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Catalytic subunit of cAMP‐dependent protein kinase is essential for cAMP‐mediated mammalian gene expression
Author(s) -
Büchler W.,
Walter U.,
Jastorff B.,
Lohmann S.M.
Publication year - 1988
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(88)80577-5
Subject(s) - protein subunit , protein kinase a , gene , microbiology and biotechnology , chemistry , map3k7 , gene expression , biology , kinase , biochemistry , mitogen activated protein kinase kinase
Cyclic AMP‐stimulated mRNA levels in cultured rat hepatocytes were inhibited by three different inhibitors of cAMP‐dependent protein kinase activity: (i) Rp‐cAMPS, a cAMP analog with a sulfur substitution at the equatorial oxygen of the cyclic monophosphate; (ii) H8, an isoquinoline sulfonamide derivative; and (iii) PKI, a 20‐amino acid synthetic peptide of the Walsh protein kinase inhibitor. These inhibitors specifically blocked the cAMP‐stimulated increase in mRNA for tyrosine aminotransferase and phospho enol pyruvate carboxykinase; they had no effect on the level of albumin mRNA which is not cAMP regulated. These results provide functional evidence that kinase activity involving protein phosphorylation is required in cAMP‐mediated gene expression in mammalian cells.