Rapid and transient translocation of PLC-gamma 1 to the cytoskeleton of thrombin-stimulated platelets. Evidence for a role of tyrosine kinases.

Cytoskeleton reorganization has been suggested to play an important role in platelet signal transduction. A number of signalling molecules are found to relocalize to this fraction upon thrombin stimulation. In this paper, we show that PLC-gamma 1, a key enzyme of the inositol lipid metabolism, is also translocated to the platelet cytoskeleton upon thrombin stimulation. Interestingly, its translocation is very rapid and transient, and correlates with the increase in PLC activity previously measured in the cytoskeleton by our group. Using a potent tyrosine kinase inhibitor, tyrphostin AG-213, we show a significant inhibition of the translocation of PLC-gamma 1, indicating an involvement of tyrosine kinases in its relocation. Thus, our results demonstrate for the first time a rapid and transient tyrosine kinase-dependent translocation of PLC-gamma 1 to the cytoskeleton of thrombin-stimulated platelets.