Acetylcholinesterase accelerates assembly of amyloid-beta-peptides into Alzheimer's fibrils: Possible role of the peripheral site of the enzyme

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dc.contributor.authorInestrosa, N.C.
dc.contributor.authorAlvarez, A
dc.contributor.authorPerez, CA
dc.contributor.authorMoreno, RD
dc.contributor.authorVicente, M
dc.contributor.authorLinker, C
dc.contributor.authorCasanueva, OI
dc.contributor.authorSoto, C
dc.contributor.authorGarrido, J
dc.date.accessioned2025-01-21T01:34:05Z
dc.date.available2025-01-21T01:34:05Z
dc.date.issued1996
dc.description.abstractAcetylcholinesterase (AChE), an important component of cholinergic synapses, colocalizes with amyloid-beta peptide (A beta) deposits of Alzheimer's brain. We report here that bovine brain AChE, as well as the human and mouse recombinant enzyme, accelerates amyloid formation from wild-type A beta and a mutant A beta peptide, which alone produces few amyloid-like fibrils. The action of AChE was independent of the subunit array of the enzyme, was not affected by edrophonium, an active site inhibitor, but it was affected by propidium, a peripheral anionic binding site ligand. Butyrylcholinesterase, an enzyme that lacks the peripheral site, did not affect amyloid formation. Furthermore, AChE is a potent amyloid-promoting factor when compared with other A beta-associated proteins. Thus, in addition to its role in cholinergic synapses, AChE may function by accelerating A beta formation and could play a role during amyloid deposition in Alzheimer's brain.
dc.fuente.origenWOS
dc.identifier.eissn1097-4199
dc.identifier.issn0896-6273
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/97512
dc.identifier.wosidWOS:A1996UG61100021
dc.issue.numero4
dc.language.isoen
dc.pagina.final891
dc.pagina.inicio881
dc.revistaNeuron
dc.rightsacceso restringido
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleAcetylcholinesterase accelerates assembly of amyloid-beta-peptides into Alzheimer's fibrils: Possible role of the peripheral site of the enzyme
dc.typeartículo
dc.volumen16
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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