The signal transduction pathway of the nonintegrin receptor of 65 kDa is different from glycoprotein VI

The identity and signal pathways of a platelet nonintegrin receptor for type I collagen, 65 kDa, are not established. In this investigation, we have examined whether there is a difference in the signal transduction pathways between the 65-kDa protein and glycoprotein VI (GP VI). Results from this study show that these two proteins are different based on the following facts. First, the anti-65-kDa antibody does not precipitate GP VI and vice versa. Second, the Fc receptor (FcR) γ chain which associates with GP VI after exposure to collagen does not associate with the 65-kDa protein. Third, tyrosine phosphorylation of the FcR γ chain was obtained by Fab fragments of anti-GP VI but not by anti-65 kDa. These results suggest that the signal transduction pathway of the platelet receptors for the 65-kDa protein and GP VI are different.