Association of pp60src with Triton X-100-insoluble residue in human blood platelets requires platelet aggregation and actin polymerization.

@article{Oda1992AssociationOP,
  title={Association of pp60src with Triton X-100-insoluble residue in human blood platelets requires platelet aggregation and actin polymerization.},
  author={Atsushi Oda and Brian J. Druker and Michael Smith and Edwin W. Salzman},
  journal={The Journal of biological chemistry},
  year={1992},
  volume={267 28},
  pages={20075-81}
}
Protein-tyrosine phosphorylation during platelet activation is inhibited under conditions that inhibit platelet binding of fibrinogen and aggregation. We suggested that pp60src, a major platelet tyrosine kinase, or its protein substrates might become associated with the cytoskeleton upon platelet stimulation, and that this might be related to aggregation. By Western blotting with an anti-Src monoclonal antibody, we found time-dependent association of pp60src with the cytoskeleton (10,000 x g… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-8 of 8 extracted citations

Similar Papers

Loading similar papers…