메뉴 건너뛰기




Volumn 287, Issue 3 50-3, 2004, Pages

Bax interacts with the voltage-dependent anion channel and mediates ethanol-induced apoptosis in rat hepatocytes

Author keywords

Alcoholic liver disease; Cytochrome c; Mitochondria; Oxidative stress

Indexed keywords

ALCOHOL; ANION CHANNEL; ANTIBODY; CYTOCHROME C; PROTEIN BAX; PROTEIN BCL 2;

EID: 4143093663     PISSN: 01931857     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpgi.00415.2003     Document Type: Article
Times cited : (98)

References (42)
  • 1
    • 0035853811 scopus 로고    scopus 로고
    • Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells
    • 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.
    • (2001) J Biol Chem , vol.276 , pp. 11615-11623
    • Antonsson, B.1    Montessuit, S.2    Sanchez, B.3    Martinou, J.C.4
  • 3
    • 0030592172 scopus 로고    scopus 로고
    • The permeability transition pore. Control points of a cyclosporin A-sensitive mitochondrial channel involved in cell death
    • Bernardi P. The permeability transition pore. Control points of a cyclosporin A-sensitive mitochondrial channel involved in cell death. Biochim Biophys Acta 1275: 5-9, 1996.
    • (1996) Biochim Biophys Acta , vol.1275 , pp. 5-9
    • Bernardi, P.1
  • 4
    • 0344653616 scopus 로고    scopus 로고
    • Complexes between porin, hexokinase, mitochondrial creatine kinase and adenylate translocator display properties of the permeability transition pore. Implication for regulation of permeability transition by the kinases
    • Beutner G, Ruck A, Riede B, and Brdiczka D. Complexes between porin, hexokinase, mitochondrial creatine kinase and adenylate translocator display properties of the permeability transition pore. Implication for regulation of permeability transition by the kinases. Biochim Biophys Acta 1368: 7-18, 1998.
    • (1998) Biochim Biophys Acta , vol.1368 , pp. 7-18
    • Beutner, G.1    Ruck, A.2    Riede, B.3    Brdiczka, D.4
  • 5
    • 0021027358 scopus 로고
    • Detection of picomole levels of hydroperoxides using a fluorescent dichlorofluorescein assay
    • Cathcart R, Schwiers E, and Ames BN. Detection of picomole levels of hydroperoxides using a fluorescent dichlorofluorescein assay. Anal Biochem 134: 111-116, 1983.
    • (1983) Anal Biochem , vol.134 , pp. 111-116
    • Cathcart, R.1    Schwiers, E.2    Ames, B.N.3
  • 6
    • 0016682696 scopus 로고
    • Isolation and subfractionation on ficoll gradients of adult rat hepatocytes. Size, morphology, and biochemical characteristics of cell fractions
    • Drochmans P, Wanson JC, and Mosselmans R. Isolation and subfractionation on ficoll gradients of adult rat hepatocytes. Size, morphology, and biochemical characteristics of cell fractions. J Cell Biol 66: 1-22, 1975.
    • (1975) J Cell Biol , vol.66 , pp. 1-22
    • Drochmans, P.1    Wanson, J.C.2    Mosselmans, R.3
  • 7
    • 0033981577 scopus 로고    scopus 로고
    • Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane
    • 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.
    • (2000) Mol Cell Biol , vol.20 , pp. 929-935
    • Eskes, R.1    Desagher, S.2    Antonsson, B.3    Martinou, J.C.4
  • 8
    • 0033593230 scopus 로고    scopus 로고
    • Bax-induced caspase activation and apoptosis via cytochrome c release from mitochondria is inhibitable by Bcl-xL
    • Finucane DM, Bossy-Wetzel E, Waterhouse NJ, Cotter TG, and Green DR. Bax-induced caspase activation and apoptosis via cytochrome c release from mitochondria is inhibitable by Bcl-xL. J Biol Chem 274: 2225-2233, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 2225-2233
    • Finucane, D.M.1    Bossy-Wetzel, E.2    Waterhouse, N.J.3    Cotter, T.G.4    Green, D.R.5
  • 9
    • 0027363543 scopus 로고
    • Apoptotic bodies in a murine model of alcoholic liver disease: Reversibility of ethanol-induced changes
    • Goldin RD, Hunt NC, Clark J, and Wickramasinghe SN. Apoptotic bodies in a murine model of alcoholic liver disease: reversibility of ethanol-induced changes. J Pathol 171: 73-76, 1993.
    • (1993) J Pathol , vol.171 , pp. 73-76
    • Goldin, R.D.1    Hunt, N.C.2    Clark, J.3    Wickramasinghe, S.N.4
  • 10
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green DR and Reed JC. Mitochondria and apoptosis. Science 281: 1309-1312, 1998.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 11
    • 0025016925 scopus 로고
    • Redox interactions between catalase and alcohol dehydrogenase pathways of ethanol metabolism in the perfused rat liver
    • Handler JA and Thurman RG. Redox interactions between catalase and alcohol dehydrogenase pathways of ethanol metabolism in the perfused rat liver. J Biol Chem 265: 1510-1515, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 1510-1515
    • Handler, J.A.1    Thurman, R.G.2
  • 12
    • 0034925049 scopus 로고    scopus 로고
    • The mitochondrial permeability transition contributes to acute ethanol-induced apoptosis in rat hepatocytes
    • Higuchi H, Adachi M, Miura S, Gores GJ, and Ishii H. The mitochondrial permeability transition contributes to acute ethanol-induced apoptosis in rat hepatocytes. Hepatology 34: 320-328, 2001.
    • (2001) Hepatology , vol.34 , pp. 320-328
    • Higuchi, H.1    Adachi, M.2    Miura, S.3    Gores, G.J.4    Ishii, H.5
  • 13
    • 0030963602 scopus 로고    scopus 로고
    • Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis
    • Hsu YT, Wolter KG, and Youle RJ. Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis. Proc Natl Acad Sci USA 94: 3668-3672, 1997.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3668-3672
    • Hsu, Y.T.1    Wolter, K.G.2    Youle, R.J.3
  • 14
    • 0038421272 scopus 로고    scopus 로고
    • Imaging the permeability pore transition in single mitochondria
    • Huser J, Rechenmacher CE, and Blatter LA. Imaging the permeability pore transition in single mitochondria. Biophys J 74: 2129-2137, 1998.
    • (1998) Biophys J , vol.74 , pp. 2129-2137
    • Huser, J.1    Rechenmacher, C.E.2    Blatter, L.A.3
  • 15
    • 0030735567 scopus 로고    scopus 로고
    • Pathogenesis of alcoholic liver disease with particular emphasis on oxidative stress
    • Ishii H, Kurose I, and Kato S. Pathogenesis of alcoholic liver disease with particular emphasis on oxidative stress. J Gastroenterol Hepatol 12: S272-S282, 1997.
    • (1997) J Gastroenterol Hepatol , vol.12
    • Ishii, H.1    Kurose, I.2    Kato, S.3
  • 18
    • 0029849790 scopus 로고    scopus 로고
    • Oxidative stress and liver disease
    • Kaplowitz N and Tsukamoto H. Oxidative stress and liver disease. Prog Liver Dis 14: 131-159, 1996.
    • (1996) Prog Liver Dis , vol.14 , pp. 131-159
    • Kaplowitz, N.1    Tsukamoto, H.2
  • 19
    • 0028672497 scopus 로고
    • Is apoptosis involved in alcoholic hepatitis?
    • Kawahara H, Matsuda Y, and Takase S. Is apoptosis involved in alcoholic hepatitis? Alcohol Alcohol 29, Suppl 1: 113-118, 1994.
    • (1994) Alcohol Alcohol , vol.29 , Issue.SUPPL. 1 , pp. 113-118
    • Kawahara, H.1    Matsuda, Y.2    Takase, S.3
  • 20
    • 0034523818 scopus 로고    scopus 로고
    • Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c
    • Korsmeyer SJ, Wei MC, Saito M, Weiler S, Oh KJ, and Schlesinger PH. 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.
    • (2000) Cell Death Differ , vol.7 , pp. 1166-1173
    • Korsmeyer, S.J.1    Wei, M.C.2    Saito, M.3    Weiler, S.4    Oh, K.J.5    Schlesinger, P.H.6
  • 23
    • 0027231210 scopus 로고
    • Nitric oxide mediates Kupffer cell-induced reduction of mitochondrial energization in hepatoma cells: A comparison with oxidative burst
    • Kurose I, Miura S, Fukumura D, Yonei Y, Saito H, Tada S, Suematsu M, and Tsuchiya M. Nitric oxide mediates Kupffer cell-induced reduction of mitochondrial energization in hepatoma cells: a comparison with oxidative burst. Cancer Res 53: 2676-2682, 1993.
    • (1993) Cancer Res , vol.53 , pp. 2676-2682
    • Kurose, I.1    Miura, S.2    Fukumura, D.3    Yonei, Y.4    Saito, H.5    Tada, S.6    Suematsu, M.7    Tsuchiya, M.8
  • 26
    • 0028038965 scopus 로고
    • Lipid hydroperoxide induced mitochondrial dysfunction following acute ethanol intoxication in rats. The critical role for mitochondrial reduced glutathione
    • Masini A, Ceccarelli D, Gallesi D, Giovannini F, and Trenti T. Lipid hydroperoxide induced mitochondrial dysfunction following acute ethanol intoxication in rats. The critical role for mitochondrial reduced glutathione. Biochem Pharmacol 47: 217-224, 1994.
    • (1994) Biochem Pharmacol , vol.47 , pp. 217-224
    • Masini, A.1    Ceccarelli, D.2    Gallesi, D.3    Giovannini, F.4    Trenti, T.5
  • 27
    • 0033613275 scopus 로고    scopus 로고
    • Bax membrane insertion during Fas(CD95)-induced apoptosis precedes cytochrome c release and is inhibited by Bcl-2
    • Murphy KM, Streips UN, and Lock RB. Bax membrane insertion during Fas(CD95)-induced apoptosis precedes cytochrome c release and is inhibited by Bcl-2. Oncogene 18: 5991-5999, 1999.
    • (1999) Oncogene , vol.18 , pp. 5991-5999
    • Murphy, K.M.1    Streips, U.N.2    Lock, R.B.3
  • 28
    • 0031902029 scopus 로고    scopus 로고
    • Apoptosis and alcoholic liver disease
    • Nanji AA. Apoptosis and alcoholic liver disease. Semin Liver Dis 18: 187-190, 1998.
    • (1998) Semin Liver Dis , vol.18 , pp. 187-190
    • Nanji, A.A.1
  • 29
    • 0032422488 scopus 로고    scopus 로고
    • Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria
    • Narita M, Shimizu S, Ito T, Chittenden T, Lutz RJ, Matsuda H, and Tsujimoto Y. Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria. Proc Natl Acad Sci USA 95: 14681-14686, 1998.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 14681-14686
    • Narita, M.1    Shimizu, S.2    Ito, T.3    Chittenden, T.4    Lutz, R.J.5    Matsuda, H.6    Tsujimoto, Y.7
  • 31
    • 0032502866 scopus 로고    scopus 로고
    • Disruption of the outer mitochondrial membrane as a result of large amplitude swelling: The impact of irreversible permeability transition
    • Petit PX, Goubern M, Diolez P, Susin SA, Zamzami N, and Kroemer G. Disruption of the outer mitochondrial membrane as a result of large amplitude swelling: the impact of irreversible permeability transition. FEBS Lett 426: 111-116, 1998.
    • (1998) FEBS Lett , vol.426 , pp. 111-116
    • Petit, P.X.1    Goubern, M.2    Diolez, P.3    Susin, S.A.4    Zamzami, N.5    Kroemer, G.6
  • 32
    • 0033021780 scopus 로고    scopus 로고
    • Transient and long-lasting openings of the mitochondrial permeability transition pore can be monitored directly in intact cells by changes in mitochondrial calcein fluorescence
    • Petronilli V, Miotto G, Canton M, Brini M, Colonna R, Bernardi P, and Di Lisa F. Transient and long-lasting openings of the mitochondrial permeability transition pore can be monitored directly in intact cells by changes in mitochondrial calcein fluorescence. Biophys J 76: 725-734, 1999.
    • (1999) Biophys J , vol.76 , pp. 725-734
    • Petronilli, V.1    Miotto, G.2    Canton, M.3    Brini, M.4    Colonna, R.5    Bernardi, P.6    Di Lisa, F.7
  • 33
    • 0034253592 scopus 로고    scopus 로고
    • BAX-dependent transport of cytochrome c reconstituted in pure liposomes
    • Saito M, Korsmeyer SJ, and Schlesinger PH. BAX-dependent transport of cytochrome c reconstituted in pure liposomes. Nat Cell Biol 2: 553-555, 2000.
    • (2000) Nat Cell Biol , vol.2 , pp. 553-555
    • Saito, M.1    Korsmeyer, S.J.2    Schlesinger, P.H.3
  • 34
    • 0036205587 scopus 로고    scopus 로고
    • Mechanisms of caspase activation and inhibition during apoptosis
    • Shi Y. Mechanisms of caspase activation and inhibition during apoptosis. Mol Cell 9: 459-470, 2002.
    • (2002) Mol Cell , vol.9 , pp. 459-470
    • Shi, Y.1
  • 35
    • 0034697365 scopus 로고    scopus 로고
    • Electrophysiological study of a novel large pore formed by Bax and the voltage-dependent anion channel that is permeable to cytochrome c
    • Shimizu S, Ide T, Yanagida T, and Tsujimoto Y. Electrophysiological study of a novel large pore formed by Bax and the voltage-dependent anion channel that is permeable to cytochrome c. J Biol Chem 275: 12321-12325, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 12321-12325
    • Shimizu, S.1    Ide, T.2    Yanagida, T.3    Tsujimoto, Y.4
  • 36
    • 0035931765 scopus 로고    scopus 로고
    • Essential role of voltage-dependent anion channel in various forms of apoptosis in mammalian cells
    • Shimizu S, Matsuoka Y, Shinohara Y, Yoneda Y, and Tsujimoto Y. Essential role of voltage-dependent anion channel in various forms of apoptosis in mammalian cells. J Cell Biol 152: 237-250, 2001.
    • (2001) J Cell Biol , vol.152 , pp. 237-250
    • Shimizu, S.1    Matsuoka, Y.2    Shinohara, Y.3    Yoneda, Y.4    Tsujimoto, Y.5
  • 37
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • 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.
    • (1999) Nature , vol.399 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 38
    • 0032504575 scopus 로고    scopus 로고
    • Mitochondria as regulators of apoptosis: Doubt no more
    • Susin SA, Zamzami N, and Kroemer G. Mitochondria as regulators of apoptosis: doubt no more. Biochim Biophys Acta 1366: 151-165, 1998.
    • (1998) Biochim Biophys Acta , vol.1366 , pp. 151-165
    • Susin, S.A.1    Zamzami, N.2    Kroemer, G.3
  • 39
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry NA and Lazebnik Y Caspases: enemies within. Science 281: 1312-1316, 1998.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 41
    • 0035129976 scopus 로고    scopus 로고
    • Bile acid-induced rat hepatocyte apoptosis is inhibited by antioxidants and blockers of the mitochondrial permeability transition
    • Yerushalmi B, Dahl R, Devereaux MW, Gumpricht E, and Sokol RJ. Bile acid-induced rat hepatocyte apoptosis is inhibited by antioxidants and blockers of the mitochondrial permeability transition. Hepatology 33: 616-626, 2001.
    • (2001) Hepatology , vol.33 , pp. 616-626
    • Yerushalmi, B.1    Dahl, R.2    Devereaux, M.W.3    Gumpricht, E.4    Sokol, R.J.5
  • 42
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • Zoratti M and Szabo I. The mitochondrial permeability transition. Biochim Biophys Acta 1241: 139-176, 1995.
    • (1995) Biochim Biophys Acta , vol.1241 , pp. 139-176
    • Zoratti, M.1    Szabo, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.