Oligomeric and fibrillar amyloid beta 42 induce platelet aggregation partially through GPVI

© 2017 Taylor & Francis The effects of the Alzheimer’s disease (AD)-associated Amyloid-ß (Aß) peptides on platelet aggregation have been previously assessed, but most of these studies focused on Aß40 species. It also remains to be determined which distinct forms of Aß peptides exert differenti...

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Main Authors: Elaskalani, O., Khan, I., Morici, M., Matthysen, C., Sabale, M., Martins, R., Verdile, G., Metharom, Pat
Format: Journal Article
Published: Informa Healthcare 2017
Online Access:http://hdl.handle.net/20.500.11937/62420
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author Elaskalani, O.
Khan, I.
Morici, M.
Matthysen, C.
Sabale, M.
Martins, R.
Verdile, G.
Metharom, Pat
author_facet Elaskalani, O.
Khan, I.
Morici, M.
Matthysen, C.
Sabale, M.
Martins, R.
Verdile, G.
Metharom, Pat
author_sort Elaskalani, O.
building Curtin Institutional Repository
collection Online Access
description © 2017 Taylor & Francis The effects of the Alzheimer’s disease (AD)-associated Amyloid-ß (Aß) peptides on platelet aggregation have been previously assessed, but most of these studies focused on Aß40 species. It also remains to be determined which distinct forms of Aß peptides exert differential effects on platelets. In AD, oligomeric Aß42 species is widely thought to be a major contributor to the disease pathogenesis. We, therefore, examine the ability of oligomeric and fibrillary Aß42 to affect platelet aggregation. We show that both forms of Aß42 induced significant platelet aggregation and that it is a novel ligand for the platelet receptor GPVI. Furthermore, a novel binding peptide that reduces the formation of soluble Aß42 oligomers was effective at preventing Aß42-dependent platelet aggregation. These results support a role for Aß42 oligomers in platelet hyperactivity.
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institution Curtin University Malaysia
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last_indexed 2025-11-14T10:22:17Z
publishDate 2017
publisher Informa Healthcare
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spelling curtin-20.500.11937-624202018-02-01T05:58:13Z Oligomeric and fibrillar amyloid beta 42 induce platelet aggregation partially through GPVI Elaskalani, O. Khan, I. Morici, M. Matthysen, C. Sabale, M. Martins, R. Verdile, G. Metharom, Pat © 2017 Taylor & Francis The effects of the Alzheimer’s disease (AD)-associated Amyloid-ß (Aß) peptides on platelet aggregation have been previously assessed, but most of these studies focused on Aß40 species. It also remains to be determined which distinct forms of Aß peptides exert differential effects on platelets. In AD, oligomeric Aß42 species is widely thought to be a major contributor to the disease pathogenesis. We, therefore, examine the ability of oligomeric and fibrillary Aß42 to affect platelet aggregation. We show that both forms of Aß42 induced significant platelet aggregation and that it is a novel ligand for the platelet receptor GPVI. Furthermore, a novel binding peptide that reduces the formation of soluble Aß42 oligomers was effective at preventing Aß42-dependent platelet aggregation. These results support a role for Aß42 oligomers in platelet hyperactivity. 2017 Journal Article http://hdl.handle.net/20.500.11937/62420 10.1080/09537104.2017.1401057 Informa Healthcare restricted
spellingShingle Elaskalani, O.
Khan, I.
Morici, M.
Matthysen, C.
Sabale, M.
Martins, R.
Verdile, G.
Metharom, Pat
Oligomeric and fibrillar amyloid beta 42 induce platelet aggregation partially through GPVI
title Oligomeric and fibrillar amyloid beta 42 induce platelet aggregation partially through GPVI
title_full Oligomeric and fibrillar amyloid beta 42 induce platelet aggregation partially through GPVI
title_fullStr Oligomeric and fibrillar amyloid beta 42 induce platelet aggregation partially through GPVI
title_full_unstemmed Oligomeric and fibrillar amyloid beta 42 induce platelet aggregation partially through GPVI
title_short Oligomeric and fibrillar amyloid beta 42 induce platelet aggregation partially through GPVI
title_sort oligomeric and fibrillar amyloid beta 42 induce platelet aggregation partially through gpvi
url http://hdl.handle.net/20.500.11937/62420