Interaction of calreticulin with amyloid beta peptide 1-42.
The interaction of calreticulin with amyloid beta (Abeta) was investigated using solid phase and solution binding assays. Calreticulin bound Abeta 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 Abeta 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.
Duus
K
K
Department of Autoimmunology, Statens Serum Institut, Artillerivej 5, DK-2300 Copenhagen, Denmark.
Hansen
P R
PR
Houen
G
G
D016229:Amyloid beta-Peptides / Q000378:metabolism*; D001665:Binding Sites; D037282:Calreticulin / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D010446:Peptide Fragments / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism; D011485:Protein Binding
D016229:Amyloid beta-Peptides; D037282:Calreticulin; D010446:Peptide Fragments; D010455:Peptides; C075222:amyloid beta-protein (1-42)