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Apicidin, Histone Deacetylase Inhibitor에 의한 Human Promyelocytic U937 세포고사
정은현(Eun-Hynu Jung),박찬희(Channy Park),임창인(Chang-In Lim),이황희(Hwanghee Blaise Lee),송훈섭(Hoon-Seob Song),염성섭(Seong-Seob Yeom),정은배(Eun-Bae Jung),이병곤(Byeong-Gon Lee),김영훈(Young-Hoon Kim),박래길(Raekil Park) 한국독성학회 2003 Toxicological Research Vol.19 No.3
Apicidin, a histone-deacetylase inhibitor, has been successfully used to inhibit the growth of cancer cells. In this study, the apoptotic potential and mechanistic insights of apicidin were<br/> investigated in human myeloid leukemia U937 cells. Treatment of U937 cells with apicidin resulted in a decrease of cell viability with apoptotic characteristics, including chromatin condensation and ladderpattern fragmentation of genomic DNA. Apicidin converted the procaspase-3 protease to catalytically active effector protease, resulting in subsequent cleavage of poly (ADP-ribose) polymerase (PARP) and inhibitor of caspase-activated deoxyribonuclease (ICAD). In addition, apicidin induced the activation of caspase-9 protease and the cytosolic release of mitochondrial cytochrome c with mitochondrial membrane potential transition. Moreover, apicidin transiently increased the expression of Fas and Fas ligand proteins. Taken together, the results suggest that apicidin induces apoptosis of U937 cells through activation of intrinsic caspase cascades and Fas/FasL system with mitochondrial dysfunction.