INHIBITION OF 80 kDa PROTEIN PHOSPHORYLATION BY SHORT-WAVELENGTH UV LIGHT IN NIH 3T3 CELLS

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 tnphosphate 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.