Inhibition of 80 kDa protein phosphorylation by short-wavelength UV light in NIH 3T3 cells

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The exposure of NIH 3T3 fibroblast cells to 254 nm UV radiation resulted in a temporary depression of DNA synthesis and inhibition of 80 kDa protein phosphorylation. This inhibition of protein phosphorylation was correlated with decreased protein kinase C activity in the membrane fractions of UV-damaged cells. The inositol triphosphate contents measured, by the competitive binding assay using bovine adrenal binding protein, showed 80% reduction in the fibroblasts treated with 15 J/m2 of UV light. The intracellular diacylglycerol concentration was also markedly reduced in UV-damaged cells. The results suggest that UV light causes acute reductions of inositol triphosphate and diacylglycerol contents in cells along with decreases in membrane protein kinase C activity, which leads to the inhibition of phosphorylation of an acidic protein of 80 kDa.
Publisher
AMER SOC PHOTOBIOLOGY
Issue Date
1993-10
Language
English
Article Type
Article
Keywords

KINASE-C; GROWTH-FACTOR; ULTRAVIOLET-LIGHT; PHORBOL ESTERS; SIGNAL TRANSDUCTION; SWISS 3T3-CELLS; DNA-REPLICATION; ACTIVATION; TRANSFORMATION; TRANSLOCATION

Citation

PHOTOCHEMISTRY AND PHOTOBIOLOGY, v.58, no.4, pp.536 - 540

ISSN
0031-8655
URI
http://hdl.handle.net/10203/57858
Appears in Collection
BS-Journal Papers(저널논문)
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