Cocaine and butyrylcholinesterase (BChE): Determination of enzymatic parameters

Mattes, Carol E.; Bradley, Roy M.; Slaughter, Elizabeth; Browne, Susan P.

doi:10.1016/0024-3205(96)00065-3

Cited by 49 publications

(31 citation statements)

References 10 publications

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“…It is the major detoxification enzyme of both natural (-) cocain and unnatural (+) cocain in plasma. The inactive metabolites produced by BChE is ecgonine methyl ester and benzoic acid that are rapidly excreted from circulation by kidney (36,37). Cocain abuse is a medical problem in all around of the world.…”

Section: Cocainementioning

confidence: 99%

Cholinesterase activity as biomarker of neurotoxicity: utility in the assessment of aquatic environment contamination

Jebali¹,

Khedher²,

Sabbagh³

et al. 2013

RGCI

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Butyrylcholinesterase is involved three different enzymatic activities in its structure like its sister enzyme, acetylcholinesterase: esterase, aryl acylamidase and peptidase (or protease). Whereas the clear role of acetylcholinesterase in cholinergic neurotransmission is well defined, the real physiological function of butyrylcholinesterase is still unknown. Both enzymes have similar molecular forms with different tissue distribution. Esteratic activity of butyrylcholinesterase becomes more important in scavenging of organophosphate and carbamate inhibitors before they reach to acetylcholinesterase; in regulating cholinergic transmission in the absence of acetylcholinesterase and in inactivation of some drugs such as cocaine aspirin, amitriptyline or in activation of others such as bambuterol, heroin. It is suggested that aryl acylamidase activity plays a role in crosstalking between seratonergic and cholinergic neurotransmission systems. In addition, peptidase activity of butyrylcholinesterase has a function in the development and progression of Alzheimer disease due to cause the production of β-amyloid protein and to help its diffusion to β-amyloid plaques.

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Section: Cocainementioning

confidence: 99%

Cholinesterase activity as biomarker of neurotoxicity: utility in the assessment of aquatic environment contamination

Jebali¹,

Khedher²,

Sabbagh³

et al. 2013

RGCI

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“…The benzoyl ester of cocaine, heroin and CPT-11 bearing a small acyl moiety and a bulky alcohol group are good substrates for the CES2 isozyme. It was interesting that BuChE hydrolyzed the benzoyl ester of cocaine, and also hydrolyzed CPT-11, but not AChE (Mattes et al, 1996;Lynch et al, 1997;Christopher et al, 1999). CPT-11 is a relatively potent and selective inhibitor of human AChE that has properties of the acute cholinergic toxicity observed in some patients (Dodds and Rivory, 1999).…”

Section: Drug Metabolismmentioning

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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“…It was interesting that BuChE hydrolyzed the benzoyl ester of cocaine, and also hydrolyzed CPT-11, but not AChE. [96][97][98] CPT-11 is a relatively potent and selective inhibitor of human AChE that has properties of the acute cholinergic toxicity observed in some patients. 99) It has been suggested that although these two CE families exhibit broad substrate specificity for ester, carbamate, or amide hydrolysis, these CE isozymes exhibit distinct catalytic efficiencies that correlate with the relative size of the substrate substituents versus that of the enzyme active sites.…”

Section: Possible Role Of Ce Isozymes In Drug Metabolismmentioning

confidence: 99%