Cloning and nucleotide sequence of a novel, male-predominant carboxylesterase in mouse liver

Aida, Kaoru; Moore, Rickie; Negishi, Masahiko

doi:10.1016/0167-4781(93)90093-s

Cited by 32 publications

(16 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It is noteworthy that both BNF and TCDD suppressed mouse liver Ces3a expression, and the TCDD-mediated suppression of Ces3a expression was AhR-dependent. Ces3a (or Es31) is expressed predominantly in male mouse livers (Aida et al, 1993). There is little information on the substrate specificity of CES3/Ces3a.…”

Section: Discussionmentioning

confidence: 99%

“…The purpose of the present study was to investigate systematically the regulation of Cess in livers of mice by prototypical MEIs that activate five transcription factors. The present study focused on one mouse Aadac gene and 11 mouse Ces genes that were investigated previously, including Ces1c (previously termed Es1) (Genetta et al, 1988), Ces1d (previously Ces3) (Dolinsky et al, 2001), Ces1e (previously Es22 or egasyn) (Ovnic et al, 1991), Ces1f (previously Es4 or TGH-2) (Poole et al, 2001), Ces1g (previously Ces1 or Est1) (Ellinghaus et al, 1998), Ces2a (previously Ces6) (Gerhard et al, 2004), Ces2b (previously Ces2A7) (Satoh and Hosokawa, 2006), Ces2c (previously Ces2) (Furihata et al, 2003), Ces2e (previously Ces5) (Gerhard et al, 2004), Ces3a (previously esterase 31 or Est31) (Aida et al, 1993), and Ces5a (previously Ces7) (Miyazaki et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Transcription Factor-Mediated Regulation of Carboxylesterase Enzymes in Livers of Mice

Zhang

Cheng²,

Aleksunes³

et al. 2012

Drug Metab Dispos

View full text Add to dashboard Cite

ABSTRACT:The induction of drug-metabolizing enzymes by chemicals is one of the major reasons for drug-drug interactions. In the present study, the regulation of mRNA expression of one arylacetamide deacetylase (Aadac) and 11 carboxylesterases (Cess) by 15 microsomal enzyme inducers (MEIs) was examined in livers of male C57BL/6 mice. The data demonstrated that Aadac mRNA expression was suppressed by three aryl hydrocarbon receptor (AhR) ligands, two constitutive androstane receptor (CAR) activators, two pregnane X receptor (PXR) ligands, and one nuclear factor erythroid 2-related factor 2 (Nrf2) activator. Ces1 subfamily mRNA expression was not altered by most of the MEIs, whereas Ces2 subfamily mRNA was readily induced by the activators of CAR, PXR, and Nrf2 but not by peroxisome proliferator-activated receptor ␣ activators.Studies using null mice demonstrated that 1) AhR was required for the 2,3,7,8-tetrachlorodibenzo-p-dioxin-mediated suppression of Aadac and Ces3a; 2) CAR was involved in the 1,4-bis[2-(3,5-dichloropyridyloxy)]benzene-mediated induction of Aadac, Ces2c, Ces2a, and Ces3a; 3) PXR was required for the pregnenolone-16␣-carbonitrile-mediated induction of Aadac, Ces2c, and Ces2a; 4) Nrf2 was required for the oltipraz-mediated induction of Ces1g and Ces2c; and 5) PXR was not required for the DEX-mediated suppression of Cess in livers of mice. In conclusion, the present study systematically investigated the regulation of Cess by MEIs in livers of mice and demonstrated that MEIs modulated mRNA expression of mouse hepatic Cess through the activation of AhR, CAR, PXR, and/or Nrf2 transcriptional pathways.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Transcription Factor-Mediated Regulation of Carboxylesterase Enzymes in Livers of Mice

Zhang

Cheng²,

Aleksunes³

et al. 2012

Drug Metab Dispos

View full text Add to dashboard Cite

show abstract

“…47) CES3 includes ES-male (CES3A2) and human CES3 (CES3A1). 48,49) Human CES3 (CES3A1) has about 40% amino acid sequence identity with both CEA1A1 and CES2A1, and is expressed in the liver and gastrointestinal tract at an extremely low level in comparison with CES1A1 and CES2A1. 49) The CES4 family includes CE-like urinary excreted protein (CAUXIN) (CES4A2), which is excreted as a major urinary protein in cat urine.…”

Section: Novel Classification and Nomenclature Of Mammalian Cesmentioning

confidence: 99%

Carboxylesterases: structure, function and polymorphism in mammals

Satoh

Hosokawa

2010

J. Pestic. Sci.

View full text Add to dashboard Cite

“…It includes human intestinal CarbE (CES2A1) (Schwer et al, 1997;Humerickhouse et al, 2000;Imai et al, 2006;Taketani et al, 2007;Yang et al, 2007;Shi et al, 2008), rCES2 (CES2A10) (Furihata et al, 2005), rat intestinal CarbE RL4 (rCES2) (CES2A6) (Furihata et al, 2003), rabbit form 2 (Ozols, 1989) and hamster AT51 (CES2A11) (Sone et al, 1994). CES3 includes ES-male (CES3A2) and human CES3 (CES3A1) (Aida et al, 1993;Sanghani et al, 2004). Human CES3 (CES3A1) has about 40% amino acid sequence identity with both CEA1A1 and CES2A1, and is expressed in the liver and gastrointestinal tract at an extremely low level in comparison with CES1A1 and CES2A1 (Sanghani et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Carboxylesterases: Structure, Function and Polymorphism

Satoh¹,

Hosokawa²

2009

Biomolecules and Therapeutics

View full text Add to dashboard Cite

-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.

show abstract

Cloning and nucleotide sequence of a novel, male-predominant carboxylesterase in mouse liver

Cited by 32 publications

References 16 publications

Transcription Factor-Mediated Regulation of Carboxylesterase Enzymes in Livers of Mice

Transcription Factor-Mediated Regulation of Carboxylesterase Enzymes in Livers of Mice

Carboxylesterases: structure, function and polymorphism in mammals

Carboxylesterases: Structure, Function and Polymorphism

Contact Info

Product

Resources

About