Vertebrate Cholinesterases: Structure and Types of Interaction

Massoulié, Jean; Toutant, Jean‐Pierre

doi:10.1007/978-3-642-73220-1_8

Cited by 76 publications

(40 citation statements)

References 258 publications

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“…In particular, a similar inhibition pattern was reported for a membrane-linked cholinesterase from the earthworm Eiseniu jbetida (Stenersen, 1980). The inhibition by excess of AcSCho, shown by a, p and y cholinesterase from D. veneta, also present in enzymes from other Annelida (Stenersen, 1980;Talesa et al, 1995a), is believed to be a distinctive feature of the acetylcholinesterases (Silver, 1974;MassouliC and Toutant, 1988). Moreover, the lower inhibition of y cholinesterase compared with a and forms again suggests differences in the active-site structure and may be due to a more extensive binding of AcSCho molecules to the active site of the acyl-y-enzyme intermediate (Rosenberry, 1975).…”

Section: B Vncsupporting

confidence: 56%

“…The presence of a soluble monomeric acetylcholinesterase showing higher inhibitor sensitivity than a dimeric form was recently observed in the annelid Hirudo medicinalis (Talesa et al, 1995a). The marked sensitivity of a and p cholinesterase towards BW284c51, together with the absence of inhibition by iso-OMPA, are typical features of acetylcholinesterases (Silver, 1974;MassouliC and Toutant, 1988).…”

Section: B Vncmentioning

confidence: 85%

“…In addition, BW284c51 and iso-OMPA were also used, since they are commonly believed, at least for Vertebrata, to be specific inhibitors of acetylcholinesterases and butyrylcholinesterases, respectively (Silver, 1974;MassouliC and Toutant, 1988). Inhibitor concentrations in the range of 1 mM to 1 nM were used in the assay and residual cholinesterase activities were determined (two distinct determinations for each inhibitor concentration).…”

Section: Purification Of Cholinesterasementioning

confidence: 99%

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Acetylcholinesterase in Dendrobaena veneta (Oligochaeta: Opisthopora) is Present with Forms Sensitive and Insensitive to Phosphatidylinositol Phospholipase C

Talesa

Romani

Rosi

et al. 1996

European Journal of Biochemistry

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Three distinct acetylcholinesterases were detected in the annelid oligochaete Dendrobuenu veneta.Two enzymes (a, p), copurified from a Triton-X-l 00-soluble extract of whole animals by affinity (edrophonium-Sepharose) chromatography, were separately eluted from a Sephadex G-200 column. Gel-filtration chromatography, sedimentation analysis and SDS/PAGE showed the a and p forms to be a globular dimer (1 10 kDa, 7.0 S) and a hydrophilic monomer (58 kDa, 5.0 S) respectively, both weakly linked to the cell membrane. The third form ( y ) , also purified to homogeneity by slower filtration through an edrophonium-Sepharose matrix, proved to be an amphiphilic globular dimer ( 1 33 kDa, 7.0 S) with a phosphatidylinositol anchor giving cell membrane insertion, detergent (Triton X-100, Brij 96) interaction and self-aggregation. The a acetylcholinesterase showed a fairly low substrate specificity : the p form hydrolyzed propionylthiocholine at the highest rate and was inactive on butyrylthiocholine ; the y acetylcholinesterase, showing a marked active-site specificity with differently sized substrates, was likely functional in cholinergic synapses. Studies with inhibitors showed incomplete inhibition of all three acetylcholinesterase by 1 mM eserine and different sensitivity for edrophonium or procainamide. The a and p forms, sensitive to 1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide, were unaffected by tetra(monoisopropy1)-pyrophosphortetramide, while both these agents inhibited the y enzyme. All three forms showed excess-substrate inhibition by acetylthiocholine. Enzyme activity was histochemically localized in the nerve ring and its minor branches. Monomeric acetylcholinesterase (p) is likely the only form present in the ganglionic glial framework.

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Section: B Vncsupporting

confidence: 56%

Section: B Vncmentioning

confidence: 85%

Section: Purification Of Cholinesterasementioning

confidence: 99%

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Acetylcholinesterase in Dendrobaena veneta (Oligochaeta: Opisthopora) is Present with Forms Sensitive and Insensitive to Phosphatidylinositol Phospholipase C

Talesa

Romani

Rosi

et al. 1996

European Journal of Biochemistry

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“…Acetylcholinesterases (AcChoEases, EC 3.1.1.7) and butyrylcholinesterases (BtChoEases, EC 3.1.1.8) (1)(2)(3) constitute a closely homologous family of proteins (4)(5)(6)(7)(8)(9)(10)(11)(12)(13). These enzymes consist of a major common catalytic domain and a small C-terminal variable region.…”

mentioning

confidence: 99%

Cholinesterase-like domains in enzymes and structural proteins: functional and evolutionary relationships and identification of a catalytically essential aspartic acid.

Krejci

Duval

Chatonnet

et al. 1991

Proc. Natl. Acad. Sci. U.S.A.

133

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Primary sequences of cholinesterases and related proteins have been systematically compared. The cholinesterase-like domain of these proteins, about 500 amino acids, may fulfill a catalytic and a structural function. We identified an aspartic acid residue that is conserved among esterases and lipases (Asp-397 in Torpedo acetylcholinesterase) but that had not been considered to be involved in the catalytic mechanism. Site-directed mutagenesis demonstrated that this residue is necessary for activity. Analysis of evolutionary relationships shows that the noncatalytic members of the family do not constitute a separate subgroup, suggesting that loss of catalytic activity occurred independently on several occasions, probably from bifunctional molecules. Cholinesterases may thus be involved in cell-cell interactions in addition to the hydrolysis of acetylcholine. This would explain their specific expression in well-defined territories during embryogenesis before the formation of cholinergic synapses and their presence in noncholinergic tissues.

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“…The red cell enzyme is a glycophospholipid-anchored dimer (Massoulib and Toutant, 1988;Chatonnet and Lockridge, 1989;Taylor, 1991). Within a species, the two forms have a highly similar aminoacid sequence (Chhajlani et al, 1989;Soreq and Prody, 1989;Soreq et al, 1990;Doctor et al, 1990;Rachinsky et al, 1990;Heider et al, 1991) and most antibodies so far raised against one form, cross-reacted with the other (Rakonczay and Brimijoin, 1988;MassouliC and Toutant, 1988). The two forms, however, differ in the N-glycosylation pattern, the C-terminus, and in their respective hydrophobic anchors.…”

Section: Discussionmentioning

confidence: 99%

Monoclonal antibodies against brain acetycholinesterases which recognize the subunits bearing the hydrophobic anchor

Liao

Mortensen

Nørgaard‐Pedersen

et al. 1993

European Journal of Biochemistry

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Monoclonal antibodies were raised against amphiphilic detergent-soluble (DS) acetylcholinesterase (AChE) from human brain caudate nucleus. Three mAb, 132-4 (IgG,), 132-5 (IgG,) and 132-6 (IgG,), specific for brain DS-AChE were selected and subcloned. These mAb reacted with native as well as heat-denatured and SDS-denatured DS-AChE, indicating that the epitopes to which mAb bound are continuous determinants. The mAb cross-reacted with DS-AChE from bovine and mouse brain and with brain DS-AChE from river trout (Sufmo rrurra f o m f u r i o ) and lake trout (SuZmo rrurru f o m u Zacusrris). No cross-reaction was detected with the following antigens : salt-soluble (SS) AChE from bovine brain, glycophospholipid-anchored AChE from human and bovine erythrocytes, DS-butyrylcholinesterase and SS-butyrylcholinesterase (BtChE) from the brains of human and bovine, DS-BtChE from chicken and BtChE from human serum. Deglycosylation of brain DSAChE with N-glycosidase F did not abolish the binding of mAb to DS-AChE. After reduction of brain DS-AChE by dithiothreitol, the mAb no longer reacted with the antigen, indicating that a disulfide bridge is important for the epitope. Monomerization of brain DS-AChE by trypsin and limited proteinase K treatment also abolished the binding of mAb to DS-ACE. Sucrose-densitygradient centrifugation showed that mAb reacted only with native tetrameric forms, but not with dimeric and monomeric forms. Western blot, after SDSPAGE under non-reducing conditions, showed that mAb reacted with those subunits carrying the hydrophobic anchor (i.e. tetramers, himers and heavy dimers) but not with those devoid of it (light dimers or monomers). Since mAb 132-4,132-5 and 132-6 recognized DS-ACE from fish up to mammalian brain in the evolutionary tree, it is concluded that the epitope to which these mAb bind, is conserved in nature.

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Vertebrate Cholinesterases: Structure and Types of Interaction

Cited by 76 publications

References 258 publications

Acetylcholinesterase in Dendrobaena veneta (Oligochaeta: Opisthopora) is Present with Forms Sensitive and Insensitive to Phosphatidylinositol Phospholipase C

Acetylcholinesterase in Dendrobaena veneta (Oligochaeta: Opisthopora) is Present with Forms Sensitive and Insensitive to Phosphatidylinositol Phospholipase C

Cholinesterase-like domains in enzymes and structural proteins: functional and evolutionary relationships and identification of a catalytically essential aspartic acid.

Monoclonal antibodies against brain acetycholinesterases which recognize the subunits bearing the hydrophobic anchor

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