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Papers In Press, published online ahead of print April 1, 2006
J. Lipid Res., doi:10.1194/jlr.C500022-JLR200

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Journal of Lipid Research, Vol. 47, 755-760, April 2006
Copyright © 2006 by American Society for Biochemistry and Molecular Biology

High density lipoproteins bind Aß 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^1,*

^* Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria 3010, Australia
Department of Medicine, University of Melbourne, St. Vincent's Hospital, Fitzroy, Victoria 3065, Australia
Howard Florey Institute of Experimental Physiology and Medicine, University of Melbourne, Parkville, Victoria 3010, Australia
^** Department of Pathology, University of Melbourne, Parkville, Victoria 3010, Australia, and Mental Health Research Institute of Victoria, Parkville, Victoria 3052, Australia

The online version of this article (available at http://www.jlr.org) contains an additional table.

Published, JLR Papers in Press, January 23, 2006.

¹ To whom correspondence should be addressed. e-mail: ghowlett{at}unimelb.edu.au

Disease-associated amyloid deposits contain both fibrillar and nonfibrillar components. The majority of these amyloid components originate or coexist in the bloodstream. To understand the nature of the interaction between the nonfibrillar and fibrillar components, we have developed a centrifugation method to isolate fibril binding proteins from human serum. Amyloid fibrils composed of either Aß peptide or apolipoprotein C-II (apoC-II) cosedimented with specific serum proteins. Gel electrophoresis, mass spectrometry peptide fingerprinting, and Western analysis identified the major binding species as proteins found in HDL particles, 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 that may contribute to the well-established protective effect of this lipoprotein class in heart disease.

Supplementary key words amyloidosis • apolipoprotein A-I • atherosclerosis • human serum • lipid • nonfibrillar component • protein aggregation • protein folding

Abbreviations: apoC-II, apolipoprotein C-II; SAA, serum amyloid A; SAP, serum amyloid P component

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