INHIBITION OF 80 KDA PROTEIN-PHOSPHORYLATION BY SHORT-WAVELENGTH UV-LIGHT IN NIH 3T3 CELLS
- Authors
- Shin, Incheol; Yoon, Yoo Sik; Kang, Kewon; Park, Sang Dai; Joe, Cheol O
- Issue Date
- Oct-1993
- Publisher
- AMER SOC PHOTOBIOLOGY
- Citation
- PHOTOCHEMISTRY AND PHOTOBIOLOGY, v.58, no.4, pp 536 - 540
- Pages
- 5
- Journal Title
- PHOTOCHEMISTRY AND PHOTOBIOLOGY
- Volume
- 58
- Number
- 4
- Start Page
- 536
- End Page
- 540
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/67066
- DOI
- 10.1111/j.1751-1097.1993.tb04928.x
- ISSN
- 0031-8655
1751-1097
- Abstract
- 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.
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