Fibronectin and the multiple interaction model for platelet-collagen adhesion.
A rapid, sensitive, and reproducible assay to determine the adhesion of platelets to collagen has been developed. Collagen fibers and adherent platelets are retained on polycarbonate membrane filters. Chemical modification of collagen by acetylation and of platelets by treatment with chymotrypsin markedly reduces adhesion. The role of fibronectin in the collagen-platelet interaction has been examined. Treatment of platelets with purified antibody or Fab' fragments to fibronectin only slightly reduces adhesion. Preincubation of platelets with high concentrations of gelatin reduces adhesion by only 22% but fails to inhibit aggregation. Thus, fibronectin has only a limited role in the adhesion of platelets to collagen and is either not involved in the adhesion that leads to aggregation or is only one of several adhesion mechanisms, any of which alone can initiate aggregation.
D000818:Animals; D001792:Blood Platelets / Q000502:physiology*; D001798:Blood Proteins / Q000502:physiology*; D002448:Cell Adhesion; D002918:Chymotrypsin; D003094:Collagen; D007140:Immunoglobulin Fab Fragments; D007700:Kinetics; D008565:Membrane Proteins / Q000097:blood*; D010974:Platelet Aggregation; D051381:Rats
D001798:Blood Proteins; D007140:Immunoglobulin Fab Fragments; D008565:Membrane Proteins; D003094:Collagen; D002918:Chymotrypsin