Acetylcholinesterase, comparative

S. Andreescu, A. Avramescu, C. Bala, V. Magearu and J.-L. Marty, Detection of organophosphorus insecticides with immobilised acetylcholinesterase—comparative study of two enzyme sensors, Anal. Bioanal. Chem., 374 (2002) 39-45. 

Kuca, K., Jun, D., Cabal, J., Hrabinova, M., Bartosova, L., Opletalova, V. (2006). Russian VX inhibition and reactivation of acetylcholinesterase compared with VX agent. Basic Clin. Pharmacol. Toxicol. 98 389-94. 

Andreescu S, Avramescu A, Bala C, Magearu V, Marty JL (2002) Detection of organophos-phorus insecticides with immobilized acetylcholinesterase comparative study between two enzyme smsms. Anal Bioanal Chem 74 39-45... 

SJ Cho, ML Garsia, J Bier, A Tropsha. Stracture-based alignment and comparative molecular held analysis of acetylcholinesterase inhibitors. J Med Chem 39(26) 5064-5071, 1996. 

Compounds that affect activities of hepatic microsomal enzymes can antagonize the effects of methyl parathion, presumably by decreasing metabolism of methyl parathion to methyl paraoxon or enhancing degradation to relatively nontoxic metabolites. For example, pretreatment with phenobarbital protected rats from methyl parathion s cholinergic effects (Murphy 1980) and reduced inhibition of acetylcholinesterase activity in the rat brain (Tvede et al. 1989). Phenobarbital pretreatment prevented lethality from methyl parathion in mice compared to saline-pretreated controls (Sultatos 1987). Pretreatment of rats with two other pesticides, chlordecone or mirex, also reduced inhibition of brain acetylcholinesterase activity in rats dosed with methyl parathion (2.5 mg/kg intraperitoneally), while pretreatment with the herbicide linuron decreased acetylcholine brain levels below those found with methyl parathion treatment alone (Tvede et al. 1989). 

Banks, A. and Russell, R.W. (1967). Effects of chronic reductions in acetylcholinesterase activity on serial problem-solving. Journal of Comparative Physiology and Psychology 64, 262-267. 

Sandahl, J.F, Baldwin, D.H., and Jenkins, J.J. et al. (2005). Comparative thresholds for acetylcholinesterase inhibition and behavioural impairment in Coho Salmon exposed to chlorpyriphos. Environmental Toxicology and Chemistry 24, 136-145. 

Donepezil is a piperidine cholinesterase inhibitor, which reversibly and non-competitively inhibits centrally active acetylcholinesterase 34 This specificity is claimed to result in fewer peripheral side effects as compared to the other ChE inhibitors. 

S. Andreescu, L. Barthelmebs, and J.L. Marty, Immobilization of acetylcholinesterase on screen-printed electrodes comparative study between three immobilization methods and applications to the detection of organophosphorus insecticides. Anal. Chim. Acta 464, 171—180 (2002). 

P.R.B. de O Marques, G.S. Nunes, T.C.R. dos Santos, S. Andreescu, and J.L. Marty, Comparative investigation between acetylcholinesterase obtained from commercial sources and genetically modified Drosophila melanogaster application in amperometric biosensors for methamidophos pesticide detection. Biosens. Bioelectron. 20, 825-832 (2004). 

Guanaranta and Wilson [111] compared the different methods for immobilization of acetylcholinesterase by direct immobilization on the matrix, introduction of 1,6 diaminohexane as a spacer, and two methods of oriented immobilization via antibody and avidin-biotin linkage. They found that the latter gave the best efficiency, i. e., tenfold higher than direct immobilization on the matrix (which was the lowest) followed by immobilization on the antibody and immobilization using a spacer. Details about the biotin-avidin technology were published by Wilchek and Bayer [112]. 

N-methylscopolamine (Costa et al. 1982b Schwab et al. 1983). Animals made tolerant to disulfoton were resistant to the lethal or adverse effects of cholinergic agonists, such as carbachol (Brodeur and DuBois 1964 Costa et al. 1981 Schwab and Murphy 1981) and oxotremorine (Costa et al. 1982b McPhillips 1969a), which are not hydrolyzed by acetylcholinesterase. Tissues from animals tolerant to disulfoton such as the ilea (Foley and McPhillips 1973 McPhillips 1969b McPhillips and Dar 1967) and the atria (Perrine and McPhillips 1970 Schwab et al. 1983), were resistant to the effects of carbachol and/or oxotremorine. Because the uterus and vas deferens have a relatively sparse parasympathetic innervation compared to the ileum and do not receive a steady flow of impulses via this system, these tissues were not as subsensitive to carbachol as the ileum (Foley and McPhillips 1973). Thus, acetylcholine accumulation may be a prerequisite for tolerance development. 

HPMA copolymers are water-soluble biocompatible polymers, widely used in anticancer drug delivery (reviewed in Reference [22]). HPMA copolymers containing reactive groups at side-chain termini were previously used for the modification of trypsin [23], chymotrypsin [23,24], and acetylcholinesterase [25]. The modification dramatically increased the acetylcholinesterase survival in the blood stream of mice and the thermostability of modified enzymes when compared to the native proteins. However, the modification involved multipoint attachment of the copolymers to the substrates, which may cause crosslinking. To modify proteins or biomedical surfaces by one point attachment, semitelechelic polymers should be used. 

Cho, S. J. Garsia, M. L. Bier, J. Tropsha, A. Structure-based alignment and comparative molecular field analysis of acetylcholinesterase inhibitors. J. Med. Chem. 1996, 39, 5064-5071. 

Comparative Toxicokinetics. Diazinon, an anticholinesterase organophosphate, inhibits acetylcholinesterase in the central and peripheral nervous system resulting in cholinergic symptoms, in some... 

Davies DB, Holub BJ. 1983. Comparative effects of organophosphorus insecticides on the activities of acetylcholinesterase, diacylglycerol kinase, and phosphatidylinositol phosphodiesterase in rat brain microsomes. Pesti Biochem Physiol 20 92-99. 

Physostigmine, an acetylcholinesterase inhibitor widely used in treatment of glaucoma. Compare with other carbamate esters (Box 12-E)... 

Acetylcholinesterase was immobilised by entrapment into a PVA-SbQ matrix (see experimental details in Refs. [88,95]). The need of polymer hydration slightly increases the response times, when compared to other immobilisation techniques. Nevertheless, the entrapment presents the advantage of providing biosensors with longer lifetimes due to the protective effect of the polymer matrix. 

The developed biosensor was applied to the analysis of cyanobacterial bloom samples from freshwater lakes of Spain, Greece, France, Scotland and Denmark. Two samples from Scotland and one from Denmark irreversibly inhibit the acetylcholinesterase. The estimated concentrations were between 1.5 and 30nmol/g of dry weight, values extremely high when compared to the intraperitoneal 50% lethal dose of anatoxin-a(s) in mice (121 nmol/kg). 

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