The ß-amyloid peptide in Alzheimer's disease decreases adhesion of vascular muscle cells to the basement membrane

Mok, Su San, Losic, Dusan, Barrow, Colin J., Turner, Bradley J., Masters, Colin L., Martin, Lisandra L. and Small, David H. 2006, The ß-amyloid peptide in Alzheimer's disease decreases adhesion of vascular muscle cells to the basement membrane, Journal of neurochemistry, vol. 96, no. 1, pp. 53-64, doi: 10.1111/j.1471-4159.2005.03539.x.

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Title The ß-amyloid peptide in Alzheimer's disease decreases adhesion of vascular muscle cells to the basement membrane
Author(s) Mok, Su San
Losic, Dusan
Barrow, Colin J.ORCID iD for Barrow, Colin J.
Turner, Bradley J.
Masters, Colin L.
Martin, Lisandra L.
Small, David H.
Journal name Journal of neurochemistry
Volume number 96
Issue number 1
Start page 53
End page 64
Publisher Raven Press (Lippincott Williams & Wilkins)
Place of publication [New York, N.Y.]
Publication date 2006-01
ISSN 0022-3042
Keyword(s) atomic force microscopy
cell viability
extracellular matrix
mitogen-activated protein kinase
Summary Cerebral amyloid angiopathy (CAA) is a major feature of Alzheimer's disease pathology. In CAA, degeneration of vascular smooth muscle cells (VSMCs) occurs close to regions of the basement membrane where the amyloid protein (Aβ) builds up. In this study, the possibility that Aβ disrupts adhesive interactions between VSMCs and the basement membrane was examined. VSMCs were cultured on a commercial basement membrane substrate (Matrigel). The presence of Aβ in the Matrigel decreased cell-substrate adhesion and cell viability. Full-length oligomeric Aβ was required for the effect, as N- and C-terminally truncated peptide analogues did not inhibit adhesion. Aβ that was fluorescently labelled at the N-terminus (fluo-Aβ) bound to Matrigel as well as to the basement membrane heparan sulfate proteoglycan (HSPG) perlecan and laminin. Adhesion of VSMCs to perlecan or laminin was decreased by Aβ. As perlecan influences VSMC viability through the extracellular signal-regulated kinase (ERK)1/2 signalling pathway, the effect of Aβ1–40 on ERK1/2 phosphorylation was examined. The level of phospho-ERK1/2 was decreased in cells following Aβ treatment. An inhibitor of ERK1/2 phosphorylation enhanced the effect of Aβ on cell adhesion. The studies suggest that Aβ can decrease VSMC viability by disrupting VSMC–extracellular matrix (ECM) adhesion.
Language eng
DOI 10.1111/j.1471-4159.2005.03539.x
Field of Research 030499 Medicinal and Biomolecular Chemistry not elsewhere classified
060105 Cell Neurochemistry
Socio Economic Objective 970103 Expanding Knowledge in the Chemical Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2005, Lippincott Williams & Wilkins
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Document type: Journal Article
Collection: School of Life and Environmental Sciences
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