Comparison of butyrylcholinesterase and acetylcholinesterase

Chatonnet, Arnaud; Lockridge, Oksana

doi:10.1042/bj2600625

Cited by 507 publications

(276 citation statements)

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“…BChE is also enriched in liver and heart, whereas AChE is particularly represented in skeletal muscles and blood cells ([ll, 121, review in [3]). Qualitative and quantitative distribution of BChE and AChE, reported in the literature, might be revised in some cases because of the variations in substrate and inhibitor specificities of BChE in different species and possible contamination of organs by serum and blood cells.…”

mentioning

confidence: 99%

Acetylcholinesterase and Butyrylcholinesterase Expression in Adult Rabbit Tissues and During Development

Jbilo¹,

L'Hermite²,

Talesa

et al. 1994

European Journal of Biochemistry

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A large cDNA fragment covering the complete sequence of the mature catalytic subunit of rabbit acetylcholinesterase (AChE) has been cloned and sequenced. This sequence was compared to that of rabbit butyrylcholinesterase [BChE;Jbilo, 0. & Chatonnet, A. (1990) Nucleic Acids Res. 18, 39901. Amino acid sequences of AChE and BChE have 51% identity. They both possessed a choline-binding site W84, a catalytic triad S200-H440-E327 and six cysteine residues (positions 67 -94, 254-265, 402-521) in conserved sequence positions to those that form three intrachain disulfide bonds in all cholinesterases (by convention, numbering of amino acids is that used for Torpedo AChE). Rabbit AChE had a larger number of aromatic residues lining the active-site gorge than rabbit BChE (14 compared to 8, respectively) and a smaller number of potential N-glycosylation sites (3 compared to 8, respectively). Both catalytic subunits have a hydrophilic C-terminus (catalytic subunits of type T). Expression of acetycholinesterase and butyrylcholinesterase genes (ACHE and BCHE) was studied in rabbit tissues and during development by a correlation of Northern-blot analysis and enzymic activities. This correlation was rendered difficult by the presence of an eserineresistant esterase active on butyrylthiocholine in serum, liver and lung. When the contribution of this carboxylesterase was taken into account, brain was found as the richest source of BChE followed by lung and heart. Rabbit liver had a very low content of BChE that correlated with the low BChE activity in plasma. During development, BCHE transcripts were detected as early as day 10 post coitum, whereas ACHE transcripts appeared only on day 12.Acetylcholinesterase belongs to a large family of proteins with conserved overall structure [l]. Functions of those proteins range from cell adhesion (as exemplified by glutactin and neurotactin) to detoxification (as liver carboxylesterases) and to the rapid hydrolysis of acetylcholine and other choline esters (cholinesterases). In vertebrates, two related enzymes : acetylcholinesterase (ACE) and butyrylcholinesterase (BChE) are able to hydrolyze acetylcholine and are inhibited by 0.01 mM eserine. Both enzymes present the same molecular forms, including globular and asymmetric molecules (reviews in [2, 31). The mechanisms of choline ester hydrolysis are basically the same in both enzymes [4] ; the substrate is directed to the bottom of a deep gorge by a series of aromatic Abbreviations. AChE and BChE, acetylcholinesterase and butyrylcholinesterase enzymes ; ACHE and BCHE, genes encoding AChE and BChE; Brij 96, 10-oleylether; Iso-OMPA, tetranionoisopropylpyrophosphortetramide; LS, LSB, HS and HSB, low salt, low-salt Brij, high salt and high-salt Brij buffers.

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confidence: 99%

Acetylcholinesterase and Butyrylcholinesterase Expression in Adult Rabbit Tissues and During Development

Jbilo¹,

L'Hermite²,

Talesa

et al. 1994

European Journal of Biochemistry

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“…It should be stressed that P AChE activity does not always relate to the severity of poisoning but it can be used as a sensitive marker of exposure to OP or carbamate compounds. 8 Many studies have stressed the importance of plasma cholinesterase levels for monitoring OP poisoning. 9,10,11,12 It has been proved that the effect of OP poisoning occurs early and is more marked in plasma cholinesterase than in red cell cholinesterase.…”

Section: Discussionmentioning

confidence: 99%

Cholinesterase Activity in Health Workers Involved in Handling and Spraying of Organophosphorous Insecticides

Madaan

Ghalaut

Sachdeva

et al. 2011

Int J Med Public Health

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humans, they are responsible for acute poisonings as well as for long term health effects, including cancer and adverse effects on reproduction. Therefore, it is very essential to balance needs with environment and health issues, when using insecticide and pesticide. The vast majority of insecticides targeted at insects, arthropods and nematodes are neurotoxic. They are capable of exerting a broad range of effects that ultimately results in mortality. At the whole organism level the insecticide effect may be either neuroexcitatory leading to hyperactivity, tremors and rigid paralysis or neuroinhibitory causing immobility and flaccid paralysis. 2 Organophosphates and Carbamates are, nowadays, widely used as insecticides and have been considered as potential chemical warfare agents. As an insecticide they are used widely for agriculture, vector control and domestic purpose. 3 Household and agricultural products containing Organophosphorous (OP) pesticides are widely prevalent eg. insecticidal preparations and fertilizers for gardens, surface and room sprays, baits for cockroaches and other insects, shampoos against lice, pet preparations etc. In INTRODUCTIONAn insecticide is a pesticide used against insects in all developmental forms. They may be natural or synthetic chemicals and may act either as ovicide, larvicide or a contact insecticide. The age of chemical insecticides began about 2000 years ago, with the use of natural products like pyrethrum and tobacco. Synthetic insecticides were introduced in 1940 with chemicals like Dichlorophenyl Trichloroethane (DDT). 1 In the present times insecticides are widely used in agriculture, medicine, industry and household. In fact, the boon of agricultural productivity of the present time is partly due to the availability of potent and effective insecticides. But, nearly all insecticides have potential to significantly alter ecosystem; many are toxic to humans and others are concentrated in the food chain. In Cholinesterase Activity in Health WorkersInvolved a B S t r a c tBackground: recent era of agricultural boon is partially the result of extensive use of insecticides and pesticides. But these compounds also have potential to significantly alter the ecosystem and can cause acute poisonings as well as long term detrimental health effects in humans. these compounds can cause toxicity through all routes of exposure. they exert their effect mainly by the inhibition of acetylcholinesterase (ache), which functions by removing acetylcholine (ach) from its postsynaptic receptors. Aims and Objectives: Human exposure to organophosphorous (oP) pesticides can develop lowered cholinesterase levels. the aim of the present study was to estimate the plasma levels of ache in personnel involved in handling of these compounds, during the period of active spraying operations. Methodology: the present study was conducted on 38 subjects working as Multipurpose Health Workers (MPHW groUP-1) and Field Workers (FW groUP-2) involved in the actual spraying of the insecticides, in District roht...

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“…BuChE inhibition was measured in vitro using a modification of the Ellman assay [7] employing butyrylthiocholine as substrate [8] and a standardized BuChE concentration (5.88 mol min −1 ml −1 ). Plasma was removed from fresh blood centrifuged at 3000 rpm for 10 min at 4°C (Sorvall RT6000B).…”

Section: In Vitro Butyrylcholinesterase Inhibitionmentioning

confidence: 99%

Pharmacological effects of a novel isosorbide-based butyrylcholinesterase inhibitor

Khan¹,

Gilmer²,

Carolan³

et al. 2008

Chemico-Biological Interactions

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Isosorbide-2-benzylcarbamate-5-benzoate, a novel butyrylcholinesterase inhibitor, shows interspecies variation in its inhibitory activity (IC 50 of 4.3 nM for human plasma butyrylcholinesterase, but 1.09 M for mouse plasma butyrylcholinesterase). Stability studies revealed that this drug is resistant to hydrolysis by human plasma (no degradation in 1 h). However, it was found to undergo rapid degradation when incubated with mouse plasma or mouse liver homogenate, yielding benzyl carbamate and benzoic acid. The addition of the carboxylesterase inhibitor bis-(4-nitrophenyl) phosphate (BNPP) inhibited the degradation of the novel drug, indicating that it may be a substrate for both butyrylcholinesterase and carboxylesterase. The absence of carboxylesterase from human plasma explains the drug's stability in this medium. In vivo, pharmacodynamic studies on single doses of 1 mg/kg to naïve male C57BL/6 mice revealed maximal plasma butyrylcholinesterase inhibition 20 min after intraperitoneal administration (~60% inhibition) and 1 h after administration by gavage (~45% inhibition). While this plasma butyrylcholinesterase inhibition was short-lived, the drug also penetrated the blood-brain barrier resulting in a slight (10-15%) but persistent (≥72 h) reduction in brain butyrylcholinesterase activity.

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Comparison of butyrylcholinesterase and acetylcholinesterase

Cited by 507 publications

References 107 publications

Acetylcholinesterase and Butyrylcholinesterase Expression in Adult Rabbit Tissues and During Development

Acetylcholinesterase and Butyrylcholinesterase Expression in Adult Rabbit Tissues and During Development

Cholinesterase Activity in Health Workers Involved in Handling and Spraying of Organophosphorous Insecticides

Pharmacological effects of a novel isosorbide-based butyrylcholinesterase inhibitor

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