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자료유형
학술저널
저자정보
저널정보
대한생화학·분자생물학회 Experimental and Molecular Medicine Experimental and Molecular Medicine 제37권 제5호
발행연도
2005.1
수록면
418 - 426 (9page)

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Phospholipase D (PLD) activity is known to be related to oxidant-induced cellular signaling and membrane disturbance. Previously, an induction of PLD activity in various cell lines by X-ray irradiation was observed. In this study, we examined the effect of UVC radia-10 kJ/m2of UVC irradiation, the PLD activity was stimulated approximately 10-fold over the basal activity. This UVC-induced PLD activity was found to be dependent on the presence of extracellular calcium and was inhibited by catalase as well as amifostine - an intracellular thiol antioxidant. Pre-treatments with Ro32-0432 - a selective inhibitor of protein kinase C (PKC) - and downregulation of PKC by preincubation of phorbol 12-myristate 13-acetate significantly inhibited the UVC-induced PLD activity. UVC-stimulated PLD activity was observed only in murine PLD2 (mPLD2)-transfected Vero 76 cells and not in human PLD1 (hPLD1)-transfected cells. Tran-sient incorporation of PKC with mPLD2 and the phosphorylation of mPLD2 byα and β forms of PKC by UVC irradiation were observed. These results suggest that the UVC-stimulated PLD activity in Vero 76 cells is mediated through transient phosphor-ylation of PLD2 by the translocation of PKC to PLD2.

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