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자료유형
학술저널
저자정보
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대한생화학·분자생물학회 Experimental and Molecular Medicine Experimental and Molecular Medicine 제36권 제5호
발행연도
2004.1
수록면
454 - 460 (7page)

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Hepatitis C Virus (HCV) is associated with a severe liver disease and increased frequency in Overexpresion of HCV core protein is known to transform fibroblast cells. Phospholipase D (PLD) activity is comonly elevated in response to mitogenic signals, and has also ben overex-pressed and hyperactivated in some human cancer cels. The aim of this study was to understand how PLD was regulated in the HCV core protein-transformed NIH3T3 mouse fibro-blast cels. We observed that PLD activity was elevated in the NIH3T3 cels overexpresing HCV core protein over the vector alone-trans-of PLD protein and protein kinase C (PKC) in the HCV core protein-transformed cels was si-milar to the control cells. Phorbol 12-myristate 13-acetate (PMA), which is known to activate PKC, stimulated PLD activity significantly more in the core protein-transformed cels, in com-parison with that of the control cels. PLD activity assay using PKC isozyme-specific inhi-bitor and PKC translocation experiment showed that PKC-δ was mainly involved in the PMA- cells. Moreover, in cells overexpresing HCV core protein, PMA also stimulated p38 kinase more potently than that of the control cels, and an inhibitor of p38 kinase abolished PMA-in-duced PLD activation in cells overexpressing HCV core protein. Taken together, these results sugest that PLD might be implicated in core protein-induced transformation.

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