Premium
Calcium mobilisation controls tyrosine protein phosphorylation independently of the activation of protein kinase C in human platelets
Author(s) -
Falet Hervé,
Rendu Francine
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00414-5
Subject(s) - tyrosine phosphorylation , protein kinase c , protein tyrosine phosphatase , phosphorylation , protein phosphorylation , thapsigargin , tyrosine , tyrosine kinase , chemistry , microbiology and biotechnology , biochemistry , protein kinase a , biology , signal transduction , intracellular
We have investigated the regulation of tyrosine proteins phosphorylation by intracellular Ca 2+ level ([Ca 2+ ] i ) and protein kinase C (PKC) during platelet stimulation. We found that chelation of extracellular calcium completely prevented phosphorylation of tyrosine proteins induced by thapsigargin and phorbol 12‐myristate 13‐acetate (PMA), whereas, when induced by thrombin, it prevented a subset of tyrosine proteins. The selective inhibition of PKC by OF 109203X did not abolish tyrosine protein phosphorylation when induced by thrombin and thapsigargin. The results suggest that in human platelets tyrosine protein phosphorylation is dependent on [Ca 2+ ] i , although direct PKC activation can also induce phosphorylation of tyrosine proteins.