c-myc gene expression is stimulated by agents that activate protein kinase C and does not account for the mitogenic effect of PDGF
Autor: | William M. Lee, Gertrud M. Giels, Shaun R. Coughlin, Lewis T. Williams, Perry W. Williams |
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Rok vydání: | 1985 |
Předmět: |
Vasopressins
Mitogen-activated protein kinase kinase Bradykinin Phosphatidylinositols General Biochemistry Genetics and Molecular Biology Cell Line Diglycerides chemistry.chemical_compound Proto-Oncogenes Animals Humans RNA Messenger Protein kinase A Protein kinase C Protein Kinase C Platelet-Derived Growth Factor MAP kinase kinase kinase biology Epidermal Growth Factor Kinase DNA Molecular biology Enzyme Activation chemistry Mitogen-activated protein kinase biology.protein Phorbol Tetradecanoylphorbol Acetate Mitogens Platelet-derived growth factor receptor Cell Division Thymidine |
Zdroj: | Cell. 43(1) |
ISSN: | 0092-8674 |
Popis: | The role of the phosphoinositide turnover-protein kinase C pathway in mediating PDGF-stimulated c- myc expression and cell proliferation was studied. Both direct activators of kinase C (e.g. phorbol ester analogues) and hormones that activate kinase C via receptor-mediated phosphoinositide turnover (e.g. PDGF, bradykinin, or vasopressin) elicited a rapid increase in c- myc mRNA expression. Desensitization of the kinase C pathway by prolonged exposure to phorbol abolished the induction of c- myc by subsequent phorbol challenge and attenuated c- myc induction by PDGF a bradykinin, but did not affect PDGF-stimulated mitogenesis. Bradykinin and phorbol esters stimulated the same magnitude of c- myc expression as PDGF but elicited less than one-tenth the PDGF-induced mitogenic response. We conclude that stimulation of c- myc expression is a common response to a diverse group of agents that elicit phosphoinositide turnover and activate protein kinase C, and that neither activation of protein kinase C nor enhanced c- myc expression is sufficient for the mitogenic action of PDGF. |
Databáze: | OpenAIRE |
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