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 Blood, 15 May 2008, Vol. 111, No. 10, pp. 4986-4996.
Prepublished online as a Blood First Edition Paper on February 27, 2008; DOI 10.1182/blood-2007-08-108472.

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HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY

Identification of a major GpVI-binding locus in human type III collagen

Gavin E. Jarvis1, Nicolas Raynal1, Jonathan P. Langford1, David J. Onley1, Allen Andrews1, Peter A. Smethurst2, and Richard W. Farndale1

1 Departments of Biochemistry and 2 Haematology, University of Cambridge, Cambridge, United Kingdom

We have analyzed the adhesion of human and murine platelets, and of recombinant human and murine GpVI ectodomains, to synthetic triple-helical collagen-like peptides. These included 57 peptides derived from the sequence of human type III collagen and 9 peptides derived from the cyanogen bromide fragment of bovine type III collagen, {alpha}1(III)CB4. We have identified several peptides that interact with GpVI, in particular a peptide designated III-30 with the sequence GAOGLRGGAGPOGPEGGKGAAGPOGPO. Both human and murine platelets bound to peptide III-30 in a GpVI-dependent manner. III-30 also supported binding of recombinant GpVI ectodomains. Cross-linked III-30 induced aggregation of human and murine platelets, although with a lower potency than collagen-related peptide. Modifications of the peptide sequence indicated that the hydroxyproline residues play a significant role in supporting its GpVI reactivity. However, many peptides containing OGP/GPO motifs did not support adhesion to GpVI. These data indicate that the ability of a triple-helical peptide to bind GpVI is not solely determined by the presence or spatial arrangement of these OGP/GPO motifs within the peptides.


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