Simultaneous purification and comparative characterization of six serine hydrolases from rat liver microsomes

Mentlein, Rolf; Heiland, Stefan; Heymann, Eberhard

doi:10.1016/0003-9861(80)90386-0

Cited by 151 publications

(86 citation statements)

References 30 publications

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“…CarbEs show ubiquitous tissue expression profiles with the highest levels of CarbE activity present in liver microsomes in many mammals (Mentlein et al, 1980;Hosokawa et al, 1984;Maki et al, 1991;Hattori et al, 1992;Hosokawa and Satoh, 1993;Watanabe et al, 1993;Hosokawa et al, 1995;Derbel et al, 1996;Lehner et al, 1999;Furihata et al, 2004a). CarbEs are categorized as phase 1 drug metabolizing enzymes that can hydrolyze a variety of ester-containing drugs and prodrugs.…”

Section: Drug Metabolismmentioning

confidence: 99%

“…They are involved in detoxification or metabolic activation of various drugs, pesticides, environmental toxicants and carcinogens. CarbEs also catalyze the hydrolysis of endogenous compounds such as shortand long-chain acyl-glycerols, long-chain acyl-carnitine, and long-chain acyl-CoA esters (Mentlein et al, 1980;Hosokawa, 1990;Maki et al, 1991;Hosokawa and Satoh, 1996;Hosokawa et al, 2001;Furihata et al, 2004a;Furihata et al, 2004b;Furihata et al, 2005). We have reviewed the characteristics of CarbEs in relation to the metabolism of xenobiotics Satoh and Hosokawa, 1998;Satoh and Hosokawa, 2006;Hosokawa et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Drug Metabolismmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Carboxylesterases: Structure, Function and Polymorphism

Satoh¹,

Hosokawa²

2009

Biomolecules and Therapeutics

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“…CE show ubiquitous tissue expression profiles with the highest levels of CE activity present in liver microsomes in many mammals. [15][16][17]20,52,74,[75][76][77][78][79] CEs are categorized as phase 1 drug-metabolizing enzymes that can hydrolyze a variety of ester-containing drugs and prodrugs. These include angiotensin-converting enzyme (ACE) inhibitors (temocapril, cilazapril, quinapril, and imidapril), 20,38,80,81) anti-tumor drugs (CPT-11 and capecitabin), 37,41,49,[82][83][84][85][86] and narcotics (cocaine, heroin and meperidine).…”

Section: Possible Role Of Ce Isozymes In Drug Metabolismmentioning

confidence: 99%

“…Carboxylesterases catalyze the hydrolysis of endogenous compounds, such as short-and long-chain acylglycerols, long-chain acyl-carnitine, and long-chain acyl-CoA esters. 2,[15][16][17][18][19][20][21][22] We have reviewed the characteristics of CEs in relation to the metabolism of xenobiotics. [23][24][25][26] Multiple isozymes of hepatic microsomal CE exist in various animal species [27][28][29] and some of these isozymes are involved in the metabolic activation of certain carcinogens, as well as being associated with hepatocarcinogenesis.…”

Section: Mammalian Cesmentioning

confidence: 99%

Carboxylesterases: structure, function and polymorphism in mammals

Satoh

Hosokawa

2010

J. Pestic. Sci.

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“…Chicken microsomal esterases were purified mainly following a procedure described for rat liver [22]. Liver homogenate was centrifuged at 5000 g and 27 000 g to remove nuclear and mitochondria1 fractions, respectively.…”

Section: Methodsmentioning

confidence: 99%

Purification of a 60‐kDa Protein from Chicken Liver Associated with the Internal Nuclear Matrix and Closely Related to Carboxylesterases

Altieri¹,

Maras²,

Ferraro³

et al. 1996

European Journal of Biochemistry

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A 60-kDa protein was purified from chicken liver internal nuclear matrix and its nuclear localization was confirmed by immunofluorescence analysis. Structural information acquired from sequence analysis of the intact protein and of fragments obtained from enzymatic and chemical cleavages strongly suggests that it belongs to the carboxylesterases family, even if with some very peculiar features. The N-terminal sequence of the 60-kDa protein is completely different from the other carboxylesterases, but is similar to a region that is normally internal to all mammalian esterase sequences and localized after the serine residue at the active site. This suggests that the protein may be derived from a gene duplication and/or rearrangement. Since the 60-kDa protein shows a low esterase activity of about 0.2 pmol . min-' . mg-' using either p-nitrophenyl acetate or p-nitrophenyl butyrate as substrates, it is not possible to rule out that the protein shares only a sequence similarity with carboxylesterases and is not a true esterase. Otherwise it could be an esterase which has developed different properties, i.e. a special substrate specificity, the requirement of additional factors or a different stability in solution. In the latter case, this protein could be related to the physiological control of hydrolysis of exogenous and endogenous esters which can act on nuclear functions and/or metabolism.Keywords: nuclear matrix proteins ; carboxylesterase; protein purification.The understanding of many important functions concerning the expression and regulation of the eukaryotic genome needs a better knowledge of the arrangement of nuclear components and the way in which they interact to form the complex architecture of the cell nucleus. The nuclear matrix is a residual structure that has been isolated from a variety of eukaryotic cells and consists mainly of the nuclear lamina, residual nucleoli and a proteinaceus network that is in contact with segments of nuclear DNA [l -41. Considerable experimental evidence suggests that the nuclear matrix plays an important role in the organization and function of the nucleus. Processes like replication, transcription, RNA splicing and DNA loop attachment are associated with the nuclear matrix (4-61. Moreover, hormone receptor function, transcription factors and various enzymatic activities are localized at the nuclear matrix level (4, 6-81, Nuclear matrix proteins have been widely investigated and it has been observed that their composition is tissue-specific and varies during cell differentiation and between normal and transformed cell types [9-121. Several proteins associated with the nuclear matrix have been identified and characterized [ Abbreviufzons PhMeSO,F, phenylmethylsulfonyl fluoride; NaWP,, phosphate-buffered saline; M60k, a 60-kDa protein purified from chicken liver internal nuclear mairix. make contacts with both cytoskeletal proteins and chrmiatin [18, 191. Considering the complexity and the importance of the nuclear matrix, we have developed procedures to purify sing...

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Simultaneous purification and comparative characterization of six serine hydrolases from rat liver microsomes

Cited by 151 publications

References 30 publications

Carboxylesterases: Structure, Function and Polymorphism

Carboxylesterases: Structure, Function and Polymorphism

Carboxylesterases: structure, function and polymorphism in mammals

Purification of a 60‐kDa Protein from Chicken Liver Associated with the Internal Nuclear Matrix and Closely Related to Carboxylesterases

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