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Vasopressin stimulates tyrosine phosphorylation by activation of pkc in the rat smooth muscle cell line, a‐10
Author(s) -
Gonzalez CARLOS B.,
Reyes Carlos E.,
Figueroa Carlos D.,
Barra Valeria,
Troncoso Silvia
Publication year - 1999
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1006/cbir.1999.0343
Subject(s) - phosphorylation , protein kinase c , tyrosine phosphorylation , staurosporine , phosphoserine , heterotrimeric g protein , protein phosphorylation , bisindolylmaleimide , biology , vasopressin , microbiology and biotechnology , chemistry , signal transduction , endocrinology , protein kinase a , g protein , serine
Arginine vasopressin (AVP)‐induced tyrosine phosphorylation was studied in a rat smooth muscle cell line, A‐10, by western blotting, using a monoclonal antibody against phosphotyrosine. AVP stimulated the phosphorylation of several cellular proteins of molecular mass 60–130kDa in a time‐ and dose‐dependent manner. Phosphorylation was mediated largely by V 1 receptor subtype since it was inhibited by selective V 1 antagonist and was only partially elicited by the V 2 agonist, desmopressin. Heterotrimeric G‐proteins seemed to be involved in the phosphorylation mechanism because fluoraluminates, an activator of heterotrimeric G‐proteins (and thus an uncoupler of the receptor—G‐protein interaction) inhibited the AVP‐induced phosphorylation. The protein kinase C (PKC) inhibitors: staurosporine, H7 and GF109203X are able to block the AVP‐stimulated phosphorylation. The last of these has been shown to be one of the most selective inhibitors of PKC. These results indicate that PKC is upstream of the phosphorylation, a motion which is supported by the fact that the AVP‐stimulated phosphorylation was downregulated by phorbol esters.