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Citation Information: J Clin Invest. 1973;52(10):2495-2506. https://doi.org/10.1172/JCI107440.
Abstract
In an effort to elucidate the nature of the collagen-platelet interaction, the effects of collagen modification on platelet aggregation have been studied. We have shown that purified rat skin (salt) soluble collagen is effective at about 20 nM in mediating platelet aggregation in human platelet-rich plasma. This concentration is somewhat greater than that required of several skin insoluble collagens (ca. 10 nM). Both the α1(I) and α2 chains from rat skin soluble collagen produced platelet aggregation, but only at concentrations of about 13 μM and 55 μM, respectively. In contrast, heat-denatured collagen and chains (e.g., 65 μM α1(I) and 160 μM α2) failed to induce platelet aggregation and to inhibit platelet aggregation by native collagen.
Authors
David Puett, Betty Kay Wasserman, John D. Ford, Leon W. Cunningham
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