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Examination of the carboxylesterase phenotype in human liver

文献类型： 外文期刊

作者： Ross, Matthew K. 1 ; Borazjani, Abdolsamad 1 ; Wang, Ran 1 ; Crow, J. Allen 1 ; Xie, Shuqi 1 ;

作者机构： 1.Mississippi State Univ, Coll Vet Med, Dept Basic Sci, Ctr Environm Hlth Sci, Mississippi State, MS 39762 USA

2.Jiangsu Acad Agr Sci, Nanjing 210014, Peoples R China

关键词： Activity-based probes;Carboxylesterases;CES1;Human liver;Interindividual variation;Pesticides

期刊名称：ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS （ 影响因子：4.013； 五年影响因子：4.076 ）

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收录情况： SCI

摘要： Carboxylesterases (CES) metabolize esters. Two CES isoforms are expressed in human liver (CES1 and CES2) and liver extracts are used in reaction phenotyping studies to discern interindividual metabolic variation. We tested the hypothesis that an individual's CES phenotype can be characterized by reporter substrates/probes that interrogate native CES1 and CES2 activities in liver and immunoblotting methods. We obtained 25 livers and found that CES1 is the main hydrolytic enzyme. Moreover, although CES1 protein levels were similar, we observed large interindividual variation in bioresmethrin hydrolysis rates (17-fold), a pyrethroid metabolized by CES1 but not CES2. Bioresmethrin hydrolysis rates did not correlate with CES1 protein levels. In contrast, procaine hydrolysis rates, a drug metabolized by CES2 but not CES1, were much less variant (3-fold). Using activity-based fluorophosphonate probes (FP-biotin), which covalently reacts with active serine hydrolases, CES1 protein was the most active enzyme in the livers. Finally, using bioorthogonal probes and click chemistry methodology, the half-life of CES 1 and 2 in cultured HepG2 cells was estimated at 96 h. The cause of the differential CES1 activities is unknown, but the underlying factors will be important to understand because several carboxylic acid ester drugs and environmental toxicants are metabolized by this enzyme.

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