J. Lipid Res.
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A more recent version of this article appeared on April 1, 2006

Papers In Press, published online ahead of print January 23, 2006
J. Lipid Res., doi:10.1194/jlr.C500022-JLR200
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Submitted on September 30, 2005
Revised on December 21, 2005
Accepted on January 23, 2006

High density lipoproteins bind Abeta and apolipoprotein C-II amyloid fibrils

Leanne M. Wilson, Chi L. L. Pham, Alicia J. Jenkins, John D. Wade, Andrew F. Hill, Matthew A. Perugini, and Geoffrey J. Howlett

Biochemistry and Molecular Biology, University of Melbourne, Melbourne, Victoria 3010

Corresponding Author: ghowlett{at}unimelb.edu.au

Disease-associated amyloid deposits contain both fibrillar and non-fibrillar components. The majority of these amyloid components originate or co-exist in the bloodstream. To understand the nature of the interaction between the non-fibrillar and fibrillar components we have developed a centrifugation method to isolate fibril-binding proteins from human serum. Amyloid fibrils composed of either Abeta peptide or apolipoprotein (apo) C-II co-sedimented with specific serum proteins. Gel electrophoresis, mass spectrometry peptide fingerprinting and western analysis identified the major binding species as proteins found in high density lipoprotein particles (HDL) including apoA-I, apoA-II, apoE, clusterin and serum amyloid A. Sedimentation analysis showed that purified human HDL and recombinant apoA-I lipid particles bound directly to Aß and apoC-II amyloid fibrils. These studies reveal a novel function of HDL which may contribute to the well-established protective effect of this lipoprotein class in heart disease.


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C. R. Stewart, A. Haw III, R. Lopez, T. O. McDonald, J. M. Callaghan, M. J. McConville, K. J. Moore, G. J. Howlett, and K. D. O'Brien
Serum amyloid P colocalizes with apolipoproteins in human atheroma: functional implications
J. Lipid Res., October 1, 2007; 48(10): 2162 - 2171.
[Abstract] [Full Text] [PDF]


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