Interaction of calreticulin with amyloid beta peptide 1-42

被引：0

作者：

Duus, K. ^{[1
]}

Hansen, P. R. ^{[2
]}

Houen, G. ^{[1
]}

机构：

[1] Statens Serum Inst, Dept Autoimmunol, DK-2300 Copenhagen, Denmark

[2] Univ Copenhagen, Fac Life Sci, Dept Nat Sci, Frederiksberg, Denmark

来源：

PROTEIN AND PEPTIDE LETTERS | 2008年 / 15卷 / 01期

关键词：

calreticulin; chaperone; amyloid beta; Alzheimer disease;

D O I：

暂无

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The interaction of calreticulin with amyloid beta (A beta) was investigated using solid phase and solution binding assays. Calreticulin bound A beta 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 A beta 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.

引用

页码：103 / 107

页数：5

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