Crosslinking of amyloid-β peptide to brain acetylcholinesterase
dc.contributor.author | Opazo, C | |
dc.contributor.author | Inestrosa, NC | |
dc.date.accessioned | 2025-01-21T01:32:53Z | |
dc.date.available | 2025-01-21T01:32:53Z | |
dc.date.issued | 1998 | |
dc.description.abstract | Acetylcholinesterase (AChE) is the enzyme responsible for the hydrolysis of the neurotransmitter acetylcholine in the central nervous system. Recently, we have found that AChE promotes the assembly of amyloid-beta peptides (A beta) into Alzheimer fibrils. The action of AChE on the state of aggregation of the A beta peptide supposes a near neighbor relationship between these two molecules. In the present work, we have studied A beta-AChE interactions using the crosslinker reagent disuccinimidyl suberate (DSS), in the presence of [I-125]-A beta peptide The A beta-AChE complexes formed by crosslinking were then analyzed by SDS-PAGE and autoradiography. We observed the formation of [I-125] A beta-labeled complexes of 70, 160, 250, and 300 kDa corresponding to monomers, dimers, tetramers, and oligomers of AChE, respectively crosslinked with the A beta peptide. Our results suggest that AChE and the A beta peptide may be involved in physiologically relevant interactions, related to the pathogenesis of Alzheimer disease (AD). | |
dc.fuente.origen | WOS | |
dc.identifier.issn | 1044-7393 | |
dc.identifier.uri | https://repositorio.uc.cl/handle/11534/97338 | |
dc.identifier.wosid | WOS:000071935100004 | |
dc.issue.numero | 1 | |
dc.language.iso | en | |
dc.pagina.final | 49 | |
dc.pagina.inicio | 39 | |
dc.revista | Molecular and chemical neuropathology | |
dc.rights | acceso restringido | |
dc.subject | Alzheimer disease | |
dc.subject | amyloid-beta | |
dc.subject | acetylcholinesterase | |
dc.subject | crosslinking | |
dc.subject | A beta-AChE complex | |
dc.subject.ods | 03 Good Health and Well-being | |
dc.subject.odspa | 03 Salud y bienestar | |
dc.title | Crosslinking of amyloid-β peptide to brain acetylcholinesterase | |
dc.type | artículo | |
dc.volumen | 33 | |
sipa.index | WOS | |
sipa.trazabilidad | WOS;2025-01-12 |