Specificity of purified monoacylglycerol lipase, palmitoyl-CoA hydrolase, palmitoyl-carnitine hydrolase, and nonspecific carboxylesterase from rat liver microsomes

Mentlein, Rolf; Suttorp, Meinolf; Heymann, Eberhard

doi:10.1016/0003-9861(84)90064-x

Cited by 106 publications

(55 citation statements)

References 41 publications

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“…Isoelectric focusing of the porcine intestine enzyme showed a single band of pI 5.1 (Fig. 1 C), while isoelectric focusing of porcine liver carboxylesterase led to 13 sharp bands in the 4.8 to 6.0 pH range [22] and five isoenzymes were detected in rat liver CE [23].…”

Section: Molecular Mass Determinationmentioning

confidence: 97%

Purification and molecular cloning of porcine intestinal glycerol‐ester hydrolase

David

Guo

Villard

et al. 1998

European Journal of Biochemistry

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A glycerol-ester hydrolase was purified to homogeneity from porcine intestinal mucosa using a partial delipidation method and an eight-step purification procedure. The isolation scheme used gave a 483-fold purification, resulting in a pure enzyme with a specific activity on tributyrin of 290 µmol · min Ϫ1 · mg Ϫ1 . The molecular mass of the enzyme was estimated at 240 kDa, based on the results of size-exclusion chromatography, and at 60 kDa, as determined by SDS/PAGE analysis. The isoelectric focusing data obtained indicated that only one isoform with a pI of 5.1 was present. Complete identity was found to exist between the N-terminal sequence of the first 25 amino acid residues and that of a porcine liver carboxylesterase. A full-length cDNA coding for the enzyme was isolated from pig small intestine. We observed that the corresponding protein originally named intestinal glycerol-ester hydrolase definitely belongs to the carboxylesterase family. The deduced amino acid sequence consisted of 565 residues and showed 97% identity with that of porcine liver carboxylesterase and more than 50% identity with those of other carboxylesterases from different mammalian species.

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Section: Molecular Mass Determinationmentioning

confidence: 97%

Purification and molecular cloning of porcine intestinal glycerol‐ester hydrolase

David

Guo

Villard

et al. 1998

European Journal of Biochemistry

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“…For example, Mentlein et al used natural substrates to classify rat liver microsomal esterases, 24,25) while others classified esterases based on their mobility on electrophoretic gels, such as aphid esterases E1-E7, 26) and German cockroach esterases E-1 and E-2. 27) Esterases from Culex mosquitoes were classified using combined criteria including preference for hydrolyzing a-or b-naphthyl acetates and electrophoretic mobility.…”

Section: Esterase Classification and Nomenclaturementioning

confidence: 99%

Overview of Carboxylesterases and Their Role in the Metabolism of Insecticides

Shan²,

2005

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Carboxylesterases hydrolyze numerous endogenous and exogenous ester-containing compounds. They play a role in the detoxification of many agrochemicals including pyrethroids, organophosphates, and carbamates. Research on these enzymes is still developing and there are several topics that should be addressed to further investigations in this area. This paper focuses on a number of these issues including enzyme nomenclature, catalytic mechanism, substrate specificity, agrochemical metabolism, role in insecticide resistance and environmental significance. It is expected that carboxylesterase research will increase with specific emphasis on isozyme and substrate identification. Future research directions are discussed and the current state of the field is evaluated.

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“…Accordingly, pharmacological inhibition of MGL leads to 2-AG accumulation in neural tissue and enhances its cannabimimetic effects (Makara et al, 2005). Additional enzymes have been shown to metabolize 2-AG, including cyclooxygenase (COX), lipooxygenase (LOX), DGL, and FAAH (Mentlein et al, 1984;Somma-Delpéro et al, 1995;Goparaju et al, 1998;Kozak et al, 2000;Dinh et al, 2004). Because 2-AG degradation appears to be complex and involve multiple enzymes and could vary between cell types, we sought to compare 2-AG hydrolysis in neurons and microglia.…”

Section: Introductionmentioning

confidence: 99%

Identification of a Novel Endocannabinoid-Hydrolyzing Enzyme Expressed by Microglial Cells

Muccioli¹,

Xu²,

Odah³

et al. 2007

J. Neurosci.

161

159

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The endocannabinoids (eCBs) anandamide and 2-arachidonoyl glycerol (2-AG) are inactivated by a two-step mechanism. First, they are carried into cells, and then anandamide is hydrolyzed by fatty acid amide hydrolase (FAAH) and 2-AG by monoacylglycerol lipase (MGL). Here we provide evidence for a previously undescribed MGL activity expressed by microglial cells. We found that the mouse microglial cell line BV-2 does not express MGL mRNA and yet efficiently hydrolyzes 2-AG. URB597 (3Ј-carbamoyl-biphenyl-3-ylcyclohexylcarbamate) reduces this hydrolysis by 50%, suggesting the involvement of FAAH. The remaining activity is blocked by classic MGL inhibitors [[1,1-biphenyl]-3-yl-carbamic acid, cyclohexyl ester (URB602) and MAFP (methylarachidonyl fluorophosphate)] and is unaffected by inhibitors of COXs (cyclooxygenases), LOXs (lipooxygenases), and DGLs (diacylglycerol lipases), indicating the involvement of a novel MGL activity. Accordingly, URB602 leads to selective accumulation of 2-AG in intact BV-2 cells. Although MGL expressed in neurons is equally distributed between the cytosolic, mitochondrial, and nuclear fractions, the novel MGL activity expressed by BV-2 cells is enriched in mitochondrial and nuclear fractions. A screen for novel inhibitors of eCB hydrolysis identified several compounds that differentially block MGL, FAAH, and the novel MGL activity. Finally, we provide evidence for expression of the novel MGL by mouse primary microglia in culture. Our results suggest the presence of a novel, pharmacologically distinct, MGL activity that controls 2-AG levels in microglia.

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Specificity of purified monoacylglycerol lipase, palmitoyl-CoA hydrolase, palmitoyl-carnitine hydrolase, and nonspecific carboxylesterase from rat liver microsomes

Cited by 106 publications

References 41 publications

Purification and molecular cloning of porcine intestinal glycerol‐ester hydrolase

Purification and molecular cloning of porcine intestinal glycerol‐ester hydrolase

Overview of Carboxylesterases and Their Role in the Metabolism of Insecticides

Identification of a Novel Endocannabinoid-Hydrolyzing Enzyme Expressed by Microglial Cells

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