Thrombospondin promotes cell-substratum adhesion.
The physiological role of the platelet-secreted protein thrombospondin (TSP) is poorly understood, although it has been postulated to be involved in platelet aggregation and cellular adhesion. In this report, TSP isolated from human platelets was found to promote, in vitro, the cell-substratum adhesion of a variety of cells, including platelets, melanoma cells, muscle cells, endothelial cells, fibroblasts, and epithelial cells. The adhesion-promoting activity of TSP was species independent, specific, and not due to contamination by fibronectin, vitronectin, laminin, or platelet factor 4. The cell surface receptor for TSP is protein in nature and appears distinct from that for fibronectin.
D000818:Animals; D018955:CD36 Antigens; D002417:Cattle; D002448:Cell Adhesion / Q000187:drug effects*; D005347:Fibroblasts / Q000187:drug effects; D005353:Fibronectins / Q000494:pharmacology; D006023:Glycoproteins / Q000494:pharmacology*; D006801:Humans; D008545:Melanoma / Q000378:metabolism; D051379:Mice; D010974:Platelet Aggregation / Q000187:drug effects; D011817:Rabbits; D051381:Rats; D011975:Receptors, Mitogen / Q000378:metabolism; D013552:Swine; D019699:Thrombospondins
D018955:CD36 Antigens; D005353:Fibronectins; D006023:Glycoproteins; D011975:Receptors, Mitogen; D019699:Thrombospondins