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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Interaction of Calreticulin with Amyloid Beta Peptide 1-42

Author(s): G. Houen, K. Duus and P. R. Hansen

Volume 15, Issue 1, 2008

Page: [103 - 107] Pages: 5

DOI: 10.2174/092986608783330459

Price: $65

Abstract

The interaction of calreticulin with amyloid beta (Aβ) was investigated using solid phase and solution binding assays. Calreticulin bound Aβ 1-42 in a time and concentration dependent fashion. The binding was optimal at pH 5 and was stimulated by Ca2+ and inhibited by Zn2+ at pH 7. Interaction took place through the hydrophobic C-terminus of Aβ 1- 42 and the polypeptide binding site of calreticulin. The results are discussed in the light of a reported role of calreticulin as a cell surface scavenger receptor.

Keywords: Calreticulin, chaperone, amyloid beta, Alzheimer disease


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