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Volumn 50, Issue 9, 2009, Pages 1721-1734

Bile acids: Regulation of apoptosis by ursodeoxycholic acid

Author keywords

Bcl 2 family; Cell death; Liver; Neuroprotection; Nuclear steroid receptors

Indexed keywords

BILE ACID; CASPASE 8; DEATH RECEPTOR; GLUCOCORTICOID RECEPTOR; MINERALOCORTICOID RECEPTOR; TAUROCHENODEOXYCHOLIC ACID; URSODEOXYCHOLIC ACID;

EID: 70350417325     PISSN: 00222275     EISSN: 15397262     Source Type: Journal    
DOI: 10.1194/jlr.R900011-JLR200     Document Type: Review
Times cited : (288)

References (145)
  • 2
    • 0029012444 scopus 로고
    • Apoptosis and hepatobiliary disease
    • Patel, T., and G. J. Gores. 1995. Apoptosis and hepatobiliary disease. Hepatology. 21: 1725-1741.
    • (1995) Hepatology , vol.21 , pp. 1725-1741
    • Patel, T.1    Gores, G.J.2
  • 3
    • 0021739393 scopus 로고
    • Physicochemical properties of bile acids and their relationship to biological properties: An overview of the problem
    • Hofmann, A. F., and A. Roda. 1984. Physicochemical properties of bile acids and their relationship to biological properties: an overview of the problem. J. Lipid Res. 25: 1477-1489.
    • (1984) J. Lipid Res , vol.25 , pp. 1477-1489
    • Hofmann, A.F.1    Roda, A.2
  • 4
    • 33748461404 scopus 로고    scopus 로고
    • Supramolecular chemistry of bile acids derivatives: Formation of gels
    • Babu, P., N. Sangeetha, and U. Maitra. 2006. Supramolecular chemistry of bile acids derivatives: formation of gels. Macromol. Symp. 241: 60-67.
    • (2006) Macromol. Symp , vol.241 , pp. 60-67
    • Babu, P.1    Sangeetha, N.2    Maitra, U.3
  • 5
    • 0026778193 scopus 로고
    • Bile acid biosynthesis
    • Russell, D. W., and K. D. Setchell. 1992. Bile acid biosynthesis. Biochemistry. 31: 4737-4749.
    • (1992) Biochemistry , vol.31 , pp. 4737-4749
    • Russell, D.W.1    Setchell, K.D.2
  • 6
    • 33749453633 scopus 로고    scopus 로고
    • The neuroprotective characteristic of ursodeoxycholic acid and its conjugates
    • G. van Berge Henegouwen, D. Keppler, U. Leuschner, G. Paumgartner, and A. Stiehl, editors. Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Rodrigues, C. M., and C. J. Steer. 2000. The neuroprotective characteristic of ursodeoxycholic acid and its conjugates. In Biology of Bile Acids in Health and Disease. G. van Berge Henegouwen, D. Keppler, U. Leuschner, G. Paumgartner, and A. Stiehl, editors. Kluwer Academic Publishers, Dordrecht, The Netherlands. 255-270.
    • (2000) Biology of Bile Acids in Health and Disease , pp. 255-270
    • Rodrigues, C.M.1    Steer, C.J.2
  • 7
    • 1242269851 scopus 로고    scopus 로고
    • Regulation of bile acid synthesis: Pathways, nuclear receptors, and mechanisms
    • Chiang, J. Y. 2004. Regulation of bile acid synthesis: pathways, nuclear receptors, and mechanisms. J. Hepatol. 40: 539-551.
    • (2004) J. Hepatol , vol.40 , pp. 539-551
    • Chiang, J.Y.1
  • 8
    • 33846886738 scopus 로고    scopus 로고
    • PXR induces CYP27A1 and regulates cholesterol metabolism in the intestine
    • Li, T., W. Chen, and J. Y. Chiang. 2007. PXR induces CYP27A1 and regulates cholesterol metabolism in the intestine. J. Lipid Res. 48: 373-384.
    • (2007) J. Lipid Res , vol.48 , pp. 373-384
    • Li, T.1    Chen, W.2    Chiang, J.Y.3
  • 9
    • 61449258999 scopus 로고    scopus 로고
    • Mechanism of vitamin D receptor inhibition of cholesterol 7α-hydroxylase gene transcription in human hepatocytes
    • Han, S., and J. Y. Chiang. 2009. Mechanism of vitamin D receptor inhibition of cholesterol 7α-hydroxylase gene transcription in human hepatocytes. Drug Metab. Dispos. 37: 469-478.
    • (2009) Drug Metab. Dispos , vol.37 , pp. 469-478
    • Han, S.1    Chiang, J.Y.2
  • 10
    • 1542275425 scopus 로고    scopus 로고
    • The farnesoid X receptor controls gene expression in a ligand- and promoter-selective fashion
    • Lew, J. L., A. Zhao, J. Yu, L. Huang, N. De Pedro, F. Pelaez, S. D. Wright, and J. Cui. 2004. The farnesoid X receptor controls gene expression in a ligand- and promoter-selective fashion. J. Biol. Chem. 279: 8856-8861.
    • (2004) J. Biol. Chem , vol.279 , pp. 8856-8861
    • Lew, J.L.1    Zhao, A.2    Yu, J.3    Huang, L.4    De Pedro, N.5    Pelaez, F.6    Wright, S.D.7    Cui, J.8
  • 11
    • 0037790917 scopus 로고    scopus 로고
    • The enzymes, regulation, and genetics of bile acid synthesis
    • Russell, D. W. 2003. The enzymes, regulation, and genetics of bile acid synthesis. Annu. Rev. Biochem. 72: 137-174.
    • (2003) Annu. Rev. Biochem , vol.72 , pp. 137-174
    • Russell, D.W.1
  • 16
    • 0036086509 scopus 로고    scopus 로고
    • Loss of nuclear receptor SHP impairs but does not eliminate negative feedback regulation of bile acid synthesis
    • Kerr, T. A., S. Saeki, M. Schneider, K. Schaefer, S. Berdy, T. Redder, B. Shan, D. W. Russell, and M. Schwarz. 2002. Loss of nuclear receptor SHP impairs but does not eliminate negative feedback regulation of bile acid synthesis. Dev. Cell. 2: 713-720.
    • (2002) Dev. Cell , vol.2 , pp. 713-720
    • Kerr, T.A.1    Saeki, S.2    Schneider, M.3    Schaefer, K.4    Berdy, S.5    Redder, T.6    Shan, B.7    Russell, D.W.8    Schwarz, M.9
  • 20
    • 37249015421 scopus 로고    scopus 로고
    • Differential regulation of bile acid homeostasis by the farnesoid X receptor in liver and intestine
    • Kim, I., S. H. Ahn, T. Inagaki, M. Choi, S. Ito, G. L. Guo, S. A. Kliewer, and F. J. Gonzalez. 2007. Differential regulation of bile acid homeostasis by the farnesoid X receptor in liver and intestine. J. Lipid Res. 48: 2664-2672.
    • (2007) J. Lipid Res , vol.48 , pp. 2664-2672
    • Kim, I.1    Ahn, S.H.2    Inagaki, T.3    Choi, M.4    Ito, S.5    Guo, G.L.6    Kliewer, S.A.7    Gonzalez, F.J.8
  • 21
    • 41649089141 scopus 로고    scopus 로고
    • The organic solute transporter α-β, Ostα-Ostβ, is essential for intestinal bile acid transport and homeostasis
    • Rao, A., J. Haywood, A. L. Craddock, M. G. Belinsky, G. D. Kruh, and P. A. Dawson. 2008. The organic solute transporter α-β, Ostα-Ostβ, is essential for intestinal bile acid transport and homeostasis. Proc. Natl. Acad. Sci. USA. 105: 3891-3896.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 3891-3896
    • Rao, A.1    Haywood, J.2    Craddock, A.L.3    Belinsky, M.G.4    Kruh, G.D.5    Dawson, P.A.6
  • 25
    • 33847011377 scopus 로고    scopus 로고
    • Principles of hepatic organic anion transporter regulation during cholestasis, inflammation and liver regeneration
    • Geier, A., M. Wagner, C. G. Dietrich, and M. Trauner. 2007. Principles of hepatic organic anion transporter regulation during cholestasis, inflammation and liver regeneration. Biochim. Biophys. Acta. 1773: 283-308.
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 283-308
    • Geier, A.1    Wagner, M.2    Dietrich, C.G.3    Trauner, M.4
  • 26
    • 33645509321 scopus 로고    scopus 로고
    • Farnesoid X receptor is essential for normal glucose homeostasis
    • Ma, K., P. K. Saha, L. Chan, and D. D. Moore. 2006. Farnesoid X receptor is essential for normal glucose homeostasis. J. Clin. Invest. 116: 1102-1109.
    • (2006) J. Clin. Invest , vol.116 , pp. 1102-1109
    • Ma, K.1    Saha, P.K.2    Chan, L.3    Moore, D.D.4
  • 27
    • 0034520470 scopus 로고    scopus 로고
    • Dissecting the pathways to death
    • Daniel, P. T. 2000. Dissecting the pathways to death. Leukemia. 14: 2035-2044.
    • (2000) Leukemia , vol.14 , pp. 2035-2044
    • Daniel, P.T.1
  • 28
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr, J. F., A. H. Wyllie, and A. R. Currie. 1972. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer. 26: 239-257.
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 29
    • 0036463649 scopus 로고    scopus 로고
    • Apoptosis-based therapies
    • Reed, J. C. 2002. Apoptosis-based therapies. Nat. Rev. Drug Discov. 1: 111-121.
    • (2002) Nat. Rev. Drug Discov , vol.1 , pp. 111-121
    • Reed, J.C.1
  • 30
    • 0036205587 scopus 로고    scopus 로고
    • Mechanisms of caspase activation and inhibition during apoptosis
    • Shi, Y. 2002. Mechanisms of caspase activation and inhibition during apoptosis. Mol. Cell. 9: 459-470.
    • (2002) Mol. Cell , vol.9 , pp. 459-470
    • Shi, Y.1
  • 31
    • 0036598992 scopus 로고    scopus 로고
    • Targeting death and decoy receptors of the tumour-necrosis factor superfamily
    • Ashkenazi, A. 2002. Targeting death and decoy receptors of the tumour-necrosis factor superfamily. Nat. Rev. Cancer. 2: 420-430.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 420-430
    • Ashkenazi, A.1
  • 32
    • 33845977959 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in cell death
    • Kroemer, G., L. Galluzzi, and C. Brenner. 2007. Mitochondrial membrane permeabilization in cell death. Physiol. Rev. 87: 99-163.
    • (2007) Physiol. Rev , vol.87 , pp. 99-163
    • Kroemer, G.1    Galluzzi, L.2    Brenner, C.3
  • 33
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: Opposing activities that mediate cell death
    • Youle, R. J., and A. Strasser. 2008. The BCL-2 protein family: opposing activities that mediate cell death. Nat. Rev. Mol. Cell Biol. 9: 47-59.
    • (2008) Nat. Rev. Mol. Cell Biol , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 34
    • 0033491193 scopus 로고    scopus 로고
    • CD95(APO-1/Fas)-mediated apoptosis: Live and let die
    • Krammer, P. H. 1999. CD95(APO-1/Fas)-mediated apoptosis: live and let die. Adv. Immunol. 71: 163-210.
    • (1999) Adv. Immunol , vol.71 , pp. 163-210
    • Krammer, P.H.1
  • 35
    • 0035936797 scopus 로고    scopus 로고
    • The TNF and TNF receptor superfamilies: Integrating mammalian biology
    • Locksley, R. M., N. Killeen, and M. J. Lenardo. 2001. The TNF and TNF receptor superfamilies: integrating mammalian biology. Cell. 104: 487-501.
    • (2001) Cell , vol.104 , pp. 487-501
    • Locksley, R.M.1    Killeen, N.2    Lenardo, M.J.3
  • 36
    • 1442301672 scopus 로고    scopus 로고
    • The dependence receptor hypothesis
    • Mehlen, P., and D. E. Bredesen. 2004. The dependence receptor hypothesis. Apoptosis. 9: 37-49.
    • (2004) Apoptosis , vol.9 , pp. 37-49
    • Mehlen, P.1    Bredesen, D.E.2
  • 37
    • 0037276437 scopus 로고    scopus 로고
    • The CD95(APO-1/Fas) DISC and beyond
    • Peter, M. E., and P. H. Krammer. 2003. The CD95(APO-1/Fas) DISC and beyond. Cell Death Differ. 10: 26-35.
    • (2003) Cell Death Differ , vol.10 , pp. 26-35
    • Peter, M.E.1    Krammer, P.H.2
  • 38
    • 0037178881 scopus 로고    scopus 로고
    • Relief of extrinsic pathway inhibition by the Bid-dependent mitochondrial release of Smac in Fas-mediated hepatocyte apoptosis
    • Li, S., Y. Zhao, X. He, T. H. Kim, D. K. Kuharsky, H. Rabinowich, J. Chen, C. Du, and X. M. Yin. 2002. Relief of extrinsic pathway inhibition by the Bid-dependent mitochondrial release of Smac in Fas-mediated hepatocyte apoptosis. J. Biol. Chem. 277: 26912-26920.
    • (2002) J. Biol. Chem , vol.277 , pp. 26912-26920
    • Li, S.1    Zhao, Y.2    He, X.3    Kim, T.H.4    Kuharsky, D.K.5    Rabinowich, H.6    Chen, J.7    Du, C.8    Yin, X.M.9
  • 39
    • 0033981577 scopus 로고    scopus 로고
    • Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane
    • Eskes, R., S. Desagher, B. Antonsson, and J. C. Martinou. 2000. Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane. Mol. Cell. Biol. 20: 929-935.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 929-935
    • Eskes, R.1    Desagher, S.2    Antonsson, B.3    Martinou, J.C.4
  • 40
    • 0030612164 scopus 로고    scopus 로고
    • Control of the G1/S transition
    • Reed, S. I. 1997. Control of the G1/S transition. Cancer Surv. 29: 7-23.
    • (1997) Cancer Surv , vol.29 , pp. 7-23
    • Reed, S.I.1
  • 41
    • 2942642501 scopus 로고    scopus 로고
    • Signal transduction mediated by cyclin D1: From mitogens to cell proliferation: a molecular target with therapeutic potential
    • Wang, C., Z. Li, M. Fu, T. Bouras, and R. G. Pestell. 2004. Signal transduction mediated by cyclin D1: from mitogens to cell proliferation: a molecular target with therapeutic potential. Cancer Treat. Res. 119: 217-237.
    • (2004) Cancer Treat. Res , vol.119 , pp. 217-237
    • Wang, C.1    Li, Z.2    Fu, M.3    Bouras, T.4    Pestell, R.G.5
  • 42
    • 0032806092 scopus 로고    scopus 로고
    • Roles of cyclin D1 and related genes in growth inhibition, senescence and apoptosis
    • Han, E. K., S. C. Ng, N. Arber, M. Begemann, and I. B. Weinstein. 1999. Roles of cyclin D1 and related genes in growth inhibition, senescence and apoptosis. Apoptosis. 4: 213-219.
    • (1999) Apoptosis , vol.4 , pp. 213-219
    • Han, E.K.1    Ng, S.C.2    Arber, N.3    Begemann, M.4    Weinstein, I.B.5
  • 43
    • 0028324310 scopus 로고
    • Analysis of cell cycle-related gene expression in postmitotic neurons: Selective induction of cyclin D1 during programmed cell death
    • Freeman, R. S., S. Estus, and E. M. Johnson, Jr. 1994. Analysis of cell cycle-related gene expression in postmitotic neurons: selective induction of cyclin D1 during programmed cell death. Neuron. 12: 343-355.
    • (1994) Neuron , vol.12 , pp. 343-355
    • Freeman, R.S.1    Estus, S.2    Johnson Jr., E.M.3
  • 44
    • 0031815596 scopus 로고    scopus 로고
    • Toward an understanding of the functional complexity of the E2F and retinoblastoma families
    • Nevins, J. R. 1998. Toward an understanding of the functional complexity of the E2F and retinoblastoma families. Cell Growth Differ. 9: 585-593.
    • (1998) Cell Growth Differ , vol.9 , pp. 585-593
    • Nevins, J.R.1
  • 45
    • 0030444208 scopus 로고    scopus 로고
    • Apoptosis induced by ectopic expression of cyclin D1 but not cyclin E
    • Sofer-Levi, Y., and D. Resnitzky. 1996. Apoptosis induced by ectopic expression of cyclin D1 but not cyclin E. Oncogene. 13: 2431-2437.
    • (1996) Oncogene , vol.13 , pp. 2431-2437
    • Sofer-Levi, Y.1    Resnitzky, D.2
  • 46
    • 0037329056 scopus 로고    scopus 로고
    • The p53-Mdm2 module and the ubiquitin system
    • Michael, D., and M. Oren. 2003. The p53-Mdm2 module and the ubiquitin system. Semin. Cancer Biol. 13: 49-58.
    • (2003) Semin. Cancer Biol , vol.13 , pp. 49-58
    • Michael, D.1    Oren, M.2
  • 47
    • 0034127434 scopus 로고    scopus 로고
    • Apoptosis and cell cycle: Distinct checkpoints with overlapping upstream control
    • Jacotot, E., K. F. Ferri, and G. Kroemer. 2000. Apoptosis and cell cycle: distinct checkpoints with overlapping upstream control. Pathol. Biol. 48: 271-279.
    • (2000) Pathol. Biol , vol.48 , pp. 271-279
    • Jacotot, E.1    Ferri, K.F.2    Kroemer, G.3
  • 49
    • 1842479900 scopus 로고    scopus 로고
    • What doesn't kill you makes you stronger: How hepatocytes survive prolonged cholestasis
    • Maher, J. J. 2004. What doesn't kill you makes you stronger: how hepatocytes survive prolonged cholestasis. Hepatology. 39: 1141-1143.
    • (2004) Hepatology , vol.39 , pp. 1141-1143
    • Maher, J.J.1
  • 51
    • 0031950282 scopus 로고    scopus 로고
    • Ursodeoxycholic acid may inhibit deoxycholic acid-induced apoptosis by modulating mitochondrial transmembrane potential and reactive oxygen species production
    • Rodrigues, C. M., G. Fan, P. Y. Wong, B. T. Kren, and C. J. Steer. 1998. Ursodeoxycholic acid may inhibit deoxycholic acid-induced apoptosis by modulating mitochondrial transmembrane potential and reactive oxygen species production. Mol. Med. 4: 165-178.
    • (1998) Mol. Med , vol.4 , pp. 165-178
    • Rodrigues, C.M.1    Fan, G.2    Wong, P.Y.3    Kren, B.T.4    Steer, C.J.5
  • 52
    • 0035129976 scopus 로고    scopus 로고
    • Bile acid-induced rat hepatocyte apoptosis is inhibited by antioxidants and blockers of the mitochondrial permeability transition
    • Yerushalmi, B., R. Dahl, M. W. Devereaux, E. Gumpricht, and R. J. Sokol. 2001. Bile acid-induced rat hepatocyte apoptosis is inhibited by antioxidants and blockers of the mitochondrial permeability transition. Hepatology. 33: 616-626.
    • (2001) Hepatology , vol.33 , pp. 616-626
    • Yerushalmi, B.1    Dahl, R.2    Devereaux, M.W.3    Gumpricht, E.4    Sokol, R.J.5
  • 55
    • 59149096566 scopus 로고    scopus 로고
    • Characterization of enantiomeric bile acid-induced apoptosis in colon cancer cell lines
    • Katona, B. W., S. Anant, D. F. Covey, and W. F. Stenson. 2009. Characterization of enantiomeric bile acid-induced apoptosis in colon cancer cell lines. J. Biol. Chem. 284: 3354-3364.
    • (2009) J. Biol. Chem , vol.284 , pp. 3354-3364
    • Katona, B.W.1    Anant, S.2    Covey, D.F.3    Stenson, W.F.4
  • 56
    • 0035167269 scopus 로고    scopus 로고
    • Deoxycholic acid (DCA) causes ligand-independent activation of epidermal growth factor receptor (EGFR) and FAS receptor in primary hepatocytes: Inhibition of EGFR/mitogen-activated protein kinase-signaling module enhances DCA-induced apoptosis
    • Qiao, L., E. Studer, K. Leach, R. McKinstry, S. Gupta, R. Decker, R. Kukreja, K. Valerie, P. Nagarkatti, W. El Deiry, et al. 2001. Deoxycholic acid (DCA) causes ligand-independent activation of epidermal growth factor receptor (EGFR) and FAS receptor in primary hepatocytes: inhibition of EGFR/mitogen-activated protein kinase-signaling module enhances DCA-induced apoptosis. Mol. Biol. Cell. 12: 2629-2645.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2629-2645
    • Qiao, L.1    Studer, E.2    Leach, K.3    McKinstry, R.4    Gupta, S.5    Decker, R.6    Kukreja, R.7    Valerie, K.8    Nagarkatti, P.9    El Deiry, W.10
  • 58
    • 22844440003 scopus 로고    scopus 로고
    • Involvement of NADPH oxidase isoforms and Src family kinases in CD95-dependent hepatocyte apoptosis
    • Reinehr, R., S. Becker, A. Eberle, S. Grether-Beck, and D. Haussinger. 2005. Involvement of NADPH oxidase isoforms and Src family kinases in CD95-dependent hepatocyte apoptosis. J. Biol. Chem. 280: 27179-27194.
    • (2005) J. Biol. Chem , vol.280 , pp. 27179-27194
    • Reinehr, R.1    Becker, S.2    Eberle, A.3    Grether-Beck, S.4    Haussinger, D.5
  • 61
    • 0032500793 scopus 로고    scopus 로고
    • Cell surface trafficking of Fas: A rapid mechanism of p53-mediated apoptosis
    • Bennett, M., K. Macdonald, S. W. Chan, J. P. Luzio, R. Simari, and P. Weissberg. 1998. Cell surface trafficking of Fas: a rapid mechanism of p53-mediated apoptosis. Science. 282: 290-293.
    • (1998) Science , vol.282 , pp. 290-293
    • Bennett, M.1    Macdonald, K.2    Chan, S.W.3    Luzio, J.P.4    Simari, R.5    Weissberg, P.6
  • 62
    • 53549104898 scopus 로고    scopus 로고
    • Multiple cyclin kinase inhibitors promote bile acid-induced apoptosis and autophagy in primary hepatocytes via p53-CD95-dependent signaling
    • Zhang, G., M. A. Park, C. Mitchell, T. Walker, H. Hamed, E. Studer, M. Graf, M. Rahmani, S. Gupta, P. B. Hylemon, et al. 2008. Multiple cyclin kinase inhibitors promote bile acid-induced apoptosis and autophagy in primary hepatocytes via p53-CD95-dependent signaling. J. Biol. Chem. 283: 24343-24358.
    • (2008) J. Biol. Chem , vol.283 , pp. 24343-24358
    • Zhang, G.1    Park, M.A.2    Mitchell, C.3    Walker, T.4    Hamed, H.5    Studer, E.6    Graf, M.7    Rahmani, M.8    Gupta, S.9    Hylemon, P.B.10
  • 63
  • 64
    • 33747871436 scopus 로고    scopus 로고
    • Involvement of endoplasmic reticulum in glycochenodeoxycholic acid-induced apoptosis in rat hepatocytes
    • Tsuchiya, S., M. Tsuji, Y. Morio, and K. Oguchi. 2006. Involvement of endoplasmic reticulum in glycochenodeoxycholic acid-induced apoptosis in rat hepatocytes. Toxicol. Lett. 166: 140-149.
    • (2006) Toxicol. Lett , vol.166 , pp. 140-149
    • Tsuchiya, S.1    Tsuji, M.2    Morio, Y.3    Oguchi, K.4
  • 65
    • 35349014047 scopus 로고    scopus 로고
    • Interaction between caspase-8 activation and endoplasmic reticulum stress in glycochenodeoxycholic acid-induced apoptotic HepG2 cells
    • Iizaka, T., M. Tsuji, H. Oyamada, Y. Morio, and K. Oguchi. 2007. Interaction between caspase-8 activation and endoplasmic reticulum stress in glycochenodeoxycholic acid-induced apoptotic HepG2 cells. Toxicology. 241: 146-156.
    • (2007) Toxicology , vol.241 , pp. 146-156
    • Iizaka, T.1    Tsuji, M.2    Oyamada, H.3    Morio, Y.4    Oguchi, K.5
  • 68
    • 0036073356 scopus 로고    scopus 로고
    • Salvia miltiorrhiza inhibits biliary obstruction-induced hepatocyte apoptosis by cytoplasmic sequestration of p53
    • Oh, S. H., J. X. Nan, D. W. Sohn, Y. C. Kim, and B. H. Lee. 2002. Salvia miltiorrhiza inhibits biliary obstruction-induced hepatocyte apoptosis by cytoplasmic sequestration of p53. Toxicol. Appl. Pharmacol. 182: 27-33.
    • (2002) Toxicol. Appl. Pharmacol , vol.182 , pp. 27-33
    • Oh, S.H.1    Nan, J.X.2    Sohn, D.W.3    Kim, Y.C.4    Lee, B.H.5
  • 69
    • 0036151709 scopus 로고    scopus 로고
    • Activation of the Raf-1/MEK/ERK cascade by bile acids occurs via the epidermal growth factor receptor in primary rat hepatocytes
    • Rao, Y. P., E. J. Studer, R. T. Stravitz, S. Gupta, L. Qiao, P. Dent, and P. B. Hylemon. 2002. Activation of the Raf-1/MEK/ERK cascade by bile acids occurs via the epidermal growth factor receptor in primary rat hepatocytes. Hepatology. 35: 307-314.
    • (2002) Hepatology , vol.35 , pp. 307-314
    • Rao, Y.P.1    Studer, E.J.2    Stravitz, R.T.3    Gupta, S.4    Qiao, L.5    Dent, P.6    Hylemon, P.B.7
  • 70
    • 0037405649 scopus 로고    scopus 로고
    • Bile acid regulation of C/EBPβ, CREB, and c-Jun function, via the extracellular signal-regulated kinase and c-Jun NH2-terminal kinase pathways, modulates the apoptotic response of hepatocytes
    • Qiao, L., S. I. Han, Y. Fang, J. S. Park, S. Gupta, D. Gilfor, G. Amorino, K. Valerie, L. Sealy, J. F. Engelhardt, et al. 2003. Bile acid regulation of C/EBPβ, CREB, and c-Jun function, via the extracellular signal-regulated kinase and c-Jun NH2-terminal kinase pathways, modulates the apoptotic response of hepatocytes. Mol. Cell. Biol. 23: 3052-3066.
    • (2003) Mol. Cell. Biol , vol.23 , pp. 3052-3066
    • Qiao, L.1    Han, S.I.2    Fang, Y.3    Park, J.S.4    Gupta, S.5    Gilfor, D.6    Amorino, G.7    Valerie, K.8    Sealy, L.9    Engelhardt, J.F.10
  • 72
    • 1242294416 scopus 로고    scopus 로고
    • Deoxycholic acid activates the c-Jun N-terminal kinase pathway via FAS receptor activation in primary hepatocytes. Role of acidic sphingomyelinase-mediated ceramide generation in FAS receptor activation
    • Gupta, S., R. Natarajan, S. G. Payne, E. J. Studer, S. Spiegel, P. Dent, and P. B. Hylemon. 2004. Deoxycholic acid activates the c-Jun N-terminal kinase pathway via FAS receptor activation in primary hepatocytes. Role of acidic sphingomyelinase-mediated ceramide generation in FAS receptor activation. J. Biol. Chem. 279: 5821-5828.
    • (2004) J. Biol. Chem , vol.279 , pp. 5821-5828
    • Gupta, S.1    Natarajan, R.2    Payne, S.G.3    Studer, E.J.4    Spiegel, S.5    Dent, P.6    Hylemon, P.B.7
  • 73
    • 0034733547 scopus 로고    scopus 로고
    • The bile acid taurochenodeoxycholate activates a phosphatidylinositol 3-kinase-dependent survival signaling cascade
    • Rust, C., L. M. Karnitz, C. V. Paya, J. Moscat, R. D. Simari, and G. J. Gores. 2000. The bile acid taurochenodeoxycholate activates a phosphatidylinositol 3-kinase-dependent survival signaling cascade. J. Biol. Chem. 275: 20210-20216.
    • (2000) J. Biol. Chem , vol.275 , pp. 20210-20216
    • Rust, C.1    Karnitz, L.M.2    Paya, C.V.3    Moscat, J.4    Simari, R.D.5    Gores, G.J.6
  • 74
    • 3042763992 scopus 로고    scopus 로고
    • Differential modulation of cellular death and survival pathways by conjugated bile acids
    • Torchia, E. C., A. Stolz, and L. B. Agellon. 2001. Differential modulation of cellular death and survival pathways by conjugated bile acids. BMC Biochem. 2: 11.
    • (2001) BMC Biochem , vol.2 , pp. 11
    • Torchia, E.C.1    Stolz, A.2    Agellon, L.B.3
  • 75
    • 0036211298 scopus 로고    scopus 로고
    • Inhibition of the MAPK and PI3K pathways enhances UDCA-induced apoptosis in primary rodent hepatocytes
    • Qiao, L., A. Yacoub, E. Studer, S. Gupta, X. Y. Pei, S. Grant, P. B. Hylemon, and P. Dent. 2002. Inhibition of the MAPK and PI3K pathways enhances UDCA-induced apoptosis in primary rodent hepatocytes. Hepatology. 35: 779-789.
    • (2002) Hepatology , vol.35 , pp. 779-789
    • Qiao, L.1    Yacoub, A.2    Studer, E.3    Gupta, S.4    Pei, X.Y.5    Grant, S.6    Hylemon, P.B.7    Dent, P.8
  • 76
    • 0942301272 scopus 로고    scopus 로고
    • Ursodeoxycholic acid (UDCA) can inhibit deoxycholic acid (DCA)-induced apoptosis via modulation of EGFR/ Raf-1/ERK signaling in human colon cancer cells
    • Im, E., and J. D. Martinez. 2004. Ursodeoxycholic acid (UDCA) can inhibit deoxycholic acid (DCA)-induced apoptosis via modulation of EGFR/ Raf-1/ERK signaling in human colon cancer cells. J. Nutr. 134: 483-486.
    • (2004) J. Nutr , vol.134 , pp. 483-486
    • Im, E.1    Martinez, J.D.2
  • 77
    • 0036204957 scopus 로고    scopus 로고
    • Ursodeoxycholic acid cytoprotection: Dancing with death receptors and survival pathways
    • Guicciardi, M. E., and G. J. Gores. 2002. Ursodeoxycholic acid cytoprotection: dancing with death receptors and survival pathways. Hepatology. 35: 971-973.
    • (2002) Hepatology , vol.35 , pp. 971-973
    • Guicciardi, M.E.1    Gores, G.J.2
  • 78
    • 0031770301 scopus 로고    scopus 로고
    • Ursodeoxycholic acid in cholestasis: Potential mechanisms of action and therapeutic applications
    • Beuers, U., J. L. Boyer, and G. Paumgartner. 1998. Ursodeoxycholic acid in cholestasis: potential mechanisms of action and therapeutic applications. Hepatology. 28: 1449-1453.
    • (1998) Hepatology , vol.28 , pp. 1449-1453
    • Beuers, U.1    Boyer, J.L.2    Paumgartner, G.3
  • 79
    • 0034945397 scopus 로고    scopus 로고
    • Ursodeoxycholic acid 'mechanisms of action and clinical use in hepatobiliary disorders'
    • Lazaridis, K. N., G. J. Gores, and K. D. Lindor. 2001. Ursodeoxycholic acid 'mechanisms of action and clinical use in hepatobiliary disorders'. J. Hepatol. 35: 134-146.
    • (2001) J. Hepatol , vol.35 , pp. 134-146
    • Lazaridis, K.N.1    Gores, G.J.2    Lindor, K.D.3
  • 80
    • 0036725044 scopus 로고    scopus 로고
    • Ursodeoxycholic acid in cholestatic liver disease: Mechanisms of action and therapeutic use revisited
    • Paumgartner, G., and U. Beuers. 2002. Ursodeoxycholic acid in cholestatic liver disease: mechanisms of action and therapeutic use revisited. Hepatology. 36: 525-531.
    • (2002) Hepatology , vol.36 , pp. 525-531
    • Paumgartner, G.1    Beuers, U.2
  • 82
    • 0032525819 scopus 로고    scopus 로고
    • A novel role for ursodeoxycholic acid in inhibiting apoptosis by modulating mitochondrial membrane perturbation
    • Rodrigues, C. M., G. Fan, X. Ma, B. T. Kren, and C. J. Steer. 1998. A novel role for ursodeoxycholic acid in inhibiting apoptosis by modulating mitochondrial membrane perturbation. J. Clin. Invest. 101: 2790-2799.
    • (1998) J. Clin. Invest , vol.101 , pp. 2790-2799
    • Rodrigues, C.M.1    Fan, G.2    Ma, X.3    Kren, B.T.4    Steer, C.J.5
  • 83
    • 0034102505 scopus 로고    scopus 로고
    • Effect of tauroursodeoxycholic acid on bile acid-induced apoptosis in primary human hepatocytes
    • Benz, C., S. Angermuller, G. Otto, P. Sauer, W. Stremmel, and A. Stiehl. 2000. Effect of tauroursodeoxycholic acid on bile acid-induced apoptosis in primary human hepatocytes. Eur. J. Clin. Invest. 30: 203-209.
    • (2000) Eur. J. Clin. Invest , vol.30 , pp. 203-209
    • Benz, C.1    Angermuller, S.2    Otto, G.3    Sauer, P.4    Stremmel, W.5    Stiehl, A.6
  • 84
    • 84889333062 scopus 로고    scopus 로고
    • Castro, R., S. Solá, C. Steer, and C. Rodrigues. 2007. Bile acids as modulators of apoptosis. In Hepatotoxicity: From Genomics to in-Vitro and in-Vivo Models. S. Sahu, editor. John Wiley & Sons, West Sussex, UK. 391-419.
    • Castro, R., S. Solá, C. Steer, and C. Rodrigues. 2007. Bile acids as modulators of apoptosis. In Hepatotoxicity: From Genomics to in-Vitro and in-Vivo Models. S. Sahu, editor. John Wiley & Sons, West Sussex, UK. 391-419.
  • 85
    • 0032846812 scopus 로고    scopus 로고
    • Ursodeoxycholic acid prevents cytochrome c release in apoptosis by inhibiting mitochondrial membrane depolarization and channel formation
    • Rodrigues, C. M., X. Ma, C. Linehan-Stieers, G. Fan, B. T. Kren, and C. J. Steer. 1999. Ursodeoxycholic acid prevents cytochrome c release in apoptosis by inhibiting mitochondrial membrane depolarization and channel formation. Cell Death Differ. 6: 842-854.
    • (1999) Cell Death Differ , vol.6 , pp. 842-854
    • Rodrigues, C.M.1    Ma, X.2    Linehan-Stieers, C.3    Fan, G.4    Kren, B.T.5    Steer, C.J.6
  • 86
    • 0037452957 scopus 로고    scopus 로고
    • Tauroursodeoxycholic acid prevents Bax-induced membrane perturbation and cytochrome C release in isolated mitochondria
    • Rodrigues, C. M., S. Sola, J. C. Sharpe, J. J. Moura, and C. J. Steer. 2003. Tauroursodeoxycholic acid prevents Bax-induced membrane perturbation and cytochrome C release in isolated mitochondria. Biochemistry. 42: 3070-3080.
    • (2003) Biochemistry , vol.42 , pp. 3070-3080
    • Rodrigues, C.M.1    Sola, S.2    Sharpe, J.C.3    Moura, J.J.4    Steer, C.J.5
  • 87
    • 0036291806 scopus 로고    scopus 로고
    • Ursodeoxycholic acid diminishes Fas-ligand-induced apoptosis in mouse hepatocytes
    • Azzaroli, F., W. Mehal, C. J. Soroka, L. Wang, J. Lee, N. Crispe, and J. L. Boyer. 2002. Ursodeoxycholic acid diminishes Fas-ligand-induced apoptosis in mouse hepatocytes. Hepatology. 36: 49-54.
    • (2002) Hepatology , vol.36 , pp. 49-54
    • Azzaroli, F.1    Mehal, W.2    Soroka, C.J.3    Wang, L.4    Lee, J.5    Crispe, N.6    Boyer, J.L.7
  • 88
    • 0036725164 scopus 로고    scopus 로고
    • Effect of tauroursodeoxycholic acid on endoplasmic reticulum stress-induced caspase-12 activation
    • Xie, Q., V. I. Khaoustov, C. C. Chung, J. Sohn, B. Krishnan, D. E. Lewis, and B. Yoffe. 2002. Effect of tauroursodeoxycholic acid on endoplasmic reticulum stress-induced caspase-12 activation. Hepatology. 36: 592-601.
    • (2002) Hepatology , vol.36 , pp. 592-601
    • Xie, Q.1    Khaoustov, V.I.2    Chung, C.C.3    Sohn, J.4    Krishnan, B.5    Lewis, D.E.6    Yoffe, B.7
  • 92
    • 25844516609 scopus 로고    scopus 로고
    • Nuclear translocation of UDCA by the glucocorticoid receptor is required to reduce TGF-β 1-induced apoptosis in rat hepatocytes
    • Solá, S., J. D. Amaral, R. E. Castro, R. M. Ramalho, P. M. Borralho, B. T. Kren, H. Tanaka, C. J. Steer, and C. M. Rodrigues. 2005. Nuclear translocation of UDCA by the glucocorticoid receptor is required to reduce TGF-β 1-induced apoptosis in rat hepatocytes. Hepatology. 42: 925-934.
    • (2005) Hepatology , vol.42 , pp. 925-934
    • Solá, S.1    Amaral, J.D.2    Castro, R.E.3    Ramalho, R.M.4    Borralho, P.M.5    Kren, B.T.6    Tanaka, H.7    Steer, C.J.8    Rodrigues, C.M.9
  • 93
    • 18844397275 scopus 로고    scopus 로고
    • A distinct microarray gene expression profile in primary rat hepatocytes incubated with ursodeoxycholic acid
    • Castro, R. E., S. Solá, X. Ma, R. M. Ramalho, B. T. Kren, C. J. Steer, and C. M. Rodrigues. 2005. A distinct microarray gene expression profile in primary rat hepatocytes incubated with ursodeoxycholic acid. J. Hepatol. 42: 897-906.
    • (2005) J. Hepatol , vol.42 , pp. 897-906
    • Castro, R.E.1    Solá, S.2    Ma, X.3    Ramalho, R.M.4    Kren, B.T.5    Steer, C.J.6    Rodrigues, C.M.7
  • 96
    • 0036098552 scopus 로고    scopus 로고
    • AP-1 as a regulator of cell life and death
    • Shaulian, E., and M. Karin. 2002. AP-1 as a regulator of cell life and death. Nat. Cell Biol. 4: E131-E136.
    • (2002) Nat. Cell Biol , vol.4
    • Shaulian, E.1    Karin, M.2
  • 97
    • 1542467261 scopus 로고    scopus 로고
    • Ursodeoxycholic acid modulates E2F-1 and p53 expression through a caspase-independent mechanism in transforming growth factor β1-induced apoptosis of rat hepatocytes
    • Solá, S., X. Ma, R. E. Castro, B. T. Kren, C. J. Steer, and C. M. Rodrigues. 2003. Ursodeoxycholic acid modulates E2F-1 and p53 expression through a caspase-independent mechanism in transforming growth factor β1-induced apoptosis of rat hepatocytes. J. Biol. Chem. 278: 48831-48838.
    • (2003) J. Biol. Chem , vol.278 , pp. 48831-48838
    • Solá, S.1    Ma, X.2    Castro, R.E.3    Kren, B.T.4    Steer, C.J.5    Rodrigues, C.M.6
  • 98
    • 36348941176 scopus 로고    scopus 로고
    • p53 is a key molecular target of ursodeoxycholic acid in regulating apoptosis
    • Amaral, J. D., R. E. Castro, S. Sola, C. J. Steer, and C. M. Rodrigues. 2007. p53 is a key molecular target of ursodeoxycholic acid in regulating apoptosis. J. Biol. Chem. 282: 34250-34259.
    • (2007) J. Biol. Chem , vol.282 , pp. 34250-34259
    • Amaral, J.D.1    Castro, R.E.2    Sola, S.3    Steer, C.J.4    Rodrigues, C.M.5
  • 99
    • 0038121949 scopus 로고    scopus 로고
    • Ursodeoxycholic acid therapy and the risk of colorectal adenoma in patients with primary biliary cirrhosis: An observational study
    • Serfaty, L., A. De Leusse, O. Rosmorduc, B. Desaint, J. F. Flejou, O. Chazouilleres, R. E. Poupon, and R. Poupon. 2003. Ursodeoxycholic acid therapy and the risk of colorectal adenoma in patients with primary biliary cirrhosis: an observational study. Hepatology. 38: 203-209.
    • (2003) Hepatology , vol.38 , pp. 203-209
    • Serfaty, L.1    De Leusse, A.2    Rosmorduc, O.3    Desaint, B.4    Flejou, J.F.5    Chazouilleres, O.6    Poupon, R.E.7    Poupon, R.8
  • 100
    • 0035895263 scopus 로고    scopus 로고
    • Ursodiol use is associated with lower prevalence of colonic neoplasia in patients with ulcerative colitis and primary sclerosing cholangitis
    • Tung, B. Y., M. J. Emond, R. C. Haggitt, M. P. Bronner, M. B. Kimmey, K. V. Kowdley, and T. A. Brentnall. 2001. Ursodiol use is associated with lower prevalence of colonic neoplasia in patients with ulcerative colitis and primary sclerosing cholangitis. Ann. Intern. Med. 134: 89-95.
    • (2001) Ann. Intern. Med , vol.134 , pp. 89-95
    • Tung, B.Y.1    Emond, M.J.2    Haggitt, R.C.3    Bronner, M.P.4    Kimmey, M.B.5    Kowdley, K.V.6    Brentnall, T.A.7
  • 102
    • 0036917814 scopus 로고    scopus 로고
    • Ursodeoxycholic acid and F(6)-D(3) inhibit aberrant crypt proliferation in the rat azoxymethane model of colon cancer: Roles of cyclin D1 and E-cadherin
    • Wali, R. K., S. Khare, M. Tretiakova, G. Cohen, L. Nguyen, J. Hart, J. Wang, M. Wen, A. Ramaswamy, L. Joseph, et al. 2002. Ursodeoxycholic acid and F(6)-D(3) inhibit aberrant crypt proliferation in the rat azoxymethane model of colon cancer: roles of cyclin D1 and E-cadherin. Cancer Epidemiol. Biomarkers Prev. 11: 1653-1662.
    • (2002) Cancer Epidemiol. Biomarkers Prev , vol.11 , pp. 1653-1662
    • Wali, R.K.1    Khare, S.2    Tretiakova, M.3    Cohen, G.4    Nguyen, L.5    Hart, J.6    Wang, J.7    Wen, M.8    Ramaswamy, A.9    Joseph, L.10
  • 103
  • 104
    • 56349117478 scopus 로고    scopus 로고
    • Ursodeoxycholic acid prevents apoptosis of mouse sensory neurons induced by cisplatin by reducing P53 accumulation
    • Park, H., M. K. Kim, and S. U. Kim. 2008. Ursodeoxycholic acid prevents apoptosis of mouse sensory neurons induced by cisplatin by reducing P53 accumulation. Biochem Biophys Res Commun. 377: 1025-1030.
    • (2008) Biochem Biophys Res Commun , vol.377 , pp. 1025-1030
    • Park, H.1    Kim, M.K.2    Kim, S.U.3
  • 105
    • 3042698849 scopus 로고    scopus 로고
    • Tauroursodeoxycholic acid prevents amyloid-β peptide-induced neuronal death via a phosphatidylinositol 3-kinase-dependent signaling pathway
    • Solá, S., R. E. Castro, P. A. Laires, C. J. Steer, and C. M. Rodrigues. 2003. Tauroursodeoxycholic acid prevents amyloid-β peptide-induced neuronal death via a phosphatidylinositol 3-kinase-dependent signaling pathway. Mol. Med. 9: 226-234.
    • (2003) Mol. Med , vol.9 , pp. 226-234
    • Solá, S.1    Castro, R.E.2    Laires, P.A.3    Steer, C.J.4    Rodrigues, C.M.5
  • 106
    • 26844537040 scopus 로고    scopus 로고
    • Hydrophilic bile salt ursodeoxycholic acid protects myocardium against reperfusion injury in a PI3K/Akt dependent pathway
    • Rajesh, K. G., R. Suzuki, H. Maeda, M. Yamamoto, X. Yutong, and S. Sasaguri. 2005. Hydrophilic bile salt ursodeoxycholic acid protects myocardium against reperfusion injury in a PI3K/Akt dependent pathway. J. Mol. Cell. Cardiol. 39: 766-776.
    • (2005) J. Mol. Cell. Cardiol , vol.39 , pp. 766-776
    • Rajesh, K.G.1    Suzuki, R.2    Maeda, H.3    Yamamoto, M.4    Yutong, X.5    Sasaguri, S.6
  • 107
    • 0035861563 scopus 로고    scopus 로고
    • Functional modulation of the glucocorticoid receptor and suppression of NF-κB-dependent transcription by ursodeoxycholic acid
    • Miura, T., R. Ouchida, N. Yoshikawa, K. Okamoto, Y. Makino, T. Nakamura, C. Morimoto, I. Makino, and H. Tanaka. 2001. Functional modulation of the glucocorticoid receptor and suppression of NF-κB-dependent transcription by ursodeoxycholic acid. J. Biol. Chem. 276: 47371-47378.
    • (2001) J. Biol. Chem , vol.276 , pp. 47371-47378
    • Miura, T.1    Ouchida, R.2    Yoshikawa, N.3    Okamoto, K.4    Makino, Y.5    Nakamura, T.6    Morimoto, C.7    Makino, I.8    Tanaka, H.9
  • 108
    • 31344468014 scopus 로고    scopus 로고
    • Role of mitochondrial glucocorticoid receptor in glucocorticoid-induced apoptosis
    • Sionov, R. V., O. Cohen, S. Kfir, Y. Zilberman, and E. Yefenof. 2006. Role of mitochondrial glucocorticoid receptor in glucocorticoid-induced apoptosis. J. Exp. Med. 203: 189-201.
    • (2006) J. Exp. Med , vol.203 , pp. 189-201
    • Sionov, R.V.1    Cohen, O.2    Kfir, S.3    Zilberman, Y.4    Yefenof, E.5
  • 109
    • 0035869234 scopus 로고    scopus 로고
    • Increased glucocorticoid production and altered cortisol metabolism in women with mild to moderate Alzheimer's disease
    • Rasmuson, S., R. Andrew, B. Nasman, J. R. Seckl, B. R. Walker, and T. Olsson. 2001. Increased glucocorticoid production and altered cortisol metabolism in women with mild to moderate Alzheimer's disease. Biol. Psychiatry. 49: 547-552.
    • (2001) Biol. Psychiatry , vol.49 , pp. 547-552
    • Rasmuson, S.1    Andrew, R.2    Nasman, B.3    Seckl, J.R.4    Walker, B.R.5    Olsson, T.6
  • 110
    • 9444279547 scopus 로고    scopus 로고
    • A-synuclein induces apoptosis by altered expression in human peripheral lymphocyte in Parkinson's disease
    • Kim, S., B. S. Jeon, C. Heo, P. S. Im, T. B. Ahn, J. H. Seo, H. S. Kim, C. H. Park, S. H. Choi, S. H. Cho, et al. 2004. A-synuclein induces apoptosis by altered expression in human peripheral lymphocyte in Parkinson's disease. FASEB J. 18: 1615-1617.
    • (2004) FASEB J , vol.18 , pp. 1615-1617
    • Kim, S.1    Jeon, B.S.2    Heo, C.3    Im, P.S.4    Ahn, T.B.5    Seo, J.H.6    Kim, H.S.7    Park, C.H.8    Choi, S.H.9    Cho, S.H.10
  • 111
    • 0031945984 scopus 로고    scopus 로고
    • Inhibition by dexamethasone of transforming growth factor β 1-induced apoptosis in rat hepatoma cells: A possible association with Bcl-xL induction
    • Yamamoto, M., K. Fukuda, N. Miura, R. Suzuki, T. Kido, and Y. Komatsu. 1998. Inhibition by dexamethasone of transforming growth factor β 1-induced apoptosis in rat hepatoma cells: a possible association with Bcl-xL induction. Hepatology. 27: 959-966.
    • (1998) Hepatology , vol.27 , pp. 959-966
    • Yamamoto, M.1    Fukuda, K.2    Miura, N.3    Suzuki, R.4    Kido, T.5    Komatsu, Y.6
  • 112
    • 0035067079 scopus 로고    scopus 로고
    • Dexamethasone inhibits spontaneous apoptosis in primary cultures of human and rat hepatocytes via Bcl-2 and Bcl-xL induction
    • Bailly-Maitre, B., G. de Sousa, K. Boulukos, J. Gugenheim, and R. Rahmani. 2001. Dexamethasone inhibits spontaneous apoptosis in primary cultures of human and rat hepatocytes via Bcl-2 and Bcl-xL induction. Cell Death Differ. 8: 279-288.
    • (2001) Cell Death Differ , vol.8 , pp. 279-288
    • Bailly-Maitre, B.1    de Sousa, G.2    Boulukos, K.3    Gugenheim, J.4    Rahmani, R.5
  • 114
    • 3042795223 scopus 로고    scopus 로고
    • Physiological and pathological consequences of the interactions of the p53 tumor suppressor with the glucocorticoid, androgen, and estrogen receptors
    • Sengupta, S., and B. Wasylyk. 2004. Physiological and pathological consequences of the interactions of the p53 tumor suppressor with the glucocorticoid, androgen, and estrogen receptors. Ann. N. Y. Acad. Sci. 1024: 54-71.
    • (2004) Ann. N. Y. Acad. Sci , vol.1024 , pp. 54-71
    • Sengupta, S.1    Wasylyk, B.2
  • 115
    • 3142580336 scopus 로고    scopus 로고
    • Modulation of nuclear steroid receptors by ursodeoxycholic acid inhibits TGF-β1-induced E2F-1/p53-mediated apoptosis of rat hepatocytes
    • Solá, S., R. E. Castro, B. T. Kren, C. J. Steer, and C. M. Rodrigues. 2004. Modulation of nuclear steroid receptors by ursodeoxycholic acid inhibits TGF-β1-induced E2F-1/p53-mediated apoptosis of rat hepatocytes. Biochemistry. 43: 8429-8438.
    • (2004) Biochemistry , vol.43 , pp. 8429-8438
    • Solá, S.1    Castro, R.E.2    Kren, B.T.3    Steer, C.J.4    Rodrigues, C.M.5
  • 116
    • 0030974158 scopus 로고    scopus 로고
    • Glucocorticoid receptor-mediated cell cycle arrest is achieved through distinct cell-specific transcriptional regulatory mechanisms
    • Rogatsky, I., J. M. Trowbridge, and M. J. Garabedian. 1997. Glucocorticoid receptor-mediated cell cycle arrest is achieved through distinct cell-specific transcriptional regulatory mechanisms. Mol. Cell. Biol. 17: 3181-3193.
    • (1997) Mol. Cell. Biol , vol.17 , pp. 3181-3193
    • Rogatsky, I.1    Trowbridge, J.M.2    Garabedian, M.J.3
  • 117
    • 0030043423 scopus 로고    scopus 로고
    • Ligand-independent activation of the glucocorticoid receptor by ursodeoxycholic acid. Repression of IFN-gamma-induced MHC class II gene expression via a glucocorticoid receptor-dependent pathway
    • Tanaka, H., Y. Makino, T. Miura, F. Hirano, K. Okamoto, K. Komura, Y. Sato, and I. Makino. 1996. Ligand-independent activation of the glucocorticoid receptor by ursodeoxycholic acid. Repression of IFN-gamma-induced MHC class II gene expression via a glucocorticoid receptor-dependent pathway. J. Immunol. 156: 1601-1608.
    • (1996) J. Immunol , vol.156 , pp. 1601-1608
    • Tanaka, H.1    Makino, Y.2    Miura, T.3    Hirano, F.4    Okamoto, K.5    Komura, K.6    Sato, Y.7    Makino, I.8
  • 119
    • 0036828914 scopus 로고    scopus 로고
    • Inhibition of glucocorticoid-induced apoptosis in 697 pre-B lymphocytes by the mineralocorticoid receptor N-terminal domain
    • Planey, S. L., A. Derfoul, A. Steplewski, N. M. Robertson, and G. Litwack. 2002. Inhibition of glucocorticoid-induced apoptosis in 697 pre-B lymphocytes by the mineralocorticoid receptor N-terminal domain. J. Biol. Chem. 277: 42188-42196.
    • (2002) J. Biol. Chem , vol.277 , pp. 42188-42196
    • Planey, S.L.1    Derfoul, A.2    Steplewski, A.3    Robertson, N.M.4    Litwack, G.5
  • 120
    • 0034117178 scopus 로고    scopus 로고
    • Subtle shifts in the ratio between pro- and antiapoptotic molecules after activation of corticosteroid receptors decide neuronal fate
    • Almeida, O. F., G. L. Conde, C. Crochemore, B. A. Demeneix, D. Fischer, A. H. Hassan, M. Meyer, F. Holsboer, and T. M. Michaelidis. 2000. Subtle shifts in the ratio between pro- and antiapoptotic molecules after activation of corticosteroid receptors decide neuronal fate. FASEB J. 14: 779-790.
    • (2000) FASEB J , vol.14 , pp. 779-790
    • Almeida, O.F.1    Conde, G.L.2    Crochemore, C.3    Demeneix, B.A.4    Fischer, D.5    Hassan, A.H.6    Meyer, M.7    Holsboer, F.8    Michaelidis, T.M.9
  • 121
    • 33749332011 scopus 로고    scopus 로고
    • Functional modulation of nuclear steroid receptors by tauroursodeoxycholic acid reduces amyloid β-peptide-induced apoptosis
    • Solá, S., J. D. Amaral, P. M. Borralho, R. M. Ramalho, R. E. Castro, M. M. Aranha, C. J. Steer, and C. M. Rodrigues. 2006. Functional modulation of nuclear steroid receptors by tauroursodeoxycholic acid reduces amyloid β-peptide-induced apoptosis. Mol. Endocrinol. 20: 2292-2303.
    • (2006) Mol. Endocrinol , vol.20 , pp. 2292-2303
    • Solá, S.1    Amaral, J.D.2    Borralho, P.M.3    Ramalho, R.M.4    Castro, R.E.5    Aranha, M.M.6    Steer, C.J.7    Rodrigues, C.M.8
  • 122
    • 0034163857 scopus 로고    scopus 로고
    • Catabolites of cholesterol synthesis pathways and forskolin as activators of the farnesoid X-activated nuclear receptor
    • Howard, W. R., J. A. Pospisil, E. Njolito, and D. J. Noonan. 2000. Catabolites of cholesterol synthesis pathways and forskolin as activators of the farnesoid X-activated nuclear receptor. Toxicol. Appl. Pharmacol. 163: 195-202.
    • (2000) Toxicol. Appl. Pharmacol , vol.163 , pp. 195-202
    • Howard, W.R.1    Pospisil, J.A.2    Njolito, E.3    Noonan, D.J.4
  • 123
    • 0034646603 scopus 로고    scopus 로고
    • Farnesoid X receptor responds to bile acids and represses cholesterol 7α-hydroxylase gene (CYP7A1) transcription
    • Chiang, J. Y., R. Kimmel, C. Weinberger, and D. Stroup. 2000. Farnesoid X receptor responds to bile acids and represses cholesterol 7α-hydroxylase gene (CYP7A1) transcription. J. Biol. Chem. 275: 10918-10924.
    • (2000) J. Biol. Chem , vol.275 , pp. 10918-10924
    • Chiang, J.Y.1    Kimmel, R.2    Weinberger, C.3    Stroup, D.4
  • 124
    • 1642483471 scopus 로고    scopus 로고
    • Feed-forward regulation of bile acid detoxification by CYP3A4: Studies in humanized transgenic mice
    • Stedman, C., G. Robertson, S. Coulter, and C. Liddle. 2004. Feed-forward regulation of bile acid detoxification by CYP3A4: studies in humanized transgenic mice. J. Biol. Chem. 279: 11336-11343.
    • (2004) J. Biol. Chem , vol.279 , pp. 11336-11343
    • Stedman, C.1    Robertson, G.2    Coulter, S.3    Liddle, C.4
  • 125
  • 126
    • 33750292972 scopus 로고    scopus 로고
    • Cell death in the nervous system
    • Bredesen, D. E., R. V. Rao, and P. Mehlen. 2006. Cell death in the nervous system. Nature. 443: 796-802.
    • (2006) Nature , vol.443 , pp. 796-802
    • Bredesen, D.E.1    Rao, R.V.2    Mehlen, P.3
  • 127
    • 0034799214 scopus 로고    scopus 로고
    • A bile acid protects against motor and cognitive deficits and reduces striatal degeneration in the 3-nitropropionic acid model of Huntington's disease
    • Keene, C. D., C. M. Rodrigues, T. Eich, C. Linehan-Stieers, A. Abt, B. T. Kren, C. J. Steer, and W. C. Low. 2001. A bile acid protects against motor and cognitive deficits and reduces striatal degeneration in the 3-nitropropionic acid model of Huntington's disease. Exp. Neurol. 171: 351-360.
    • (2001) Exp. Neurol , vol.171 , pp. 351-360
    • Keene, C.D.1    Rodrigues, C.M.2    Eich, T.3    Linehan-Stieers, C.4    Abt, A.5    Kren, B.T.6    Steer, C.J.7    Low, W.C.8
  • 128
    • 0033769186 scopus 로고    scopus 로고
    • Tauroursodeoxycholic acid partially prevents apoptosis induced by 3-nitropropionic acid: Evidence for a mitochondrial pathway independent of the permeability transition
    • Rodrigues, C. M., C. L. Stieers, C. D. Keene, X. Ma, B. T. Kren, W. C. Low, and C. J. Steer. 2000. Tauroursodeoxycholic acid partially prevents apoptosis induced by 3-nitropropionic acid: evidence for a mitochondrial pathway independent of the permeability transition. J. Neurochem. 75: 2368-2379.
    • (2000) J. Neurochem , vol.75 , pp. 2368-2379
    • Rodrigues, C.M.1    Stieers, C.L.2    Keene, C.D.3    Ma, X.4    Kren, B.T.5    Low, W.C.6    Steer, C.J.7
  • 129
    • 0036677435 scopus 로고    scopus 로고
    • Tauroursodeoxycholic acid, a bile acid, is neuroprotective in a transgenic animal model of Huntington's disease
    • Keene, C. D., C. M. Rodrigues, T. Eich, M. S. Chhabra, C. J. Steer, and W. C. Low. 2002. Tauroursodeoxycholic acid, a bile acid, is neuroprotective in a transgenic animal model of Huntington's disease. Proc. Natl. Acad. Sci. USA. 99: 10671-10676.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10671-10676
    • Keene, C.D.1    Rodrigues, C.M.2    Eich, T.3    Chhabra, M.S.4    Steer, C.J.5    Low, W.C.6
  • 130
    • 0035998716 scopus 로고    scopus 로고
    • Tauroursodeoxycholic acid improves the survival and function of nigral transplants in a rat model of Parkinson's disease
    • Duan, W. M., C. M. Rodrigues, L. R. Zhao, C. J. Steer, and W. C. Low. 2002. Tauroursodeoxycholic acid improves the survival and function of nigral transplants in a rat model of Parkinson's disease. Cell Transplant. 11: 195-205.
    • (2002) Cell Transplant , vol.11 , pp. 195-205
    • Duan, W.M.1    Rodrigues, C.M.2    Zhao, L.R.3    Steer, C.J.4    Low, W.C.5
  • 131
    • 30044434872 scopus 로고    scopus 로고
    • Similar patterns of mitochondrial vulnerability and rescue induced by genetic modification of α-synuclein, parkin and DJ-1 in C. elegans
    • Ved, R., S. Saha, B. Westlund, C. Perier, L. G. Burnam, A. Sluder, M. Hoener, C. M. Rodrigues, A. Alfonso, C. Steer, et al. 2005. Similar patterns of mitochondrial vulnerability and rescue induced by genetic modification of α-synuclein, parkin and DJ-1 in C. elegans. J. Biol. Chem. 280: 42655-42668.
    • (2005) J. Biol. Chem , vol.280 , pp. 42655-42668
    • Ved, R.1    Saha, S.2    Westlund, B.3    Perier, C.4    Burnam, L.G.5    Sluder, A.6    Hoener, M.7    Rodrigues, C.M.8    Alfonso, A.9    Steer, C.10
  • 133
    • 0038623782 scopus 로고    scopus 로고
    • Tauroursodeoxycholic acid reduces apoptosis and protects against neurological injury after acute hemorrhagic stroke in rats
    • Rodrigues, C. M., S. Sola, Z. Nan, R. E. Castro, P. S. Ribeiro, W. C. Low, and C. J. Steer. 2003. Tauroursodeoxycholic acid reduces apoptosis and protects against neurological injury after acute hemorrhagic stroke in rats. Proc. Natl. Acad. Sci. USA. 100: 6087-6092.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6087-6092
    • Rodrigues, C.M.1    Sola, S.2    Nan, Z.3    Castro, R.E.4    Ribeiro, P.S.5    Low, W.C.6    Steer, C.J.7
  • 136
    • 6344279913 scopus 로고    scopus 로고
    • The bile acid tauroursodeoxycholic acid modulates phosphorylation and translocation of bad via phosphatidylinositol 3-kinase in glutamate-induced apoptosis of rat cortical neurons
    • Castro, R. E., S. Sola, R. M. Ramalho, C. J. Steer, and C. M. Rodrigues. 2004. The bile acid tauroursodeoxycholic acid modulates phosphorylation and translocation of bad via phosphatidylinositol 3-kinase in glutamate-induced apoptosis of rat cortical neurons. J. Pharmacol. Exp. Ther. 311: 845-852.
    • (2004) J. Pharmacol. Exp. Ther , vol.311 , pp. 845-852
    • Castro, R.E.1    Sola, S.2    Ramalho, R.M.3    Steer, C.J.4    Rodrigues, C.M.5
  • 137
    • 34250819839 scopus 로고    scopus 로고
    • Intracellular amyloid-β in Alzheimer's disease
    • LaFerla, F. M., K. N. Green, and S. Oddo. 2007. Intracellular amyloid-β in Alzheimer's disease. Nat. Rev. Neurosci. 8: 499-509.
    • (2007) Nat. Rev. Neurosci , vol.8 , pp. 499-509
    • LaFerla, F.M.1    Green, K.N.2    Oddo, S.3
  • 138
    • 0034327232 scopus 로고    scopus 로고
    • Bilirubin and amyloid-β peptide induce cytochrome c release through mitochondrial membrane permeabilization
    • Rodrigues, C. M., S. Sola, R. Silva, and D. Brites. 2000. Bilirubin and amyloid-β peptide induce cytochrome c release through mitochondrial membrane permeabilization. Mol. Med. 6: 936-946.
    • (2000) Mol. Med , vol.6 , pp. 936-946
    • Rodrigues, C.M.1    Sola, S.2    Silva, R.3    Brites, D.4
  • 139
    • 3342885971 scopus 로고    scopus 로고
    • Inhibition of the E2F-1/p53/Bax pathway by tauroursodeoxycholic acid in amyloid β-peptide-induced apoptosis of PC12 cells
    • Ramalho, R. M., P. S. Ribeiro, S. Solá, R. E. Castro, C. J. Steer, and C. M. Rodrigues. 2004. Inhibition of the E2F-1/p53/Bax pathway by tauroursodeoxycholic acid in amyloid β-peptide-induced apoptosis of PC12 cells. J. Neurochem. 90: 567-575.
    • (2004) J. Neurochem , vol.90 , pp. 567-575
    • Ramalho, R.M.1    Ribeiro, P.S.2    Solá, S.3    Castro, R.E.4    Steer, C.J.5    Rodrigues, C.M.6
  • 140
    • 33746862168 scopus 로고    scopus 로고
    • Tauroursodeoxycholic acid modulates p53-mediated apoptosis in Alzheimer's disease mutant neuroblastoma cells
    • Ramalho, R. M., P. M. Borralho, R. E. Castro, S. Solá, C. J. Steer, and C. M. Rodrigues. 2006. Tauroursodeoxycholic acid modulates p53-mediated apoptosis in Alzheimer's disease mutant neuroblastoma cells. J. Neurochem. 98: 1610-1618.
    • (2006) J. Neurochem , vol.98 , pp. 1610-1618
    • Ramalho, R.M.1    Borralho, P.M.2    Castro, R.E.3    Solá, S.4    Steer, C.J.5    Rodrigues, C.M.6
  • 141
    • 44649156233 scopus 로고    scopus 로고
    • Apoptosis in transgenic mice expressing the P301L mutated form of human tau
    • Ramalho, R. M., R. J. Viana, R. E. Castro, C. J. Steer, W. C. Low, and C. M. Rodrigues. 2008. Apoptosis in transgenic mice expressing the P301L mutated form of human tau. Mol. Med. 14: 309-317.
    • (2008) Mol. Med , vol.14 , pp. 309-317
    • Ramalho, R.M.1    Viana, R.J.2    Castro, R.E.3    Steer, C.J.4    Low, W.C.5    Rodrigues, C.M.6
  • 142
    • 0034812181 scopus 로고    scopus 로고
    • Amyloid β-peptide disrupts mitochondrial membrane lipid and protein structure: Protective role of tauroursodeoxycholate
    • Rodrigues, C. M., S. Solá, M. A. Brito, C. D. Brondino, D. Brites, and J. J. Moura. 2001. Amyloid β-peptide disrupts mitochondrial membrane lipid and protein structure: protective role of tauroursodeoxycholate. Biochem. Biophys. Res. Commun. 281: 468-474.
    • (2001) Biochem. Biophys. Res. Commun , vol.281 , pp. 468-474
    • Rodrigues, C.M.1    Solá, S.2    Brito, M.A.3    Brondino, C.D.4    Brites, D.5    Moura, J.J.6
  • 145
    • 49349097870 scopus 로고    scopus 로고
    • Anti-apoptotic treatment reduces transthyretin deposition in a transgenic mouse model of familial amyloidotic polyneuropathy
    • Macedo, B., A. R. Batista, N. Ferreira, M. R. Almeida, and M. J. Saraiva. 2008. Anti-apoptotic treatment reduces transthyretin deposition in a transgenic mouse model of familial amyloidotic polyneuropathy. Biochim. Biophys. Acta. 1782: 517-522.
    • (2008) Biochim. Biophys. Acta , vol.1782 , pp. 517-522
    • Macedo, B.1    Batista, A.R.2    Ferreira, N.3    Almeida, M.R.4    Saraiva, M.J.5


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