Predominant contributions of carboxylesterase 1 and 2 in hydrolysis of anordrin in humans

References

• Ahmed TA, Hayslip J, Leggas M. (2013). Pharmacokinetics of high-dose simvastatin in refractory and relapsed chronic lymphocytic leukemia patients. Cancer Chemother Pharmacol 72:1369–74
   PubMed Web of Science ®Google Scholar
• Bin X, Peiqin Z, Weijuan Y. (1989). Antitumor action of Anordrin on experimental tumors. Tumor 9:197–9
   Google Scholar
• Chatterton RT, Jr., Berman C, Walters NN. (1989). Anti-uterotrophic and folliculostatic activities of anordiol (2 alpha,17 alpha-diethynyl-A-nor-5 alpha-androstane-2 beta,17 beta-diol). Contraception 39:291–7
   PubMed Web of Science ®Google Scholar
• Chatterton RT Jr, Kowalski W, Lu YC, et al. (1994). Pharmacokinetics and pharmacodynamics of anordrin (2 alpha, 17 alpha-diethynyl-A-nor-5 alpha-androstane-2 beta, 17 beta-diol diproprionate). Steroids 59:217–23
   PubMed Web of Science ®Google Scholar
• Chih-Ping K, Ming-Kang C, Hsiu-Chuan C, et al. (1976). Pharmacological studies of a contraceptive drug anordrin. Chin Med J (Engl) 2:177–84
   PubMed Web of Science ®Google Scholar
• Fukami T, Kariya M, Kurokawa T, et al. (2015). Comparison of substrate specificity among human arylacetamide deacetylase and carboxylesterases. Eur J Pharm Sci 78:47–53
   PubMed Web of Science ®Google Scholar
• Fukami T, Yokoi T. (2012). The emerging role of human esterases. Drug Metab Pharmacokinet 27:466–77
   PubMed Web of Science ®Google Scholar
• Gu Z, Zhu D, Qi L, et al. (1984). Studies on the antifertility effects of anordrin and its analogues. Acta Physiol Sinica 36:611–13
   Google Scholar
• Higgins JW, Bao JQ, Ke AB, et al. (2014). Utility of Oatp1a/1b-knockout and OATP1B1/3-humanized mice in the study of OATP-mediated pharmacokinetics and tissue distribution: case studies with pravastatin, atorvastatin, simvastatin, and carboxydichlorofluorescein. Drug Metab Dispos 42:182–92
   PubMed Web of Science ®Google Scholar
• Hirano M, Maeda K, Shitara Y, et al. (2006). Drug-drug interaction between pitavastatin and various drugs via OATP1B1. Drug Metab Dispos 34:1229–36
   PubMed Web of Science ®Google Scholar
• Holmes RS, Wright MW, Laulederkind SJ, et al. (2010). Recommended nomenclature for five mammalian carboxylesterase gene families: human, mouse, and rat genes and proteins. Mamm Genome 21:427–41
   PubMed Web of Science ®Google Scholar
• Imai T. (2006). Human carboxylesterase isozymes: catalytic properties and rational drug design. Drug. Metab Pharmacokinet 21:173–85
   PubMed Web of Science ®Google Scholar
• Khanna R, Morton CL, Danks MK, et al. (2000). Proficient metabolism of irinotecan by a human intestinal carboxylesterase. Cancer Res 60:4725–8
   PubMed Web of Science ®Google Scholar
• Li B, Sedlacek M, Manoharan I, et al. (2005). Butyrylcholinesterase, paraoxonase, and albumin esterase, but not carboxylesterase, are present in human plasma. Biochem Pharmacol 70:1673–84
   PubMed Web of Science ®Google Scholar
• Ma ZC, Lou LG, Zhang Z, et al. (2000). Antiangiogenic effect of alpha-anordrin in vitro and in vivo. Acta Pharmacol Sin 21:939–44
   PubMed Web of Science ®Google Scholar
• Mehta RR, Jenco JM, Chatterton RT. Jr. (1981). Antiestrogenic and antifertility actions of anordrin (2 alpha, 17 alpha-diethynyl-A-nor-5 alpha-androstane-2 beta, 17 beta-diol 2,17-dipropionate). Steroids 38:679–91
   PubMed Web of Science ®Google Scholar
• Mehta RR, Jenco JM, Chatterton RT, et al. (1982). Antagonism of the actions of estrogens, androgens and progesterone by anordrin (2-alpha,17-alpha-diethynyl-a-nor-5-alpha-androstane-2-beta,17-beta-diol dipropionate). Steroids 40:65–80
   PubMed Web of Science ®Google Scholar
• Nakajima A, Fukami T, Kobayashi Y, et al. (2011). Human arylacetamide deacetylase is responsible for deacetylation of rifamycins: rifampicin, rifabutin, and rifapentine. Biochem Pharmacol 82:1747–56
   PubMed Web of Science ®Google Scholar
• Ross MK, Borazjani A, Wang R, et al. (2012). Examination of the carboxylesterase phenotype in human liver. Arch Biochem Biophys 522:44–56
   PubMed Web of Science ®Google Scholar
• Sang G, Shao Q, Zhang L. (1999). A randomized multicentre clinical trial on different doses of mifepristone alone and in combination with anordrin as emergency contraception. Zhonghua fu chan ke za Zhi 34:331–4
   PubMedGoogle Scholar
• Sato Y, Miyashita A, Iwatsubo T, et al. (2012). Simultaneous absolute protein quantification of carboxylesterases 1 and 2 in human liver tissue fractions using liquid chromatography-tandem mass spectrometry. Drug Metab Dispos 40:1389–96
   PubMed Web of Science ®Google Scholar
• Shimizu M, Fukami T, Nakajima M, et al. (2014). Screening of specific inhibitors for human carboxylesterases or arylacetamide deacetylase. Drug Metab Dispos 42:1103–9
   PubMed Web of Science ®Google Scholar
• Takahashi S, Katoh M, Saitoh T, et al. (2008). Allosteric kinetics of human carboxylesterase 1: species differences and interindividual variability. J Pharm Sci 97:5434–45
   PubMed Web of Science ®Google Scholar
• Wang XW, Zhu HJ, Markowitz JS. (2015). Carboxylesterase 1-mediated drug-drug interactions between clopidogrel and simvastatin. Biol Pharm Bull 38:292–7
   PubMed Web of Science ®Google Scholar
• Watanabe A, Fukami T, Nakajima M, et al. (2009). Human arylacetamide deacetylase is a principal enzyme in flutamide hydrolysis. Drug Metab Dispos 37:1513–20
   PubMed Web of Science ®Google Scholar
• Watanabe A, Fukami T, Takahashi S, et al. (2010). Arylacetamide deacetylase is a determinant enzyme for the difference in hydrolase activities of phenacetin and acetaminophen. Drug Metab Dispos 38:1532–7
   PubMed Web of Science ®Google Scholar
• Zhu H, Markowitz JS. (2013). Carboxylesterase 1 (CES1) genetic polymorphisms and oseltamivir activation. Eur J Clin Pharmacol 69:733–4
   PubMed Web of Science ®Google Scholar