Journal
BLOOD
Volume 111, Issue 10, Pages 4986-4996Publisher
AMER SOC HEMATOLOGY
DOI: 10.1182/blood-2007-08-108472
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Funding
- British Heart Foundation Funding Source: Medline
- Medical Research Council [G0601378, G0400701] Funding Source: Medline
- Wellcome Trust Funding Source: Medline
- Medical Research Council [G0400701, G0601378] Funding Source: researchfish
- MRC [G0601378, G0400701] Funding Source: UKRI
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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 GAOGLRGGAGPOG-PEGGKGAAGPOGPO. 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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