The α5β1 Integrin Mediates Elimination of Amyloid-β Peptide and Protects Against Apoptosis

The amyloid-β peptide (Aβ) can mediate cell attachment by binding to β1 integrins through an arg-his-asp sequence. We show here that the α5β1 integrin, a fibronectin receptor, is an efficient binder of Aβ, and mediates cell attachment to nonfibrillar Aβ. Cells engineered to express α5β1 internalized...

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Detalles Bibliográficos
Autores principales: Matter, Michelle L., Zhang, Zhuohua, Nordstedt, Christer, Ruoslahti, Erkki
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1998
Materias:
Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2132763/
https://www.ncbi.nlm.nih.gov/pubmed/9585419
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author Matter, Michelle L.
Zhang, Zhuohua
Nordstedt, Christer
Ruoslahti, Erkki
author_facet Matter, Michelle L.
Zhang, Zhuohua
Nordstedt, Christer
Ruoslahti, Erkki
author_sort Matter, Michelle L.
collection PubMed
description The amyloid-β peptide (Aβ) can mediate cell attachment by binding to β1 integrins through an arg-his-asp sequence. We show here that the α5β1 integrin, a fibronectin receptor, is an efficient binder of Aβ, and mediates cell attachment to nonfibrillar Aβ. Cells engineered to express α5β1 internalized and degraded more added Aβ1-40 than did α5β1-negative control cells. Deposition of an insoluble Aβ1-40 matrix around the α5β1-expressing cells was reduced, and the cells showed less apoptosis than the control cells. Thus, the α5β1 integrin may protect against Aβ deposition and toxicity, which is a course of Alzheimer's disease lesions.
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spelling pubmed-21327632008-05-01 The α5β1 Integrin Mediates Elimination of Amyloid-β Peptide and Protects Against Apoptosis Matter, Michelle L. Zhang, Zhuohua Nordstedt, Christer Ruoslahti, Erkki J Cell Biol Articles The amyloid-β peptide (Aβ) can mediate cell attachment by binding to β1 integrins through an arg-his-asp sequence. We show here that the α5β1 integrin, a fibronectin receptor, is an efficient binder of Aβ, and mediates cell attachment to nonfibrillar Aβ. Cells engineered to express α5β1 internalized and degraded more added Aβ1-40 than did α5β1-negative control cells. Deposition of an insoluble Aβ1-40 matrix around the α5β1-expressing cells was reduced, and the cells showed less apoptosis than the control cells. Thus, the α5β1 integrin may protect against Aβ deposition and toxicity, which is a course of Alzheimer's disease lesions. The Rockefeller University Press 1998-05-18 /pmc/articles/PMC2132763/ /pubmed/9585419 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Matter, Michelle L.
Zhang, Zhuohua
Nordstedt, Christer
Ruoslahti, Erkki
The α5β1 Integrin Mediates Elimination of Amyloid-β Peptide and Protects Against Apoptosis
title The α5β1 Integrin Mediates Elimination of Amyloid-β Peptide and Protects Against Apoptosis
title_full The α5β1 Integrin Mediates Elimination of Amyloid-β Peptide and Protects Against Apoptosis
title_fullStr The α5β1 Integrin Mediates Elimination of Amyloid-β Peptide and Protects Against Apoptosis
title_full_unstemmed The α5β1 Integrin Mediates Elimination of Amyloid-β Peptide and Protects Against Apoptosis
title_short The α5β1 Integrin Mediates Elimination of Amyloid-β Peptide and Protects Against Apoptosis
title_sort α5β1 integrin mediates elimination of amyloid-β peptide and protects against apoptosis
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2132763/
https://www.ncbi.nlm.nih.gov/pubmed/9585419
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