dc.creatorMuñoz, Francisco J.
dc.creatorOpazo, Carlos
dc.creatorGil-Gómez, Gabriel
dc.creatorTapia, Gladys
dc.creatorFernández, Virginia
dc.creatorValverde, Miguel A.
dc.creatorInestrosa, Nibaldo C.
dc.date.accessioned2019-01-29T17:51:53Z
dc.date.available2019-01-29T17:51:53Z
dc.date.created2019-01-29T17:51:53Z
dc.date.issued2002
dc.identifierJournal of Neuroscience, Volumen 22, Issue 8, 2018, Pages 3081-3089
dc.identifier02706474
dc.identifierhttp://repositorio.uchile.cl/handle/2250/163599
dc.description.abstractAmyloid β-peptide (Aβ) fibril deposition on cerebral vessels produces cerebral amyloid angiopathy that appears in the majority of Alzheimer's disease patients. An early onset of a cerebral amyloid angiopathy variant called hereditary cerebral hemorrhage with amyloidosis of the Dutch type is caused by a point mutation in Aβ yielding AβGlu22→Gln. The present study addresses the effect of amyloid fibrils from both wild-type and mutated Aβ on vascular cells, as well as the putative protective role of antioxidants on amyloid angiopathy. For this purpose, we studied the cytotoxicity induced by Aβ1-40 Glu22→Gln and Aβ1-40 wild-type fibrils on human venule endothelial cells and rat aorta smooth muscle cells. We observed that AβGlu22→Gln fibrils are more toxic for vascular cells than the wild-type fibrils. We also evaluated the cytotoxicity of Aβ fibrils bound with acetyl-cholinesterase (AChE), a common component of amyloid deposits. Aβ1-40 wild-type-AChE fibrillar complexes, similar to neurona
dc.languageen
dc.rightshttp://creativecommons.org/licenses/by-nc-nd/3.0/cl/
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
dc.sourceJournal of Neuroscience
dc.subject17β-estradiol
dc.subjectAcetylcholinesterase
dc.subjectAlzheimer's disease
dc.subjectAmyloid
dc.subjectCAA
dc.subjectEndothelial cells
dc.subjectHCHWA-D
dc.subjectOxidative stress
dc.subjectVascular smooth muscle cells
dc.subjectVitamin C
dc.subjectVitamin E
dc.titleVitamin E but not 17β-estradiol protects against vascular toxicity induced by β-amyloid wild type and the dutch amyloid variant
dc.typeArtículos de revistas


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