Abstract

Amyloid consists of cross-beta-sheet fibrils and is associated with about 25 human diseases, including several neurodegenerative diseases, systemic and localized amyloidoses and type II diabetes mellitus. Amybid-forming proteins differ in structures and sequences, and it is to a large extent unknown what makes them convert from their native conformations into amyloid. In this review, current understanding of amino acid sequence determinants and the effects of molecular chaperones on amyloid formation are discussed. Studies of the nonpolar, transmembrane surfactant protein C (SP-C) have revealed amino acid sequence features that determine its amyloid fibril formation, features that are also found in the amyloid beta-peptide in Alzheimer's disease and the prion protein. Moreover, a proprotein chaperone domain (CTC(Brichos)) that prevents amyloid-like aggregation during proSP-C biosynthesis can prevent fibril formation also of other amyloidogenic proteins. (C) 2010 Elsevier Inc. All rights reserved.

Keywords

Protein misfolding; Secondary structure; Brichos; Surfactant protein C; Alzheimer's disease; Prion

Published in

Biochemical and Biophysical Research Communications
2010, volume: 396, number: 1, pages: 2-6
Publisher: ACADEMIC PRESS INC ELSEVIER SCIENCE

Authors' information