Interaction of Calreticulin with Amyloid Beta Peptide 1-42
Copyright policy )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.
- University of Copenhagen Denmark
- University of Copenhagen Denmark
- Statens Serum Institut Denmark
Amyloid beta-Peptides, Binding Sites, Peptide Fragments, calreticulin, amyloid beta, /dk/atira/pure/core/keywords/Life, chaperone, Humans, Alzheimer disease, Calreticulin, Peptides, Former LIFE faculty, Protein Binding
Amyloid beta-Peptides, Binding Sites, Peptide Fragments, calreticulin, amyloid beta, /dk/atira/pure/core/keywords/Life, chaperone, Humans, Alzheimer disease, Calreticulin, Peptides, Former LIFE faculty, Protein Binding
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