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Prevention of TNF-induced necrotic cell death by rottlerinthrough a Nox1 NADPH oxidase
변희선,원민호,박경아,김영래,Byung Lyul Choi,Hyunji Lee,Jang Hee Hong,Longzhen Piao,박종선,김진만,Gi Ryang Kweon,Sung Hyun Kang,한진,허강민 생화학분자생물학회 2008 Experimental and molecular medicine Vol.40 No.2
Previous studies have demonstrated that rottlerin, a specific PKCδ inhibitor, potentiates death receptor- mediated apoptosis through a cytochrome c-depend-ent or -independent pathway. However, its ability to regulate necrotic cell death, as well as the underlying ine fibrosarcoma L929 cells, treatment with rotlerin protected the cells against TNF-induced necrosis, whereas it sensitized the cels to apoptosis induced by co-treatment with Hsp90 inhibitor geldanamycin and TNF, in a maner independent of its ability to inhibit PKC-δ. TNF treatment induced rapid accumulation of mitochondrial superoxide (O2-) through the Nox1 NADPH oxidase when cells undergo necrosis. More-GTP-bound form of small GTPase Rac1 by TNF treat-ment, and subsequently suppressed mitochondrial O2- production and poly(ADP-ribose) polymerase activa-tion, thus inhibiting necrotic cell death. Therefore, our study suggests that Nox1 NADPH oxidase is a new mo-lecular target for anti-necrotic activity of rotlerin upon death-receptor ligation.
p53에 의한 HIV - 1 Tat 활성억제와 인산화관련 가능성 연구
변희선,이상구,배용수 대한바이러스학회 1998 Journal of Bacteriology and Virology Vol.28 No.1
HIV-1 tat, a strong transactivator, is essential for the HIV-1 replication and AIDS progression. The Tat function is markedly inhibited by human anti-oncogene p53. This work was initiated to identify the p53-associated inhibitory mechanism on tat-mediated transactivation. Inhibitory function of p53 was confirmed by co-transfection of tat-expressing Jurkat cells with LTR-CAT plasmid, or H3T1 cells (LTR-CAT integrated HeLa cells) with different ratio of pSV-tat/pCDNA- p53 plasmids. Results from the direct protein-protein interaction between soluble p53 and tat, and yeast two-hybrid experiments showed that the co-suppression mechanism is unlikely to be due to the direct interaction. CAT activity was not affected by tat in Jurkat cells which were transfected with p53-promoter-CAT or p53-enhancer-CAT, suggesting that the tat-mediated p53 suppression is not directly associated with p53-promoter. Finally, we have tested protein kinase activity in p53-tranfected Jurkat cells, which might phosphorylate HIV-1 tat, resulting in inhibition of tat function. Some of our data lead us to assurne that the p53-mediated tat inhibition is likely to be associated with p53-associated, signaling-mediated phosphorylation of tat, resulting in the dysfunction of tat. This study is now under investigation.