Participation of calpain in protein-tyrosine phosphorylation and dephosphorylation in human blood platelets.

@article{Ariyoshi1995ParticipationOC,
  title={Participation of calpain in protein-tyrosine phosphorylation and dephosphorylation in human blood platelets.},
  author={Hideo Ariyoshi and Atsushi Oda and Edwin W. Salzman},
  journal={Arteriosclerosis, thrombosis, and vascular biology},
  year={1995},
  volume={15 4},
  pages={511-4}
}
The possible role of calpains in protein-tyrosine phosphorylation in platelets was examined by the use of the cell-permeant calpain inhibitor calpeptin. In platelets stimulated by 1 U/mL thrombin, protein-tyrosine phosphorylation was maximal after 2 minutes and was followed by protein-tyrosine dephosphorylation. Calpeptin (30 mumol/L) or vanadate (2 mmol/L) enhanced protein-tyrosine phosphorylation and delayed protein-tyrosine dephosphorylation. The effects of these two compounds were not… CONTINUE READING

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CalpainGene product plays role in biological processProteolysis
We also observed proteolysis of pp60src and autoproteolysis of mu - calpain .
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