Elevated SAP in Alzheimer’s disease
Their observations support serum amyloid P component as a therapeutic target in Alzheimer’s disease."
The deposition of amyloid beta in the brain of individuals with Alzheimer’s disease is the focus of much research into both its cause and treatment.
While there may not be a consensus as to whether the deposition contributes to the disease or is a consequence of the disease, there is agreement that it is not favoured thermodynamically, meaning that something else is promoting the process.
Other proteins are often co-deposited in vivo with amyloid beta and one such protein is serum amyloid P component (or SAP). Recent evidence has suggested that SAP is elevated in Alzheimer’s disease and a team of researchers from Keele University in Staffordshire, led by Professor Chris Exley, has shown that physiologically-significant concentrations of SAP promote the deposition of amyloid beta under conditions approaching those found in vivo.
Professor Exley said: “We have shown that SAP is bound by fibrils of amyloid beta and that this interaction stabilises the fibrils over timescales which are physiologically significant. This is the first example of a physiologically significant biomolecule promoting and stabilising the formation of amyloid fibrils of amyloid beta 42 under near-physiological conditions.”
The group also found that this property of SAP was enhanced in the presence of aluminium, a metal which has also been shown to be co-deposited with amyloid beta in Alzheimer’s disease. There have been recent efforts to reduce the plasma concentration of SAP as a therapy for Alzheimer’s disease and the research provides strong evidence that SAP is involved in the deposition of amyloid beta 42 in Alzheimer’s disease and that by reducing the plasma concentration of SAP it might also reduce the deposition of amyloid beta. Their observations support serum amyloid P component as a therapeutic target in Alzheimer’s disease.
Serum Amyloid P Component Accelerates the Formation and Enhances the Stability of Amyloid Fibrils in a Physiologically Significant Under-Saturated Solution of Amyloid-β42 by Matthew Mold, Annette K Shrive, Christopher Exley will be published in the Journal of Alzheimer's Disease Volume 29, issue 4 (April 2012); DOI: 10.3233/JAD-2012-120076
ABOUT THE JOURNAL OF ALZHEIMER’S DISEASE (JAD)
The Journal of Alzheimer's Disease (http://www.j-alz.com) is an international multidisciplinary journal to facilitate progress in understanding the etiology, pathogenesis, epidemiology, genetics, behaviour, treatment and psychology of Alzheimer's disease. The journal publishes research reports, reviews, short communications, book reviews, and letters-to-the-editor. Groundbreaking research that has appeared in the journal includes novel therapeutic targets, mechanisms of disease and clinical trial outcomes. The Journal of Alzheimer's Disease has an Impact Factor of 4.261 according to Thomson Reuters' 2011 edition of Journal Citation Reports. It is ranked #19 on the Index Copernicus Top 100 Journal List. The Journal is published by IOS Press (www.iospress.com).
Professor Christopher Exley,
The Birchall Centre, Lennard-Jones Laboratories,
Keele University, Staffordshire, ST5 5BG, UK
Tel: 44 1782 734080; Email: email@example.com