrease the active glucagon like peptide-1 (GLP-1) and disrupt glucose metabolism in mice with a leaky gut. Furthermore, the current drugs targeting human DPP4, including sitagliptin, had little effect on microbial DPP4. Using high-throughput screening, we identified daurisoline-d4 (Dau-d4) as a selective microbial DPP4 inhibitor that improves glucose tolerance in diabetic mice.
ESTHER : Wang_2023_Science_381_eadd5787
PubMedSearch : Wang_2023_Science_381_eadd5787
PubMedID: 37535747
Gene_locus related to this paper: bactn-BT4193

Title : Widespread Expansion of Protein Interaction Capabilities by Alternative Splicing - Yang_2016_Cell_164_805
Author(s) : Yang X , Coulombe-Huntington J , Kang S , Sheynkman GM , Hao T , Richardson A , Sun S , Yang F , Shen YA , Murray RR , Spirohn K , Begg BE , Duran-Frigola M , MacWilliams A , Pevzner SJ , Zhong Q , Trigg SA , Tam S , Ghamsari L , Sahni N , Yi S , Rodriguez MD , Balcha D , Tan G , Costanzo M , Andrews B , Boone C , Zhou XJ , Salehi-Ashtiani K , Charloteaux B , Chen AA , Calderwood MA , Aloy P , Roth FP , Hill DE , Iakoucheva LM , Xia Y , Vidal M
Ref : Cell , 164 :805 , 2016
Abstract : While alternative splicing is known to diversify the functional characteristics of some genes, the extent to which protein isoforms globally contribute to functional complexity on a proteomic scale remains unknown. To address this systematically, we cloned full-length open reading frames of alternatively spliced transcripts for a large number of human genes and used protein-protein interaction profiling to functionally compare hundreds of protein isoform pairs. The majority of isoform pairs share less than 50% of their interactions. In the global context of interactome network maps, alternative isoforms tend to behave like distinct proteins rather than minor variants of each other. Interaction partners specific to alternative isoforms tend to be expressed in a highly tissue-specific manner and belong to distinct functional modules. Our strategy, applicable to other functional characteristics, reveals a widespread expansion of protein interaction capabilities through alternative splicing and suggests that many alternative "isoforms" are functionally divergent (i.e., "functional alloforms").
ESTHER : Yang_2016_Cell_164_805
PubMedSearch : Yang_2016_Cell_164_805
PubMedID: 26871637
Gene_locus related to this paper: human-NDRG4

Title : Influence of butyl benzyl phthalate (BBP) exposure on nervous system and antioxidant system in zebrafish - Zhang_2014_Ecotoxicology_23_1854
Author(s) : Zhang C , Yang X , He Z , Zhong Q , Guo J , Hu XJ , Xiong L , Liu D
Ref : Ecotoxicology , 23 :1854 , 2014
Abstract : In order to observe the toxic effects of butyl benzyl phthalate (BBP) on zebrafish, the AChE and SOD activity of zebrafish exposed to different concentrations of BBP (0, 0.332, 0.665, 1.33 mg L(-1)) in a short-term (7d) test were determined. Semi-quantitative PCR was used to determine the mRNA transcript levels of the AChE and SOD gene in zebrafish brain and muscle. The results showed: AChE activity decreased with increased exposure concentration, and was significantly inhibited (p < 0.01) compared with the control group at 0.665 mg L(-1) concentration. Low BBP concentrations stimulated and high concentrations inhibited SOD activity with a concentration of 0.332 mg L(-1) resulting in a significant induction (p < 0.05) compared with the control, and 0.665 and 1.33 mg L(-1) concentrations resulting in significant inhibition (p < 0.05, p < 0.01) relative to the control group. The RT-PCR data showed a decrease in brain and muscle mRNA transcription of AChE gene with an increase in exposure concentration. The mRNA transcription of SOD in the brain was not different between the exposed groups and control group; in muscle, the mRNA transcription inhibition decreased and then increased: all differences from the control were statistically significant.
ESTHER : Zhang_2014_Ecotoxicology_23_1854
PubMedSearch : Zhang_2014_Ecotoxicology_23_1854
PubMedID: 25239577

Title : In Vitro Evaluation of the Inhibitory Potential of Pharmaceutical Excipients on Human Carboxylesterase 1A and 2 - Zhang_2014_PLoS.One_9_e93819
Author(s) : Zhang C , Xu Y , Zhong Q , Li X , Gao P , Feng C , Chu Q , Chen Y , Liu D
Ref : PLoS ONE , 9 :e93819 , 2014
Abstract : Two major forms of human carboxylesterase (CES), CES1A and CES2, dominate the pharmacokinetics of most prodrugs such as imidapril and irinotecan (CPT-11). Excipients, largely used as insert vehicles in formulation, have been recently reported to affect drug enzyme activity. The influence of excipients on the activity of CES remains undefined. In this study, the inhibitory effects of 25 excipients on the activities of CES1A1 and CES2 were evaluated. Imidapril and CPT-11 were used as substrates and cultured with liver microsomes in vitro. Imidapril hydrolase activities of recombinant CES1A1 and human liver microsomes (HLM) were strongly inhibited by sodium lauryl sulphate (SLS) and polyoxyl 40 hydrogenated castor oil (RH40) [Inhibition constant (Ki) = 0.04+/-0.01 mug/ml and 0.20+/-0.09 mug/ml for CES1A1, and 0.12+/-0.03 mug/ml and 0.76+/-0.33 mug/ml, respectively, for HLM]. The enzyme hydrolase activity of recombinant CES2 was substantially inhibited by Tween 20 and polyoxyl 35 castor oil (EL35) (Ki = 0.93+/-0.36 mug/ml and 4.4+/-1.24 mug/ml, respectively). Thus, these results demonstrate that surfactants such as SLS, RH40, Tween 20 and EL35 may attenuate the CES activity; such inhibition should be taken into consideration during drug administration.
ESTHER : Zhang_2014_PLoS.One_9_e93819
PubMedSearch : Zhang_2014_PLoS.One_9_e93819
PubMedID: 24699684

Title : Draft genome sequence of Streptomyces coelicoflavus ZG0656 reveals the putative biosynthetic gene cluster of acarviostatin family alpha-amylase inhibitors - Guo_2012_Lett.Appl.Microbiol_55_162
Author(s) : Guo X , Geng P , Bai F , Bai G , Sun T , Li X , Shi L , Zhong Q
Ref : Lett Appl Microbiol , 55 :162 , 2012
Abstract : AIMS: The aims of this study are to obtain the draft genome sequence of Streptomyces coelicoflavus ZG0656, which produces novel acarviostatin family alpha-amylase inhibitors, and then to reveal the putative acarviostatin-related gene cluster and the biosynthetic pathway. METHODS AND
RESULTS: The draft genome sequence of S. coelicoflavus ZG0656 was generated using a shotgun approach employing a combination of 454 and Solexa sequencing technologies. Genome analysis revealed a putative gene cluster for acarviostatin biosynthesis, termed sct-cluster. The cluster contains 13 acarviostatin synthetic genes, six transporter genes, four starch degrading or transglycosylation enzyme genes and two regulator genes. On the basis of bioinformatic analysis, we proposed a putative biosynthetic pathway of acarviostatins. The intracellular steps produce a structural core, acarviostatin I00-7-P, and the extracellular assemblies lead to diverse acarviostatin end products.
CONCLUSIONS: The draft genome sequence of S. coelicoflavus ZG0656 revealed the putative biosynthetic gene cluster of acarviostatins and a putative pathway of acarviostatin production. SIGNIFICANCE AND IMPACT OF THE STUDY: To our knowledge, S. coelicoflavus ZG0656 is the first strain in this species for which a genome sequence has been reported. The analysis of sct-cluster provided important insights into the biosynthesis of acarviostatins. This work will be a platform for producing novel variants and yield improvement.
ESTHER : Guo_2012_Lett.Appl.Microbiol_55_162
PubMedSearch : Guo_2012_Lett.Appl.Microbiol_55_162
PubMedID: 22691180
Gene_locus related to this paper: 9actn-h1q5r8 , 9acto-h1qtl0 , 9acto-h1qi18 , 9acto-h1qeg2 , 9acto-h1qpr2

Title : Enzymatic assay method for evaluating the lipase activity in complex extracts from transgenic corn seed - Zhong_2006_J.Agric.Food.Chem_54_3181
Author(s) : Zhong Q , Glatz CE
Ref : Journal of Agricultural and Food Chemistry , 54 :3181 , 2006
Abstract : A colorimetric method was established to determine the activity of recombinant lipase in extracts from transgenic corn seed. The system was an oil-in-water emulsion that was stabilized by a surfactant to accommodate the organic phase substrate and aqueous phase enzyme. The lipase activity was measured by monitoring the release of nitrophenol at 346 nm from the substrate, 4-nitrophenyl butyrate. Emulsions prepared with various surfactant types and concentrations were tested. For each surfactant, the measured activity was greatest when the surfactant concentration was close to the critical micelle concentration, consistent with the changing trend of oil droplet size as a function of surfactant concentration. The optimal system, with 0.01% (w/w) Tween 80, demonstrated good reproducibility, high sensitivity, robustness, and a linear response to lipase concentration.
ESTHER : Zhong_2006_J.Agric.Food.Chem_54_3181
PubMedSearch : Zhong_2006_J.Agric.Food.Chem_54_3181
PubMedID: 16637669