Identification carboxylesterase

R. Mentlein, A. Ronai, M. Robbi, E. Heymann, O. von Deimling, Genetic Identification of Rat Liver Carboxylesterases Isolated in Different Laboratories , Biochim. Biophys. Acta 1987, 913, 27-38. 

B. Ab, T. Imamura, Characteristics Of Rat Lung Carboxylesterases/Amidases , Proc. West. Pharmacol. Soc. 1985, 28, 319-322 B. Ab, S. Kaur, Mammaban Tissue Acet-ylsabcybc Acid Esterase(s) Identification, Distribution and Discrimination from Other Esterases , J. Pharmacol. Exp. Then 1983, 226, 589 - 594. 

Mentlein, R., Ronai, A., Robbi, M., Heymann, E., Deimling. O.V. (1987). Genetic identification of rat liver carboxylesterases isolated in different laboratories. Biochim. Biophys. Acta 913 27-38. 

Wadkins RM, Hyatt JL, Wei X, Yoon KJ, Wierdl M, Edwards CC, et al. Identification and characterization of novel benzil (diphenylethane-l,2-dione) analogues as inhibitors of mammalian carboxylesterases. J Med Chem 2005 48 2906-15. 

Metabolism also plays a critical role in the pharmacology of cocaine. The rapid hydrolysis of cocaine via two different pathways leads to its rapid inactivation/detoxification. This rapid metabolism has been a major determinant in the methods and modes of cocaine abuse. Identification and characterization of these hydrolytic enzymes would be useful in that selective induction of these enzymes offers a potential treatment strategy for dealing with cocaine overdose. It is conceivable that long-term elevation of the enzyme or enzymatic activity could be used in conjunction with maintenance therapy for cocaine addicts. Hydrolases or esterases are also responsible for the transesterfication of cocaine. The pharmacological effect of cocaine is prolonged and enhanced when cocaine is used in conjunction with ethanol. A carboxylesterase catalyzes an ethyl transeterification of cocaine to cocaethylene, which is biologically active. 

Tabata, T Katoh, M., Tokudome, S., Nakajima, M., and Yokoi, T. (2(XH) Identification of the cytosolic carboxylesterase catalyzing the 5 -deoxy-5-fluorocytidine formation from capecitabine in human liver. Drug Metab. Dispos. 32, 1103-1110. 

The methods for determination of blood cholinesterases inhibition (AChE and BuChE) do not allow identification of the OP and do not provide reliable evidence for exposure at inhibition levels less than 20%. Moreover, they are less suitable for retrospective detection of exposure due to de novo synthesis of enzymes. A method has been developed which is based on reactivation of phosphylated cholinesterase and carboxylesterase (CaE) by fluoride ions. Treatment of the inhibited enzyme with fluoride ions can inverse the inhibition reaction, yielding a restored enzyme and a phos-phofluoridate which is subsequently isolated and quantified by gas chromatography and phosphorus-specific or mass spectrometric detection (Dll, Pll). Human (and monkey) plasma does not contain CaE but its BuChE concentration is relatively high [70-80 nM (M25, D8)], much higher than the concentration of AChE in blood [ca. 3 nM (H5)]. The plasma of laboratory animals, such as rats and guinea pigs, contains considerable concentrations... 

Stok JE, Huang H, Jraies PD, Wheelock CE, Morisseau C, Hammock BD (2004) Identification, expression, and purification of a pyrethroid-hydrolyzing carboxylesterase from mouse liver microsomes. J Biol Chem 279 29863-29869... 

Wester RC, Bucks DAW, Maibach HI (1994) Human in vivo percutaneous absorption of pyrethrin and piperonyl butoxide. Food Chem Toxicol 32 51-53 Wheelock CE, Wheelock AM, Zhang R, Stok JE, Morisseau C, Le Valley SE (2003) Evaluation of alpha-cyanoesters as fluorescent substrates for examining intraindividual variation in general and pyrethroid-selective esterases in human liver microsomes. Anal Bioehran 315 208—222 Wheelock CR, Miller JL, Miller MJ, Phillips BM, Huntley SA, Gee SJ, Tjeerdem RS, Hammock BD (2006) Use of carboxylesterase activity to remove pyrethroid-associated toxicity to Ceiiodaphnia dubia and Hyalella azteca toxicity in identification evaluations. Environ Toxicol Chem 25 973-984... 

Jewell, W.T., Miller, M.G., 1998. Identification of a carboxylesterase as the major protein bound by molinate. Toxicol. Appl. Pharmacol. 149, 226-234. 

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