Plasma fibronectin-C1q complex formation and its effect on C1q inhibition of collagen-induced platelet aggregation.
The first component of complement (C1q) contains a collagen-like structure which evidently accounts for its ability to bind to platelets and to inhibit collagen-induced platelet aggregation. This present investigation explored the interaction among C1q, plasma fibronectin (Pl Fn) and platelets. Gel filtration chromatography (Sepharose 2B and 4B) of preincubated mixtures of C1q and Pl Fn yielded evidence of complex formation. Preincubation of Pl Fn with platelets did not affect collagen-induced platelet aggregation nor did preincubation of Pl Fn with C1q significantly affect C1q-mediated inhibition of collagen-induced platelet aggregation. These observations may indicate that the site of interaction between Pl Fn and C1q is different from the site of interaction between C1q and platelets.
D001792:Blood Platelets / Q000276:immunology; D002850:Chromatography, Gel; D003166:Complement Activating Enzymes / Q000276:immunology*; D015922:Complement C1q; D005353:Fibronectins / Q000097:blood / Q000276:immunology*; D006801:Humans; D010974:Platelet Aggregation
D005353:Fibronectins; D015922:Complement C1q; D003166:Complement Activating Enzymes