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Insulin but not phorbol ester treatment increases phosphorylation of vinculin by protein kinase C in BC3H‐1 myocytes
Author(s) -
Cooper Denise R.,
de Ruiz Galaretta Carlos M.,
Fanjul Luisa F.,
Mojsilovic Ljubomir,
Standaert Mary L.,
Pollet Robert J.,
Farese Robert V.
Publication year - 1987
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(87)80025-x
Subject(s) - protein kinase c , phorbol ester , chemistry , phosphorylation , myocyte , insulin , phorbol , vinculin , immunoprecipitation , microbiology and biotechnology , biochemistry , endocrinology , biology , focal adhesion , gene
Insulin was found to increase protein kinase C activity in BC3H‐1 myocytes as determined by in vitro phosphorylation of both a lysine‐rich histone fraction (histone III‐S) and vinculin. TPA treatment for 20 min or 18 h provoked an apparent loss of histone‐directed but not vinculin‐directed phosphorylation by cytosolic C‐kinase. Thus, chronic TPA‐induced ‘desensitization’ or ‘depletion’ of cellular protein kinase C is more apparent than real, and is not a valid means for evaluating the role of C‐kinase in hormone action.