A freeze-fracture and thin section study of the interaction of blood platelets with native type I collagen fibrils.
The membranes of non-activated and activated human blood platelets have been studied with freeze-fracture and conventional electron microscopy. Aggregated platelets activated by ADP or by native collagen fibrils did not show any intramembrane particle clustering. No intramembrane modification is detectable at the contact regions with collagen fibrils. However, a local densification of the cortical cytoplasm is noted in thin sections where platelets make contact with collagen fibrils. These results suggest that either the membrane receptor for collagen is not visualized by freeze-fracturing or that, as suggested previously, the binding site on collagen may not have a specificity and affinity as high as expected from a conventional receptor-ligand interaction.
D001792:Blood Platelets / Q000378:metabolism* / Q000648:ultrastructure; D002462:Cell Membrane / Q000648:ultrastructure; D003094:Collagen / Q000378:metabolism* / Q000494:pharmacology; D005614:Freeze Fracturing; D006801:Humans; D066298:In Vitro Techniques; D008854:Microscopy, Electron; D010974:Platelet Aggregation / Q000187:drug effects
D003094:Collagen