The platelet reactivity of collagen type I: evidence for multiple platelet-reactive sites in the type I collagen molecule.
In this study, the ability of peptides, obtained by fragmentation of the collagen type I molecule, to induce platelet aggregation has been examined. In order to satisfy requirements for tertiary and quaternary structure, peptides were first renatured (where necessary) to restore triple-helical configuration and then polymerised. Fragmentation with mammalian collagenase indicated the presence of platelet-reactive sites in both the N-terminal three-quarter and C-terminal one quarter fragment of the collagen molecule. Cleavage with cyanogen bromide indicated the presence in the constituent alpha 1(I)-chain of at least four platelet-reactive sites. Our results suggest a relatively wide distribution of platelet-binding sites situated throughout the length of the collagen (type I) molecule, each probably of relatively low affinity and low structural specificity, at least in terms of amino acid sequence, and probably of a similar nature to those that might be expected to exist in any collagen-like species.
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D003094:Collagen / Q000494:pharmacology*; D003488:Cyanogen Bromide; D005976:Glutaral / Q000494:pharmacology; D006801:Humans; D046911:Macromolecular Substances; D003012:Microbial Collagenase; D010446:Peptide Fragments / Q000302:isolation & purification / Q000494:pharmacology*; D010974:Platelet Aggregation / Q000187:drug effects*; D011485:Protein Binding; D011487:Protein Conformation; D012867:Skin
D046911:Macromolecular Substances; D010446:Peptide Fragments; D003094:Collagen; D003012:Microbial Collagenase; D003488:Cyanogen Bromide; D005976:Glutaral