Adhesion of human platelets to immobilized trimeric collagen.

Human platelets adhere to trimeric Type 1 chick collagen that was covalently linked to plastic slides, providing the basis for a well-defined quantitative assay. The number of platelets that adhere is a function both of platelet concentration and of collagen density on the slides. In contrast with other in vitro assays using collagen that is not covalently linked to the substratum, we found no platelet-platelet aggregation. Adhesion was absolutely dependent on Mg2+, whereas Ca2+ was ineffective. Native trimeric collagen conformation was required for adhesion, since platelets did not bind to slides containing heat-denatured collagen, or isolated alpha 1(1) or or alpha 2(1) chains. Modifications of collagen oligosaccharides had no effect on adhesion. Adhesion was inhibited by cytochalasin D but was not affected by prostaglandin E1, apyrase, acetylsalicylic acid, or theophylline. Because this assay measures platelet-collagen adhesion in the absence of platelet-platelet aggregation, it should facilitate identification of the platelet surface components that directly mediate this adhesion.