Induction and phosphorylation of protein kinase C-{alpha} and mitogen-activated protein kinase by hypoxia and by radiation in Chinese hamster V79 cells
- Medical Research Council, Oxon (United Kingdom)
- Imperial Cancer Research Fund, London (United Kingdom)
Protein kinase C (PKC) and mitogen-activated protein (MAP) kinase are protein-serine/threonine kinases which are important regulators of diverse cellular processes including metabolism, proliferation and differentiation. This study shows that both hypoxia and X irradiation of serum-deprived Chinese hamster V79 cells cause the induction and phosphorylation of the PKC-{alpha} isoform. The increased induction and phosphorylation of PKC occur mainly in the nuclear fraction. Unlike the PKC activator TPA, neither hypoxic nor radiation stress causes translocation of PKC-{alpha} from the cytosol to the membrane. The induction of PKC-{alpha} by hypoxia is accompanied by an increased expression of MAP kinase but, in contrast, this does not occur when PKC-{alpha} is induced by radiation. Radiation, like TPA, causes a complete redistribution of MAP kinase from the cytosol to the nucleus. 28 refs., 7 figs.
- Sponsoring Organization:
- USDOE
- OSTI ID:
- 387310
- Journal Information:
- Radiation Research, Journal Name: Radiation Research Journal Issue: 2 Vol. 145; ISSN 0033-7587; ISSN RAREAE
- Country of Publication:
- United States
- Language:
- English
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