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
Protein & Peptide Letters
Title: Interaction of Calreticulin with Amyloid Beta Peptide 1-42
Volume: 15 Issue: 1
Author(s): G. Houen, K. Duus and P. R. Hansen
Affiliation:
Keywords: Calreticulin, chaperone, amyloid beta, Alzheimer disease
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.
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Cite this article as:
Houen G., Duus K. and Hansen R. P., Interaction of Calreticulin with Amyloid Beta Peptide 1-42, Protein & Peptide Letters 2008; 15 (1) . https://dx.doi.org/10.2174/092986608783330459
DOI https://dx.doi.org/10.2174/092986608783330459 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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