Interaction of Calreticulin with Amyloid Beta Peptide 1-42

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

Journal Name: Protein & Peptide Letters

Volume 15 , Issue 1 , 2008

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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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Article Details

VOLUME: 15
ISSUE: 1
Year: 2008
Page: [103 - 107]
Pages: 5
DOI: 10.2174/092986608783330459

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