Tyrosine-specific protein phosphorylation is regulated by glycoprotein IIb-IIIa in platelets.

@article{Ferrell1989TyrosinespecificPP,
  title={Tyrosine-specific protein phosphorylation is regulated by glycoprotein IIb-IIIa in platelets.},
  author={James E Ferrell and Geoffrey S. Martin},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1989},
  volume={86 7},
  pages={
          2234-8
        }
}
We have previously shown that a number of platelet proteins become phosphorylated at tyrosine residues in response to platelet-activating agents. Here we present two lines of evidence implicating a platelet integrin, glycoprotein IIb-IIIa, in the regulation of a specific subset of these tyrosine phosphorylations. (i) Two peptides that inhibit the binding of fibrinogen and other ligands to gpIIb-IIIa, Arg-Gly-Asp-Ser and His-His-Leu-Gly-Gly-Ala-Lys-Gln-Ala-Gly-Asp-Val, also inhibited the… CONTINUE READING
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