Purification and Characterization of Two Rat-Liver Microsomal Carboxylesterases (Hydrolase A and B)

Morgan, E. W.; Yan, Bingfang; Greenway, Denise; Petersen, Dennis R.; Parkinson, Andrew

doi:10.1006/abbi.1994.1531

Cited by 105 publications

(77 citation statements)

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“…Hydrolase A is the most abundant rat hepatic CE (Morgan et al, 1994;Sanghani et al, 2002). The k cat value obtained for deltamethrin hydrolysis by pure rat serum CE (this study) was ϳ2-fold greater than the k cat for hydrolase A (Godin et al, 2006).…”

Section: Discussionmentioning

confidence: 51%

Identification of Rat and Human Cytochrome P450 Isoforms and a Rat Serum Esterase That Metabolize the Pyrethroid Insecticides Deltamethrin and Esfenvalerate

Godin

Crow²,

Scollon³

et al. 2007

Drug Metab Dispos

123

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ABSTRACT:The metabolism of (␣S)-cyano-3-phenoxybenzyl (1R, 3R)-cis-3-(2,2-dibromovinyl)-2,2-dimethylcyclopropane carboxylate (deltamethrin) and (␣S)-cyano-3-phenoxybenzyl 2-(4-chlorophenyl)-3-methylbutyrate (esfenvalerate) by rat and human liver microsomes differs with respect to the biotransformation pathway (oxidation versus hydrolysis) responsible for their clearance. This study aims to further explore the species differences in the metabolism of these chemicals. Using a parent depletion approach, rat and human cytochromes P450 (P450s) were screened for their ability to eliminate deltamethrin or esfenvalerate during in vitro incubations. Rat P450 isoforms CYP1A1, CYP2C6, CYP2C11, and CYP3A2 and human P450 isoforms CYP2C8, CYP2C19, and CYP3A5 were capable of metabolizing either pyrethroid. Human CYP2C9 metabolized esfenvalerate but not deltamethrin. Rat and human P450s that metabolize esfenvalerate and deltamethrin do so with similar kinetics. In addition to the liver, a potential site of metabolic elimination of pyrethroids is the blood via serum carboxylesterase (CE) hydrolysis. The serum of rats, but not humans, contains significant quantities of CE. Deltamethrin and esfenvalerate were metabolized effectively by rat serum and a purified rat serum CE. In contrast, neither pyrethroid was metabolized by human serum or purified human serum esterases (acetylcholinesterase and butyrylcholinesterase). These studies suggest that the difference in rates of oxidative metabolism of pyrethroids by rat and human hepatic microsomes is dependent on the expression levels of individual P450 isoforms rather than their specific activity. Furthermore, these studies show that the metabolic elimination of deltamethrin and esfenvalerate in blood may be important to their disposition in rats but not in humans.

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Section: Discussionmentioning

confidence: 51%

Identification of Rat and Human Cytochrome P450 Isoforms and a Rat Serum Esterase That Metabolize the Pyrethroid Insecticides Deltamethrin and Esfenvalerate

Godin

Crow²,

Scollon³

et al. 2007

Drug Metab Dispos

123

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“…[2][3][4][5][6][7][8][9][10][11][12][13][14] These enzymes efficiently catalyze the hydrolysis of a variety of ester-and amide-containing chemicals as well as drugs and chemicals to the respective free acids. They are also involved in the detoxification or metabolic activation of various drugs, pesticides, environmental toxicants and carcinogens.…”

Section: Mammalian Cesmentioning

confidence: 99%

Carboxylesterases: structure, function and polymorphism in mammals

Satoh

Hosokawa

2010

J. Pestic. Sci.

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“…Mammalian CarbEs are members of an α,β-hydrolase-fold family and are found in various mammalian species (Hosokawa, 1990;Kroetz et al, 1993;Brzezinski et al, 1994;Morgan et al, 1994;Yan et al, 1994;Yan et al, 1995a;Yan et al, 1995b;Yan et al, 1995c;Kusano et al, 1996;Brzezinski et al, 1997;Langmann et al, 1997a;Langmann et al, 1997b;Ellinghaus et al, 1998). It has been suggested that CarbEs can be classified into five major groups denominated from CES1 to CES5, according to the homology of the amino acid sequence (Satoh and Hosokawa, 1998;Satoh and Hosokawa, 2006;Hosokawa et al, 2007), and the majority of CarbEs that have been identified to belong to the CES1 or CES2 family.…”

Section: Introductionmentioning

confidence: 99%

Carboxylesterases: Structure, Function and Polymorphism

Satoh¹,

Hosokawa²

2009

Biomolecules and Therapeutics

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-This review covers current developments in molecular-based studies of the structure and function of carboxylesterases. To allay the confusion of the classic classification of carboxylesterase isozymes, we have proposed a novel nomenclature and classification of mammalian carboxylesterases on the basis of molecular properties. In addition, mechanisms of regulation of gene expression of carboxylesterases by xenobiotics, and involvement of carboxylesterase in drug metabolism are also described.

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Purification and Characterization of Two Rat-Liver Microsomal Carboxylesterases (Hydrolase A and B)

Cited by 105 publications

References 0 publications

Identification of Rat and Human Cytochrome P450 Isoforms and a Rat Serum Esterase That Metabolize the Pyrethroid Insecticides Deltamethrin and Esfenvalerate

Identification of Rat and Human Cytochrome P450 Isoforms and a Rat Serum Esterase That Metabolize the Pyrethroid Insecticides Deltamethrin and Esfenvalerate

Carboxylesterases: structure, function and polymorphism in mammals

Carboxylesterases: Structure, Function and Polymorphism

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