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MRP14 (S100A9) protein interacts with alzheimer beta-amyloid peptide and induces its fibrillization
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
Umeå University, Faculty of Medicine, Umeå Centre for Molecular Medicine (UCMM).
2012 (English)In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 7, no 3, e32953- p.Article in journal (Refereed) Published
Abstract [en]

Increasing evidence supports the contribution of local inflammation to the development of Alzheimer's disease (AD) pathology, although the precise mechanisms are not clear. In this study, we demonstrate that the pro-inflammatory protein S100A9 interacts with the A beta 1-40 peptide and promotes the formation of fibrillar beta-amyloid structures. This interaction also results in reduced S100A9 cytotoxicity by the binding of S100A9 toxic species to A beta 1-40 amyloid structures. These results suggest that secretion of S100A9 during inflammation promotes the formation of amyloid plaques. By acting as a sink for toxic species, plaque formation may be the result of a protective response within the brain of AD patients, in part mediated by S100A9.

Place, publisher, year, edition, pages
San Francisco: Public Library of Science , 2012. Vol. 7, no 3, e32953- p.
National Category
Microbiology in the medical area
Identifiers
URN: urn:nbn:se:umu:diva-56429DOI: 10.1371/journal.pone.0032953ISI: 000303909200010OAI: oai:DiVA.org:umu-56429DiVA: diva2:534700
Available from: 2012-06-18 Created: 2012-06-18 Last updated: 2017-12-07Bibliographically approved

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Zhang, CeGilthorpe, Jonathan
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