Differential responses of rat hepatic microsomal carboxylesterase isozymes to glucocorticoids and pregnenolone 16α-carbonitrile
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Structural organization and characterization of the regulatory element of the human carboxylesterase (CES1A1 and CES1A2) genes
2008, Drug Metabolism and PharmacokineticsPregnane X receptor is a target of farnesoid X receptor
2006, Journal of Biological ChemistryCitation Excerpt :PXR regulates an entire program of genes involved in the detoxification and elimination of toxic substrates from the body (10). Among the genes that are regulated by PXR in the liver and intestine are those coding for CYPs of the 3a (35, 45–47) or 2b (48–50) subfamily, genes encoding phase II enzymes including members of the glutathione S-transferase (51), sulfotransferase (52, 53), UDP-glucuronosyltransferase (54) and carboxylesterase families (55), and genes encoding proteins involved in transport such as multidrug resistance proteins Mdr1 (49, 56) and Mrp2 (57, 58) and the organic anion transport protein 1a4 (Oatp1a4 formerly Oatp2). Members of the OATP family account for Na+-independent bile acid transport into the hepatocyte and also remain candidates for bile acid efflux at the basolateral membrane since Oatp1a1 and -1a4 are able to operate as bidirectional exchangers (14, 57).
Toxicological implications of esterases - From molecular structures to functions
2005, Toxicology and Applied PharmacologyInduction of PXR-mediated metabolism by β-carotene
2005, Biochimica et Biophysica Acta - Molecular Basis of DiseaseDexamethasone-induced methylprednisolone hemisuccinate hydrolase: Its identification as a member of the rat carboxylesterase 2 family and its unique existence in plasma
2005, Biochemical PharmacologyCitation Excerpt :Hattori et al. [19,20] reported that methylprednisolone hemisuccinate (MPHS) was hydrolyzed to methylprednisolone via CES in rat liver microsomes and that several clinically used glucocorticoids, including dexamethasone, caused a remarkable increase in the level of this hydrolytic activity. In contrast to the report of induction of CES activity, some researchers have shown that the level of microsomal p-nitrophenylacetate hydrolase activity was significantly decreased in rat liver microsomes [18,21,22]. This apparent contradiction in the same animals is probably due to the different methods for determination of CES activity by using different CES substrates; thus, it is hypothesized that the CES isozyme contributing to p-nitrophenylacetate hydrolysis in rat liver microsomes is different from the one contributing to MPHS hydrolysis.