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
收藏
页码：103 / 107
页数：5
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