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Thromb Haemost 1986; 56(01): 095-099
DOI: 10.1055/s-0038-1661610
Original Article
Schattauer GmbH Stuttgart

The Platelet Reactivity of Collagen Type I: Evidence for Multiple Platelet-Reactive Sites in the Type I Collagen Molecule

C M Fitzsimmons
Strangeways Research Laboratory, Cambridge, UK
,
T E Cawston
*   The Rheumatology Research Unit at Addenbrooke’s Hospital, Cambridge, UK
,
M J Barnes
Strangeways Research Laboratory, Cambridge, UK
› Author Affiliations
Further Information

Publication History

Received 03 April 1986

Accepted 09 September 1986

Publication Date:
13 July 2018 (online)

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Summary

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 cq^-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.

Keywords

Platelets - Collagen - Platelet-reactive sites
 

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