메뉴 건너뛰기




Volumn 103, Issue 1, 1999, Pages 137-145

Toxic bile salts induce rodent hepatocyte apoptosis via direct activation of Fas

Author keywords

[No Author keywords available]

Indexed keywords

BILE SALT; CASPASE; CATHEPSIN B; FAS ANTIGEN; GLYCOCHENODEOXYCHOLIC ACID; GREEN FLUORESCENT PROTEIN; LAMIN B; MESSENGER RNA; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PROTEINASE;

EID: 0032919402     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI4765     Document Type: Article
Times cited : (483)

References (42)
  • 1
    • 0025247125 scopus 로고
    • Hepatic injury induced by bile salts: Correlation between biochemical and morphological events
    • Schmucker, D.L., Ohta, M., Kanai, S., Sato, V., and Kitani, K. 1990. Hepatic injury induced by bile salts: correlation between biochemical and morphological events. Hepatology. 12:1216-1221.
    • (1990) Hepatology , vol.12 , pp. 1216-1221
    • Schmucker, D.L.1    Ohta, M.2    Kanai, S.3    Sato, V.4    Kitani, K.5
  • 2
    • 0015434595 scopus 로고
    • Mechanism of cholestasis. 5. Bile acids in normal rat livers and in those after bile duct ligation
    • Greim, H., et al. 1972. Mechanism of cholestasis. 5. Bile acids in normal rat livers and in those after bile duct ligation. Gastroenterology. 63:837-845.
    • (1972) Gastroenterology , vol.63 , pp. 837-845
    • Greim, H.1
  • 3
    • 0015434596 scopus 로고
    • Mechanism of cholestasis. 6. Bile acids in human livers with or without biliary obstruction
    • Greim, H., et al. 1972. Mechanism of cholestasis. 6. Bile acids in human livers with or without biliary obstruction. Gastroenterology. 63:846-850.
    • (1972) Gastroenterology , vol.63 , pp. 846-850
    • Greim, H.1
  • 4
    • 0028135420 scopus 로고
    • Increases of intracellular magnesium promote glycochenodeoxycholate-induced apoptosis in rat hepatocytes
    • Patel, T., Bronk, S.F., and Gores, G.J. 1994. Increases of intracellular magnesium promote glycochenodeoxycholate-induced apoptosis in rat hepatocytes. J. Clin. Invest. 94:2183-2192.
    • (1994) J. Clin. Invest. , vol.94 , pp. 2183-2192
    • Patel, T.1    Bronk, S.F.2    Gores, G.J.3
  • 5
    • 0028911047 scopus 로고
    • Nuclear serine protease activity contributes to bile acid-induced apoptosis in hepatocytes
    • Kwo, P., Patel, T., Bronk, S.F., and Gores, G.J. 1995. Nuclear serine protease activity contributes to bile acid-induced apoptosis in hepatocytes. Am. J. Physiol. (Lond.). 268:G613-G621.
    • (1995) Am. J. Physiol. (Lond.) , vol.268
    • Kwo, P.1    Patel, T.2    Bronk, S.F.3    Gores, G.J.4
  • 6
    • 0029927422 scopus 로고    scopus 로고
    • The role of proteases during apoptosis
    • Patel, T., Gores, G.J., and Kaufmann, S.H. 1996. The role of proteases during apoptosis. FASEB J. 10:587-597.
    • (1996) FASEB J. , vol.10 , pp. 587-597
    • Patel, T.1    Gores, G.J.2    Kaufmann, S.H.3
  • 7
    • 0029995766 scopus 로고    scopus 로고
    • A license to kill
    • Fraser, A., and Evan, G. 1996. A license to kill Cell. 85:781-784.
    • (1996) Cell , vol.85 , pp. 781-784
    • Fraser, A.1    Evan, G.2
  • 8
    • 0041523475 scopus 로고    scopus 로고
    • Cathepsin B contributes to bile salt-induced apoptosis of rat hepatocytes
    • Roberts, L.R., et al. 1997. Cathepsin B contributes to bile salt-induced apoptosis of rat hepatocytes. Gastroenterology. 12:1-10.
    • (1997) Gastroenterology , vol.12 , pp. 1-10
    • Roberts, L.R.1
  • 9
    • 0031753981 scopus 로고    scopus 로고
    • Cystatin A expression reduces bile salt-induced apoptosis in a rat hepatoma cell line
    • Jones, B.A., Roberts, P.J., Faubion, W.A., Kominami, E., and Gores, G.J. 1998. Cystatin A expression reduces bile salt-induced apoptosis in a rat hepatoma cell line. Am. J. Physiol. 275:G723-G730.
    • (1998) Am. J. Physiol. , vol.275
    • Jones, B.A.1    Roberts, P.J.2    Faubion, W.A.3    Kominami, E.4    Gores, G.J.5
  • 10
    • 0030973417 scopus 로고    scopus 로고
    • Multiple species of CPP32 and Mch2 are the major active caspases present in apoptotic cells
    • Faleiro, L., Kobayashi, R., Fearnhead, H., and Lazebnik, Y. 1997. Multiple species of CPP32 and Mch2 are the major active caspases present in apoptotic cells. EMBO J. 16:2271-2281.
    • (1997) EMBO J. , vol.16 , pp. 2271-2281
    • Faleiro, L.1    Kobayashi, R.2    Fearnhead, H.3    Lazebnik, Y.4
  • 11
    • 0009530192 scopus 로고    scopus 로고
    • Human ICE/CED-3 protease nomenclature
    • Alnemri, E.S., et al. 1996. Human ICE/CED-3 protease nomenclature. Cell. 87:171.
    • (1996) Cell , vol.87 , pp. 171
    • Alnemri, E.S.1
  • 12
    • 0032546783 scopus 로고    scopus 로고
    • ERICE, a novel FLICE-activatable caspase
    • Humke, E.W., Ni, J., and Dixit, V.M. 1998. ERICE, a novel FLICE-activatable caspase. J. Biol. Chem. 273:15702-15707.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15702-15707
    • Humke, E.W.1    Ni, J.2    Dixit, V.M.3
  • 13
    • 0030702084 scopus 로고    scopus 로고
    • Caspases: Intracellular signaling by proteolysis
    • Salvesen, G., and Dixit, V.M. 1997. Caspases: intracellular signaling by proteolysis. Cell. 91:443-446.
    • (1997) Cell , vol.91 , pp. 443-446
    • Salvesen, G.1    Dixit, V.M.2
  • 14
    • 0031045588 scopus 로고    scopus 로고
    • CRADD, a novel human apoptotic adaptor molecule for caspase-2, and FasL/tumor necrosis factor receptor-interacting protein RIP
    • Ahmad, M., et al. 1997. CRADD, a novel human apoptotic adaptor molecule for caspase-2, and FasL/tumor necrosis factor receptor-interacting protein RIP. Cancer Res. 57:615-619.
    • (1997) Cancer Res. , vol.57 , pp. 615-619
    • Ahmad, M.1
  • 15
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORT/FADD-interacting protease, in Fas/APO-1-and TNF receptor-induced cell death
    • Boldin, M.P., Goncharov, T.M., Goltsev, Y.V., and Wallach, D. 1996. Involvement of MACH, a novel MORT/FADD-interacting protease, in Fas/APO-1-and TNF receptor-induced cell death. Cell. 85:803-815.
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 16
    • 15844412409 scopus 로고    scopus 로고
    • FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95(APO-1) death-inducing signaling complex
    • Muzio, M., et al. 1996. FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95(APO-1) death-inducing signaling complex. Cell. 85:817-827.
    • (1996) Cell , vol.85 , pp. 817-827
    • Muzio, M.1
  • 17
    • 10544236916 scopus 로고    scopus 로고
    • Signal transduction by DR3, a death domain-containing receptor related to TNFR-1 and CD95
    • Chinnaiyan, A.M., et al. 1996. Signal transduction by DR3, a death domain-containing receptor related to TNFR-1 and CD95. Science. 274:990-992.
    • (1996) Science , vol.274 , pp. 990-992
    • Chinnaiyan, A.M.1
  • 18
    • 0030705234 scopus 로고    scopus 로고
    • p28 Bap31, a Bcl-2/Bcl-XL- and procaspase-8-associated protein in the endoplasmic reticulum
    • Ng, F., et al. 1997. p28 Bap31, a Bcl-2/Bcl-XL- and procaspase-8-associated protein in the endoplasmic reticulum. J. Cell Biol. 139:327-338.
    • (1997) J. Cell Biol. , vol.139 , pp. 327-338
    • Ng, F.1
  • 19
    • 0032536771 scopus 로고    scopus 로고
    • Two CD95 (APO-1/Fas) signaling pathways
    • Scaffidi, C. et al. 1998 Two CD95 (APO-1/Fas) signaling pathways. EMBO J. 17:1675-1687.
    • (1998) EMBO J. , vol.17 , pp. 1675-1687
    • Scaffidi, C.1
  • 20
    • 0019781507 scopus 로고
    • Mouse liver cell culture. I. Hepatocyte isolation
    • Klaunig, J., et al. 1981, Mouse liver cell culture. I. Hepatocyte isolation. In Vitro. 17:913-925.
    • (1981) In Vitro , vol.17 , pp. 913-925
    • Klaunig, J.1
  • 21
    • 0031014749 scopus 로고    scopus 로고
    • Development and initial application of an in vitro model of apoptosis in rodent cholangiocytes
    • Que, F.G., Gores, G.J., and LaRusso, N.F. 1997. Development and initial application of an in vitro model of apoptosis in rodent cholangiocytes. Am. J. Physiol. 272:G106-G115.
    • (1997) Am. J. Physiol. , vol.272
    • Que, F.G.1    Gores, G.J.2    LaRusso, N.F.3
  • 22
    • 0028179134 scopus 로고
    • Inactivation of interleukin-1 beta converting enzyme by peptide (acyloxy) methyl ketones
    • Thornberry, N.A., et al. 1994. Inactivation of interleukin-1 beta converting enzyme by peptide (acyloxy) methyl ketones. Biochemistry. 33:3934-3940.
    • (1994) Biochemistry , vol.33 , pp. 3934-3940
    • Thornberry, N.A.1
  • 23
    • 0030977847 scopus 로고    scopus 로고
    • Target protease specificity of the viral serpin CrmA: Analysis of five caspases
    • Zhou, Q., et al. 1997. Target protease specificity of the viral serpin CrmA: analysis of five caspases. J. Biol. Chem. 272:7797-7800.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7797-7800
    • Zhou, Q.1
  • 24
    • 0001396685 scopus 로고
    • The slow-binding and slow, tight-binding inhibition of enzyme-catalysed reactions
    • Morrison, J.F. 1982. The slow-binding and slow, tight-binding inhibition of enzyme-catalysed reactions. Trends Biochem. Sci. 7:102-105.
    • (1982) Trends Biochem. Sci. , vol.7 , pp. 102-105
    • Morrison, J.F.1
  • 25
    • 0029807603 scopus 로고    scopus 로고
    • Selective induction of apoptosis in Hep 3B cells by topoisomerase I inhibitors: Evidence for a protease-dependent pathway that does not activate cysteine protease P32
    • Adjei, P., Kaufmann, S.H., Leung, W., Mao, F., and Gores, G.J. 1996. Selective induction of apoptosis in Hep 3B cells by topoisomerase I inhibitors: evidence for a protease-dependent pathway that does not activate cysteine protease P32. J. Clin. Invest. 98:2588-2595.
    • (1996) J. Clin. Invest. , vol.98 , pp. 2588-2595
    • Adjei, P.1    Kaufmann, S.H.2    Leung, W.3    Mao, F.4    Gores, G.J.5
  • 26
    • 0030881603 scopus 로고    scopus 로고
    • Biochemical characteristics of caspases-3, -6,-7, and -8
    • Salvesen, G., and Stennicke, H. 1997. Biochemical characteristics of caspases-3, -6,-7, and -8. J. Biol. Chem. 272:25719-25723.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25719-25723
    • Salvesen, G.1    Stennicke, H.2
  • 27
    • 12644286556 scopus 로고    scopus 로고
    • Death effector domain-containing herpesvirus and poxvirus proteins inhibit both Fas- and TNFR1-induced apoptosis
    • Bertin, J. et al. 1997. Death effector domain-containing herpesvirus and poxvirus proteins inhibit both Fas- and TNFR1-induced apoptosis. Proc. Natl. Acad. Sci. USA. 94:1172-1176.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1172-1176
    • Bertin, J.1
  • 28
    • 0032518446 scopus 로고    scopus 로고
    • Dominant-negative FADD inhibits TNFR60-, Fas/Apo1- and TRAIL-R/Apo2-mediated cell death but not gene induction
    • Wajant, H., et al. 1998. Dominant-negative FADD inhibits TNFR60-, Fas/Apo1- and TRAIL-R/Apo2-mediated cell death but not gene induction. Curr. Biol. 8:113-116.
    • (1998) Curr. Biol. , vol.8 , pp. 113-116
    • Wajant, H.1
  • 29
    • 15444344933 scopus 로고    scopus 로고
    • Activation of multiple interleukin-1beta converting enzyme homologues in cytosol and nuclei of HL-60 cells during etoposide-induced apoptosis
    • Martins, L.M., et al. 1997. Activation of multiple interleukin-1beta converting enzyme homologues in cytosol and nuclei of HL-60 cells during etoposide-induced apoptosis. J. Biol. Chem. 272:7421-7430.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7421-7430
    • Martins, L.M.1
  • 30
    • 0031943921 scopus 로고    scopus 로고
    • Ultraviolet light induces apoptosis via direct activation of CD95 (Fas/APO-1) independently of its ligand CD95L
    • Aragane, Y., et al. 1998. Ultraviolet light induces apoptosis via direct activation of CD95 (Fas/APO-1) independently of its ligand CD95L. J. Cell Biol. 140:171-182.
    • (1998) J. Cell Biol. , vol.140 , pp. 171-182
    • Aragane, Y.1
  • 31
    • 0030868999 scopus 로고    scopus 로고
    • Ultraviolet radiation-induced apoptosis is mediated by activation of CD-95 (Fas/APO-1)
    • Rehemtulla, A., Hamilton, C., Chinnaiyan, A.M. and Dixit, V.M. 1997. Ultraviolet radiation-induced apoptosis is mediated by activation of CD-95 (Fas/APO-1). J. Biol. Chem. 272:25783-25786.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25783-25786
    • Rehemtulla, A.1    Hamilton, C.2    Chinnaiyan, A.M.3    Dixit, V.M.4
  • 33
    • 0030948457 scopus 로고    scopus 로고
    • Substrate specificities of caspase family proteases
    • Talanian, R.V., et al. 1997. Substrate specificities of caspase family proteases. J. Biol. Chem. 272:9677-9682.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9677-9682
    • Talanian, R.V.1
  • 34
    • 0032548502 scopus 로고    scopus 로고
    • Bcl-xL functions downstream of caspase-8 to inhibit Fas- and tumor necrosis factor receptor 1-induced apoptosis of MCF7 breast carcinoma cells
    • Srinivasan, A., et al. 1998. Bcl-xL functions downstream of caspase-8 to inhibit Fas- and tumor necrosis factor receptor 1-induced apoptosis of MCF7 breast carcinoma cells. J. Biol. Chem. 273:4523-4529.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4523-4529
    • Srinivasan, A.1
  • 35
    • 0028380851 scopus 로고
    • Mutations in the Fas antigen gene in lpr mice
    • Nagata, S. 1994. Mutations in the Fas antigen gene in lpr mice. Semin. Immunol. 6:3-8.
    • (1994) Semin. Immunol. , vol.6 , pp. 3-8
    • Nagata, S.1
  • 36
    • 0027291205 scopus 로고
    • Lethal effect of the anti-Fas antibody in mice
    • Ogasawara, J., et al. 1993. Lethal effect of the anti-Fas antibody in mice. Nature. 364:806-809.
    • (1993) Nature , vol.364 , pp. 806-809
    • Ogasawara, J.1
  • 37
    • 0032550366 scopus 로고    scopus 로고
    • Conversion of membrane-bound Fas(CD95) ligand to its soluble form is associated with downregulation of its proapoptotic activity and loss of liver toxicity
    • Schneider, P., et al. 1998. Conversion of membrane-bound Fas(CD95) ligand to its soluble form is associated with downregulation of its proapoptotic activity and loss of liver toxicity. J. Exp. Med. 187:1205-1213.
    • (1998) J. Exp. Med. , vol.187 , pp. 1205-1213
    • Schneider, P.1
  • 38
    • 0032143986 scopus 로고    scopus 로고
    • Targeted disruption of the mouse caspase 8 gene ablates cell death induction by the TNF receptors, FAS/APO1, and DR3 and is lethal prenatally
    • Varfolomeev, E.E., et al. 1998. Targeted disruption of the mouse caspase 8 gene ablates cell death induction by the TNF receptors, FAS/APO1, and DR3 and is lethal prenatally. Immunity. 9:267-276.
    • (1998) Immunity , vol.9 , pp. 267-276
    • Varfolomeev, E.E.1
  • 39
    • 0030931876 scopus 로고    scopus 로고
    • Caspases; the executioners of apoptosis
    • Cohen, G. 1997. Caspases; the executioners of apoptosis. Biochem. J. 326:1-16.
    • (1997) Biochem. J. , vol.326 , pp. 1-16
    • Cohen, G.1
  • 40
    • 0032518448 scopus 로고    scopus 로고
    • Role of an acidic compartment in tumor-necrosis-factor-alpha-induced production of ceramide, activation of caspase-3 and apoptosis
    • Monney, L., et al. 1997. Role of an acidic compartment in tumor-necrosis-factor-alpha-induced production of ceramide, activation of caspase-3 and apoptosis. Eur. J. Biochem. 251:295-303.
    • (1997) Eur. J. Biochem. , vol.251 , pp. 295-303
    • Monney, L.1
  • 41
    • 0030892234 scopus 로고    scopus 로고
    • Apoptosis by death factor
    • Nagata, S. 1997. Apoptosis by death factor. Cell. 88:355-365.
    • (1997) Cell , vol.88 , pp. 355-365
    • Nagata, S.1
  • 42
    • 0028351832 scopus 로고
    • Ursodeoxycholate conjugates protect against disruption of cholesterol-rich membranes by bile salts
    • Heuman, D., and Bajaj, R. 1994. Ursodeoxycholate conjugates protect against disruption of cholesterol-rich membranes by bile salts. Gastroenterology. 106:1333-1341.
    • (1994) Gastroenterology , vol.106 , pp. 1333-1341
    • Heuman, D.1    Bajaj, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.