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Volumn 22, Issue 3-4, 2003, Pages 62-70

A Bcl-2 transgene expressed in hepatocytes does not protect mice from fulminant liver destruction induced by Fas ligand

Author keywords

Apoptosis; Bcl 2; FasL; Hepatitis

Indexed keywords

CASPASE; CELL NUCLEUS DNA; CYTOCHROME C; FAS ANTIBODY; FAS ANTIGEN; FAS LIGAND; FASL PROTEIN; MEMBRANE PROTEIN; PROTEIN BCL 2; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 0037708792     PISSN: 10434666     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1043-4666(03)00111-X     Document Type: Article
Times cited : (9)

References (36)
  • 1
    • 0033396491 scopus 로고    scopus 로고
    • Fas ligand-induced apoptosis
    • Nagata S. Fas ligand-induced apoptosis. Annu Rev Genet. 33:1999;29-55.
    • (1999) Annu Rev Genet , vol.33 , pp. 29-55
    • Nagata, S.1
  • 2
    • 0028883850 scopus 로고
    • Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor
    • Kischkel F.C., Hellbardt S., Behrmann I., Germer M., Pawlita M., Krammer P.H., et al. Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor. EMBO J. 14:1995;5579-5588.
    • (1995) EMBO J , vol.14 , pp. 5579-5588
    • Kischkel, F.C.1    Hellbardt, S.2    Behrmann, I.3    Germer, M.4    Pawlita, M.5    Krammer, P.H.6
  • 3
    • 0029026548 scopus 로고
    • FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis
    • Chinnaiyan A.M., O'Rourke K., Tewari M., Dixit V.M. FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. Cell. 81:1995;505-512.
    • (1995) Cell , vol.81 , pp. 505-512
    • Chinnaiyan, A.M.1    O'Rourke, K.2    Tewari, M.3    Dixit, V.M.4
  • 4
    • 0028913550 scopus 로고
    • A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain
    • Boldin M.P., Varfolomeev E.E., Pancer Z., Mett I.L., Camonis J.H., Wallach D. A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain. J Biol Chem. 270:1995;7795-7798.
    • (1995) J Biol Chem , vol.270 , pp. 7795-7798
    • Boldin, M.P.1    Varfolomeev, E.E.2    Pancer, Z.3    Mett, I.L.4    Camonis, J.H.5    Wallach, D.6
  • 5
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death
    • Boldin M.P., Goncharov T.M., Goltsev Y.V., Wallach D. Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death. Cell. 85:1996;803-815.
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 6
    • 15844412409 scopus 로고    scopus 로고
    • FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex
    • Muzio M., Chinnaiyan A.M., Kischkel F.C., O'Rourke K., Shevchenko A., Ni J., et al. FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex. Cell. 85:1996;817-827.
    • (1996) Cell , vol.85 , pp. 817-827
    • Muzio, M.1    Chinnaiyan, A.M.2    Kischkel, F.C.3    O'Rourke, K.4    Shevchenko, A.5    Ni, J.6
  • 7
    • 0030925774 scopus 로고    scopus 로고
    • FLICE is activated by association with the CD95 death-inducing signaling complex (DISC)
    • Medema J.P., Scaffidi C., Kischkel F.C., Shevchenko A., Mann M., Krammer P.H., et al. FLICE is activated by association with the CD95 death-inducing signaling complex (DISC). EMBO J. 16:1997;2794-2804.
    • (1997) EMBO J , vol.16 , pp. 2794-2804
    • Medema, J.P.1    Scaffidi, C.2    Kischkel, F.C.3    Shevchenko, A.4    Mann, M.5    Krammer, P.H.6
  • 9
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P., Nijhawan D., Budihardjo I., Srinivasula S.M., Ahmad M., Alnemri E.S., et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell. 91:1997;479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6
  • 10
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H., Zhu H., Xu C.J., Yuan J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell. 94:1998;491-501.
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 11
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo X., Budihardjo I., Zou H., Slaughter C., Wang X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell. 94:1998;481-490.
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 12
    • 0034105784 scopus 로고    scopus 로고
    • Apaf-1 oligomerizes into biologically active approximately 700-kDa and inactive approximately 1.4-MDa apoptosome complexes
    • Cain K., Bratton S.B., Langlais C., Walker G., Brown D.G., Sun X.M., et al. Apaf-1 oligomerizes into biologically active approximately 700-kDa and inactive approximately 1.4-MDa apoptosome complexes. J Biol Chem. 275:2000;6067-6070.
    • (2000) J Biol Chem , vol.275 , pp. 6067-6070
    • Cain, K.1    Bratton, S.B.2    Langlais, C.3    Walker, G.4    Brown, D.G.5    Sun, X.M.6
  • 13
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck R.M., Bossy-Wetzel E., Green D.R., Newmeyer D.D. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science. 275:1997;1132-1136.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 14
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked
    • Yang J., Liu X., Bhalla K., Kim C.N., Ibrado A.M., Cai J., et al. Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked. Science. 275:1997;1129-1132.
    • (1997) Science , vol.275 , pp. 1129-1132
    • Yang, J.1    Liu, X.2    Bhalla, K.3    Kim, C.N.4    Ibrado, A.M.5    Cai, J.6
  • 17
    • 13344279418 scopus 로고    scopus 로고
    • Bcl-2 protects from lethal hepatic apoptosis induced by an anti-Fas antibody in mice
    • Lacronique V., Mignon A., Fabre M., Viollet B., Rouquet N., Molina T., et al. Bcl-2 protects from lethal hepatic apoptosis induced by an anti-Fas antibody in mice. Nat Med. 2:1996;80-86.
    • (1996) Nat Med , vol.2 , pp. 80-86
    • Lacronique, V.1    Mignon, A.2    Fabre, M.3    Viollet, B.4    Rouquet, N.5    Molina, T.6
  • 18
    • 0029976410 scopus 로고    scopus 로고
    • A bcl-2 transgene expressed in hepatocytes protects mice from fulminant liver destruction but not from rapid death induced by anti-Fas antibody injection
    • Rodriguez I., Matsuura K., Khatib K., Reed J.C., Nagata S., Vassalli P. A bcl-2 transgene expressed in hepatocytes protects mice from fulminant liver destruction but not from rapid death induced by anti-Fas antibody injection. J Exp Med. 183:1996;1031-1036.
    • (1996) J Exp Med , vol.183 , pp. 1031-1036
    • Rodriguez, I.1    Matsuura, K.2    Khatib, K.3    Reed, J.C.4    Nagata, S.5    Vassalli, P.6
  • 19
    • 0033607006 scopus 로고    scopus 로고
    • Bid-deficient mice are resistant to Fas-induced hepatocellular apoptosis
    • Yin X.M., Wang K., Gross A., Zhao Y., Zinkel S., Klocke B., et al. Bid-deficient mice are resistant to Fas-induced hepatocellular apoptosis. Nature. 400:1999;886-891.
    • (1999) Nature , vol.400 , pp. 886-891
    • Yin, X.M.1    Wang, K.2    Gross, A.3    Zhao, Y.4    Zinkel, S.5    Klocke, B.6
  • 20
    • 0028856130 scopus 로고
    • Targeted mutation in the Fas gene causes hyperplasia in peripheral lymphoid organs and liver
    • Adachi M., Suematsu S., Kondo T., Ogasawara J., Tanaka T., Yoshida N., et al. Targeted mutation in the Fas gene causes hyperplasia in peripheral lymphoid organs and liver. Nat Genet. 11:1995;294-300.
    • (1995) Nat Genet , vol.11 , pp. 294-300
    • Adachi, M.1    Suematsu, S.2    Kondo, T.3    Ogasawara, J.4    Tanaka, T.5    Yoshida, N.6
  • 21
    • 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., Holler N., Bodmer J.L., Hahne M., Frei K., Fontana A., et al. 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. 187:1998;1205-1213.
    • (1998) J Exp Med , vol.187 , pp. 1205-1213
    • Schneider, P.1    Holler, N.2    Bodmer, J.L.3    Hahne, M.4    Frei, K.5    Fontana, A.6
  • 24
    • 0033571453 scopus 로고    scopus 로고
    • Activation of caspases in lethal experimental hepatitis and prevention by acute phase proteins
    • Van Molle W., Denecker G., Rodriguez I., Brouckaert P., Vandenabeele P., Libert C. Activation of caspases in lethal experimental hepatitis and prevention by acute phase proteins. J Immunol. 163:1999;5235-5241.
    • (1999) J Immunol , vol.163 , pp. 5235-5241
    • Van Molle, W.1    Denecker, G.2    Rodriguez, I.3    Brouckaert, P.4    Vandenabeele, P.5    Libert, C.6
  • 25
    • 0032971161 scopus 로고    scopus 로고
    • Caspase-independent programmed cell death with necrotic morphology
    • Kitanaka C., Kuchino Y. Caspase-independent programmed cell death with necrotic morphology. Cell Death Differ. 6:1999;508-515.
    • (1999) Cell Death Differ , vol.6 , pp. 508-515
    • Kitanaka, C.1    Kuchino, Y.2
  • 26
    • 0031465443 scopus 로고    scopus 로고
    • Conversion of Bcl-2 to a Bax-like death effector by caspases
    • Cheng E.H., Kirsch D.G., Clem R.J., Ravi R., Kastan M.B., Bedi A., et al. Conversion of Bcl-2 to a Bax-like death effector by caspases. Science. 278:1997;1966-1968.
    • (1997) Science , vol.278 , pp. 1966-1968
    • Cheng, E.H.1    Kirsch, D.G.2    Clem, R.J.3    Ravi, R.4    Kastan, M.B.5    Bedi, A.6
  • 27
    • 0034676089 scopus 로고    scopus 로고
    • Cross-talk in cell death signaling
    • Roy S., Nicholson D.W. Cross-talk in cell death signaling. J Exp Med. 192:2000;F21-F25.
    • (2000) J Exp Med , vol.192
    • Roy, S.1    Nicholson, D.W.2
  • 28
    • 0031743125 scopus 로고    scopus 로고
    • A caspase-activated factor (CAF) induces mitochondrial membrane depolarization and cytochrome c release by a nonproteolytic mechanism
    • Steemans M., Goossens V., Van de Craen M., Van Herreweghe F., Vancompernolle K., De Vos K., et al. A caspase-activated factor (CAF) induces mitochondrial membrane depolarization and cytochrome c release by a nonproteolytic mechanism. J Exp Med. 188:1998;2193-2198.
    • (1998) J Exp Med , vol.188 , pp. 2193-2198
    • Steemans, M.1    Goossens, V.2    Van de Craen, M.3    Van Herreweghe, F.4    Vancompernolle, K.5    De Vos, K.6
  • 29
    • 0032583164 scopus 로고    scopus 로고
    • Caspase-independent cell killing by Fas-associated protein with death domain
    • Kawahara A., Ohsawa Y., Matsumura H., Uchiyama Y., Nagata S. Caspase-independent cell killing by Fas-associated protein with death domain. J Cell Biol. 143:1998;1353-1360.
    • (1998) J Cell Biol , vol.143 , pp. 1353-1360
    • Kawahara, A.1    Ohsawa, Y.2    Matsumura, H.3    Uchiyama, Y.4    Nagata, S.5
  • 31
    • 0034123026 scopus 로고    scopus 로고
    • Cleavage of BID during cytotoxic drug and UV radiation-induced apoptosis occurs downstream of the point of Bcl-2 action and is catalysed by caspase-3: A potential feedback loop for amplification of apoptosis-associated mitochondrial cytochrome c release
    • Slee E.A., Keogh S.A., Martin S.J. Cleavage of BID during cytotoxic drug and UV radiation-induced apoptosis occurs downstream of the point of Bcl-2 action and is catalysed by caspase-3: a potential feedback loop for amplification of apoptosis-associated mitochondrial cytochrome c release. Cell Death Differ. 7:2000;556-565.
    • (2000) Cell Death Differ , vol.7 , pp. 556-565
    • Slee, E.A.1    Keogh, S.A.2    Martin, S.J.3
  • 32
    • 0027362667 scopus 로고
    • Investigation of the subcellular distribution of the bcl-2 oncoprotein: Residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes
    • Krajewski S., Tanaka S., Takayama S., Schibler M.J., Fenton W., Reed J.C. Investigation of the subcellular distribution of the bcl-2 oncoprotein: residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes. Cancer Res. 53:1993;4701-4714.
    • (1993) Cancer Res , vol.53 , pp. 4701-4714
    • Krajewski, S.1    Tanaka, S.2    Takayama, S.3    Schibler, M.J.4    Fenton, W.5    Reed, J.C.6
  • 33
    • 0033939697 scopus 로고    scopus 로고
    • Selective localization of Bcl-2 to the inner mitochondrial and smooth endoplasmic reticulum membranes in mammalian cells
    • Gotow T., Shibata M., Kanamori S., Tokuno O., Ohsawa Y., Sato N., et al. Selective localization of Bcl-2 to the inner mitochondrial and smooth endoplasmic reticulum membranes in mammalian cells. Cell Death Differ. 7:2000;666-674.
    • (2000) Cell Death Differ , vol.7 , pp. 666-674
    • Gotow, T.1    Shibata, M.2    Kanamori, S.3    Tokuno, O.4    Ohsawa, Y.5    Sato, N.6
  • 34
    • 0036119432 scopus 로고    scopus 로고
    • A matrix-assisted laser desorption ionization post-source decay (MALDI-PSD) analysis of proteins released from isolated liver mitochondria treated with recombinant truncated Bid
    • Van Loo G., Demol H., van Gurp M., Hoorelbeke B., Schotte P., Beyaert R., et al. A matrix-assisted laser desorption ionization post-source decay (MALDI-PSD) analysis of proteins released from isolated liver mitochondria treated with recombinant truncated Bid. Cell Death Differ. 9:2002;301-308.
    • (2002) Cell Death Differ , vol.9 , pp. 301-308
    • Van Loo, G.1    Demol, H.2    Van Gurp, M.3    Hoorelbeke, B.4    Schotte, P.5    Beyaert, R.6


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