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Papers In Press, published online ahead of print December 2, 2005
Biochemistry Dept., University of Cambrdige, Cambridge CB2 1QW
Corresponding Author: rwf10{at}cam.ac.uk
A set of 57 synthetic peptides encompassing the whole of the triple-helical domain of human collagen III was used to locate binding sites for the collagen-binding integrin a2ß1. The capacity of the peptides to support Mg2+-dependent binding of several integrin preparations was examined. Wild-type integrins (recombinant a2 I-domain, a2ß1 purified from platelet membranes, and recombinant soluble a2ß1 expressed as an a2-fos:ß1-jun heterodimer) bound well to only three peptides, two containing Gxx'GER motifs, GROGER and GMOGER, whilst the third contained two adjacent Gxx'GEN motifs, GLKGEN and GLOGEN. Two mutant a2 I-domains were tested, the inactive T221A, which recognised no peptides, and the constitutively active E318W, which bound a larger subset of peptides. Adhesion of activated human platelets to GER-containing peptides was greater than that of resting platelets, and HT1080 cells bound well to more of the peptides than platelets. Binding of cells and recombinant proteins was abolished by an anti-a2 monoclonal antibody, 6F1, and by chelation of Mg2+. We describe two novel high-affinity integrin binding motifs in human collagen III, GROGER and GLOGEN, and a third motif, GLKGEN, which displays intermediate activity. Each motif was verified using shorter synthetic peptides.
J. Biol. Chem, 10.1074/jbc.M509818200
Submitted on September 7, 2005
Revised on November 22, 2005
Accepted on December 2, 2005
The use of synthetic peptides to locate novel integrin
2
1-binding motifs in human collagen III
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