Stable complexes involving acetylcholinesterase and amyloid-ß-peptide change the biochemical properties of the enzyme and increase the neurotoxicity of Alzheimer's fibrils
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- dc.contributor.author Álvarez, Alejandra R.ca
- dc.contributor.author Alarcón Martínez, Rodrigoca
- dc.contributor.author Opazo, Carlos M.ca
- dc.contributor.author Campos, Eliseo O.ca
- dc.contributor.author Muñoz López, Francisco José, 1964-ca
- dc.contributor.author Calderón, Frances H.ca
- dc.contributor.author Dajas, Federicoca
- dc.contributor.author Gentry, Mary K.ca
- dc.contributor.author Doctor, Bhupendra P.ca
- dc.contributor.author Mello, Fernando G. deca
- dc.contributor.author Inestrosa, Nibaldo C.ca
- dc.date.accessioned 2012-07-05T06:54:28Z
- dc.date.available 2012-07-05T06:54:28Z
- dc.date.issued 1998ca
- dc.description.abstract Brain acetylcholinesterase (AChE) forms stable complexes with amyloid-beta peptide (Abeta) during its assembly into filaments, in agreement with its colocalization with the Abeta deposits of Alzheimer's brain. The association of the enzyme with nascent Abeta aggregates occurs as early as after 30 min of incubation. Analysis of the catalytic activity of the AChE incorporated into these complexes shows an anomalous behavior reminiscent of the AChE associated with senile plaques, which includes a resistance to low pH, high substrate concentrations, and lower sensitivity to AChE inhibitors. Furthermore, the toxicity of the AChE-amyloid complexes is higher than that of the Abeta aggregates alone. Thus, in addition to its possible role as a heterogeneous nucleator during amyloid formation, AChE, by forming such stable complexes, may increase the neurotoxicity of Abeta fibrils and thus may determine the selective neuronal loss observed in Alzheimer's brain.
- dc.format.mimetype application/pdfca
- dc.identifier.citation Alvarez A, Alarcón R, Opazo C, Campos EO, Muñoz FJ, Calderón FH et al. Stable complexes involving acetylcholinesterase and amyloid-ß-peptide change the biochemical properties of the enzyme and increase the neurotoxicity of Alzheimer's fibrils. J Neurosci. 1998;18(9):3213-23. DOI: 10.1523/jneurosci.18-09-03213.1998ca
- dc.identifier.doi http://dx.doi.org/10.1523/jneurosci.18-09-03213.1998
- dc.identifier.issn 0270-6474ca
- dc.identifier.uri http://hdl.handle.net/10230/16675
- dc.language.iso engca
- dc.publisher Society for Neuroscienceca
- dc.relation.ispartof Journal of Neuroscience. 1998;18(9):3213-23
- dc.rights © 1998, Society for Neuroscience. The published version is available at: http://www.jneurosci.org/content/18/9/3213ca
- dc.rights.accessRights info:eu-repo/semantics/openAccess
- dc.subject.keyword AChE
- dc.subject.keyword Ab-amyloid fibrils
- dc.subject.keyword AChE-Ab-amyloid fibril complexes
- dc.subject.keyword Amyloid formation
- dc.subject.keyword Alzheimer’s disease
- dc.subject.keyword Neurotoxicity
- dc.subject.other Alzheimer, Malaltia d' -- Fisiologia patològica
- dc.subject.other Proteïna beta-amiloide
- dc.title Stable complexes involving acetylcholinesterase and amyloid-ß-peptide change the biochemical properties of the enzyme and increase the neurotoxicity of Alzheimer's fibrilsca
- dc.type info:eu-repo/semantics/articleca
- dc.type.version info:eu-repo/semantics/publishedVersion