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Vasoconstrictor‐induced protein‐tyrosine phosphorylation in cultured vascular smooth muscle cells
Author(s) -
Tsuda Terutaka,
Kawahara Yasuhiro,
Shii Kozui,
Koide Masanobu,
Ishida Yoshihiro,
Yokoyama Mitsuhiro
Publication year - 1991
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(91)80721-e
Subject(s) - tyrosine phosphorylation , phosphorylation , ionomycin , vascular smooth muscle , protein kinase c , angiotensin ii , tyrosine , protein tyrosine phosphatase , protein phosphorylation , tyrosine kinase , microbiology and biotechnology , chemistry , receptor tyrosine kinase , biology , protein kinase a , medicine , biochemistry , endocrinology , intracellular , signal transduction , receptor , smooth muscle
In cultured rat aortic smooth muscle cells, angiotensin II induced tyrosine phosphorylation of at least 9 proteins with molecular masses of 190, 117, 105, 82, 79, 77, 73, 45 and 40 kDa in time‐ and dose‐dependent manners. Other vasoconstrictors such as [Arg]vasopressin, 5‐hydroxytryptamine and norepinephrine induced the tyrosine phosphorylation of the same set of proteins as angiotensin II. The tyrosine phosphorylation of these proteins was mimicked by the protein kinase C‐activating phorbol ester, phorbol 12 myristate, 13‐acetate, and the Ca 2+ ionophore, ionomycin. These results demonstrate that the vasoconstrictors stimulate the tyrosine phosphorylation of several proteins in vascular smooth muscle cells and suggest that the tyrosine phosphorylation reactions are the events distal to the activation of protein kinase C and Ca 2+ mobilization in the intracellular signalling pathways of the vasoconstrictors.