Deoxycholic acid can induce apoptosis in the human colon cancer cell line HCT116 in the absence of bax

Nutrition and Cancer

Volumn 60, Issue 1, 2008, Pages 91-96

  Yui, Satoko ^a   Kanamoto, Ryuhei ^a   Saeki, Tohru ^a  

^a KYOTO PREFECTURAL UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 3; CASPASE 8; CASPASE 9; CYTOCHROME C; DEOXYCHOLIC ACID; PROTEIN BAX; PROTEIN BCL 2; URSODEOXYCHOLIC ACID;

APOPTOSIS; ARTICLE; CANCER CELL; CELL LINE; CELL STRAIN HCT116; COLON CANCER; CONTROLLED STUDY; DRUG MECHANISM; ENZYME ACTIVATION; HUMAN; HUMAN CELL; MITOCHONDRION; PROTEIN FAMILY; PROTEIN SECRETION;

APOPTOSIS; BCL-2-ASSOCIATED X PROTEIN; CASPASE 3; CASPASE 8; CASPASE 9; CASPASES; COLONIC NEOPLASMS; DEOXYCHOLIC ACID; ENZYME ACTIVATION; HCT116 CELLS; HUMANS; URSODEOXYCHOLIC ACID;

EID: 38749092227     PISSN: 01635581     EISSN: None     Source Type: Journal    
DOI: 10.1080/01635580701525893     Document Type: Article

References (33)

1. Li P, Nijhawan D, Budihardjo I, Srinivasula SM, Ahmad M, et al.: Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91, 479-489, 1997.
2. Bossy-Wetzel E, Newmeyer DD, and Green DR: Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization. EMBO J 17, 37-49, 1998.
3. Jurgensmeier JM, Xie Z, Deveraux Q, Ellerby L, Bredesen D, et al.: Bax directly induces release of cytochrome c from isolated mitochondria. Proc Natl Acad Sci USA 95, 4997-5002, 1998.
4. Eskes R, Desagher S, Antonsson B, and Martinou JC: Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane. Mol Cell Biol 20, 929-935, 2000.
5. Antonsson B, Montessuit S, Lauper S, Eskes R, and Martinou JC: Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria. Biochem J 345(Pt 2), 271-278, 2000.
6. Adachi M, Higuchi H, Miura S, Azuma T, Inokuchi S, et al.: Bax interacts with the voltage-dependent anion channel and mediates ethanol-induced apoptosis in rat hepatocytes. Am J Physiol Gastrointest Liver Physiol 287, G695-705, 2004.
7. Kuwana T, Mackey MR, Perkins G, Ellisman MH, Latterich M, et al.: Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane. Cell 111, 331-342, 2002.
8. Shimizu S, Narita M, and Tsujimoto Y: Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature 399, 483-487, 1999.
9. Yui S, Saeki T, Kanamoto R, and Iwami K: Characteristics of apoptosis in HCT116 colon cancer cells induced by deoxycholic acid. J Biochem (Tokyo) 138, 151-157, 2005.
10. Theodorakis P, Lomonosova E, and Chinnadurai G: Critical requirement of BAX for manifestation of apoptosis induced by multiple stimuli in human epithelial cancer cells. Cancer Res 62, 3373-3376, 2002.
11. Yamaguchi H, Bhalla K, and Wang HG: Bax plays a pivotal role in thapsigargin-induced apoptosis of human colon cancer HCT116 cells by controlling Smac/Diablo and Omi/HtrA2 release from mitochondria. Cancer Res 63, 1483-1489, 2003.
12. Zhang L, Yu J, Park BH, Kinzler KW, and Vogelstein B: Role of Bax in the apoptotic response to anticancer agents. Science 290, 989-992, 2000.
13. Rashmi R, Kumar S, and Karunagaran D: Human colon cancer cells lacking Bax resist curcumin-induced apoptosis and Bax requirement is dispensable with ectopic expression of Smac or downregulation of Bcl-XL. Carcinogenesis 26, 713-723, 2005.
14. Subramanian T and Chinnadurai G: Pro-apoptotic activity of transiently expressed Bcl-2 occurs independent of Bax and Bak. J Cell Biochem 89, 1102-1114, 2003.
15. Zhao Y, Li S, Childs EE, Kuharsky DK, and Yin XM: Activation of prodeath Bcl-2 family proteins and mitochondria apoptosis pathway in tumor necrosis factor-alpha-induced liver injury. J Biol Chem 276, 27432-27440, 2001.
16. Qian W, Nishikawa M, Haque AM, Hirose M, Mashimo M, et al.: Mitochondrial density determines the cellular sensitivity to cisplatin-induced cell death. Am J Physiol Cell Physiol 289, C1466-1475, 2005.
17. Antonsson B, Montessuit S, Sanchez B, and Martinou JC: Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells. J Biol Chem 276, 11615-11623, 2001.
18. Marchetti C, Migliorati G, Moraca R, Riccardi C, Nicoletti I, et al.: Deoxycholic acid and SCFA-induced apoptosis in the human tumor cell-line HT-29 and possible mechanisms. Cancer Lett 114, 97-99, 1997.
19. Korsmeyer SJ, Wei MC, Saito M, Weiler S, Oh KJ, et al.: Pro-apoptotic cascade activates BID, which oligomerizes Bak or Bax into pores that result in the release of cytochrome c. Cell Death Differ 7, 1166-1173, 2000.
20. Yin XM: Signal transduction mediated by Bid, a pro-death Bcl-2 family proteins, connects the death receptor and mitochondria apoptosis pathways. Cell Res 10, 161-167, 2000.
21. Gross A, McDonnell JM, and Korsmeyer SJ: Bcl-2 family members and the mitochondria in apoptosis. Genes Dev 13, 1899-1911, 1999.
22. Pusl T and Beuers U: Ursodeoxycholic acid treatment of vanishing bile duct syndromes. World J Gastroenterol 12, 3487-3495, 2006.
23. Rodrigues CM, Fan G, Ma X, Kren BT, and Steer CJ: A novel role for ursodeoxycholic acid in inhibiting apoptosis by modulating mitochondrial membrane perturbation. J Clin Invest 101, 2790-2799, 1998.
24. Rodrigues CM, Fan G, Wong PY, Kren BT, and Steer CJ: Ursodeoxycholic acid may inhibit deoxycholic acid-induced apoptosis by modulating mitochondrial transmembrane potential and reactive oxygen species production. Mol Med 4, 165-178, 1998.
25. Rodrigues CM, Ma X, Linehan-Stieers C, Fan G, Kren BT, et al.: Ursodeoxycholic acid prevents cytochrome c release in apoptosis by inhibiting mitochondrial membrane depolarization and channel formation. Cell Death Differ 6, 842-854, 1999.
26. Im E, Akare S, Powell A, and Martinez JD: Ursodeoxycholic acid can suppress deoxycholic acid-induced apoptosis by stimulating Akt/PKB-dependent survival signaling. Nutr Cancer 51, 110-116, 2005.
27. Brunet A, Bonni A, Zigmond MJ, Lin MZ, Juo P, et al.: Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor. Cell 96, 857-868, 1999.
28. Cardone MH, Roy N, Stennicke HR, Salvesen GS, Franke TF, et al.: Regulation of cell death protease caspase-9 by phosphorylation. Science 282, 1318-1321, 1998.
29. Datta SR, Dudek H, Tao X, Masters S, Fu H, et al.: Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell 91, 231-241, 1997.
30. Masuyama N, Oishi K, Mori Y, Ueno T, Takahama Y, et al.: Akt inhibits the orphan nuclear receptor Nur77 and T-cell apoptosis. J Biol Chem 276, 32799-32805, 2001.
31. Lindsten T, Ross AJ, King A, Zong WX, Rathmell JC, et al.: The combined functions of proapoptotic Bcl-2 family members Bak and Bax are essential for normal development of multiple tissues. Mol Cell 6, 1389-1399, 2000.
32. Opferman JT and Korsmeyer SJ: Apoptosis in the development and maintenance of the immune system. Nat Immunol 4, 410-415, 2003.
33. Srinivasula SM, Ahmad M, Fernandes-Alnemri T, and Alnemri ES: Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization. Mol Cell 1, 949-957, 1998.