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REVIEW

Amyloid accomplices and enforcers

Department of Molecular and Cell Biology, University of Connecticut, Storrs, Connecticut 06269-3125, USA

Amyloid-related diseases are often ascribed to protein "misfolding." Yet in the absence of high-resolution structures for mature fibrils or intermediates, the connection between the mechanism of amyloid formation and protein folding remains tenuous. The simplistic view of amyloid fibrillogenesis as a homogeneous self-assembly process is being increasingly challenged by observations that amyloids interact with a variety of cofactors including metals, glycosaminoglycans, glycoproteins such as serum amyloid P and apolipo-protein E, and constituents of basement membranes such as perlecan, laminin, and agrin. These "pathological chaperones" have effects that range from mediating the rate of amyloid fibril formation to increasing the stability of amyloid deposits, and may contribute to amyloid toxicity. An increasing appreciation of the role of accessory molecules in amyloid etiology has paved the way to novel diagnostics and therapeutic strategies.

Keywords: Alzheimer A peptide; protein folding; extracellular matrix proteins; heparan sulfate proteoglycans; basal lamina

Abbreviations: A, Alzheimer-peptide • AD, Alzheimer’s disease • apoE, apolipoprotein E • APP, (Alzheimer) amyloid precursor protein • IAPP, islet amyloid polypeptide • GAG, glycosaminoglycan • HSPG, heparan sulfate proteoglycan • LNS, laminin neurexin and SHBG-like domain • PrP^C, soluble form of prion protein • PrP^Sc, protease-resistant form of prion protein • SAA, serum amyloid A • SAP, serum amyloid P component

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.04887005.

Reprint requests to: Andrei Alexandrescu, Department of Molecular and Cell Biology, University of Connecticut, 91 North Eagleville Road, U-3125, Storrs, CT 06269-3125, USA; e-mail: andrei{at}uconn.edu; fax: (860) 486-4331.

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