Catalytic subunit of cAMP-dependent protein kinase is essential for cAMP-mediated mammalian gene expression
In: FEBS Letters, Jg. 228 (1988-02-08), S. 27-32
Online
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Zugriff:
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 phosphoenolpyruvate 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.
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Catalytic subunit of cAMP-dependent protein kinase is essential for cAMP-mediated mammalian gene expression
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Autor/in / Beteiligte Person: | Jastorff, Bernd ; Lohmann, Suzanne M. ; Büchler, W. ; Walter, Ulrich |
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Zeitschrift: | FEBS Letters, Jg. 228 (1988-02-08), S. 27-32 |
Veröffentlichung: | Wiley, 1988 |
Medientyp: | unknown |
ISSN: | 0014-5793 (print) |
DOI: | 10.1016/0014-5793(88)80577-5 |
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