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Volumn 114, Issue 5, 1998, Pages 1035-1045

Concanavalin A-induced liver cell damage: Activation of intracellular pathways triggered by tumor necrosis factor in mice

Author keywords

[No Author keywords available]

Indexed keywords

CONCANAVALIN A; DNA FRAGMENT; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; PROTEIN KINASE; TUMOR NECROSIS FACTOR; TUMOR NECROSIS FACTOR ANTIBODY; TUMOR NECROSIS FACTOR RECEPTOR;

EID: 0031958385     PISSN: 00165085     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0016-5085(98)70324-5     Document Type: Article
Times cited : (135)

References (39)
  • 2
    • 0026643743 scopus 로고
    • A T cell-dependent experimental liver injury in mice inducible by concanavalin A
    • G Tiegs J Hentschel A Wendel A T cell-dependent experimental liver injury in mice inducible by concanavalin A J Clin Invest 90 1992 196 203
    • (1992) J Clin Invest , vol.90 , pp. 196-203
    • Tiegs, G1    Hentschel, J2    Wendel, A3
  • 3
    • 0028795171 scopus 로고
    • Concanavalin A-induced T-cell-mediated hepatic injury in mice: the role of tumor necrosis factor
    • F Gantner M Leist AW Lohse PG Germann A Tiegs Concanavalin A-induced T-cell-mediated hepatic injury in mice: the role of tumor necrosis factor Hepatology 21 1995 190 198
    • (1995) Hepatology , vol.21 , pp. 190-198
    • Gantner, F1    Leist, M2    Lohse, AW3    Germann, PG4    Tiegs, A5
  • 4
    • 0028895940 scopus 로고
    • Activation of the 55 kDa TNF receptor is necessary and sufficient for TNF-induced liver failure, hepatocyte apoptosis, and nitrite release
    • M Leist F Gantner S Jilg A Wendel Activation of the 55 kDa TNF receptor is necessary and sufficient for TNF-induced liver failure, hepatocyte apoptosis, and nitrite release J Immunol 154 1995 1307 1316
    • (1995) J Immunol , vol.154 , pp. 1307-1316
    • Leist, M1    Gantner, F2    Jilg, S3    Wendel, A4
  • 5
  • 6
    • 0028277663 scopus 로고
    • Unraveling function in the TNF ligand and receptor families
    • B Beutler C van Huffel Unraveling function in the TNF ligand and receptor families Science 264 1994 667 668
    • (1994) Science , vol.264 , pp. 667-668
    • Beutler, B1    van Huffel, C2
  • 7
    • 0029664821 scopus 로고    scopus 로고
    • p75NTR: a receptor after all
    • NTR: a receptor after all Science 272 1996 506 507
    • (1996) Science , vol.272 , pp. 506-507
    • Bothwell, M1
  • 8
    • 0030032106 scopus 로고    scopus 로고
    • TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways
    • H Hsu HB Shu MG Pan DV Goedell TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways Cell 84 1996 299 308
    • (1996) Cell , vol.84 , pp. 299-308
    • Hsu, H1    Shu, HB2    Pan, MG3    Goedell, DV4
  • 9
    • 0029967670 scopus 로고    scopus 로고
    • Systematic mutational analysis of the death domain of the tumor necrosis factor receptor 1-associated protein TRADD
    • A Park VR Baichwal Systematic mutational analysis of the death domain of the tumor necrosis factor receptor 1-associated protein TRADD J Biol Chem 271 1996 9858 9862
    • (1996) J Biol Chem , vol.271 , pp. 9858-9862
    • Park, A1    Baichwal, VR2
  • 11
    • 0030298294 scopus 로고    scopus 로고
    • Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-κB activation prevents cell death
    • Z-G Liu H Hsu DV Goeddel M Karin Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-κB activation prevents cell death Cell 87 1996 565 576
    • (1996) Cell , vol.87 , pp. 565-576
    • Liu, Z-G1    Hsu, H2    Goeddel, DV3    Karin, M4
  • 12
    • 85119817526 scopus 로고    scopus 로고
    • Hsu H, Huang J, Shu H-B, Baichwal V, Goedell DV. TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex. Immunity 199;4:387-396.
  • 13
    • 0028978626 scopus 로고
    • TRAF2 mediated activation of NF-κB by TNF receptor 2 and CD40
    • M Rothe V Sarma VM Dixit DV Goedell TRAF2 mediated activation of NF-κB by TNF receptor 2 and CD40 Science 269 1995 1424 1427
    • (1995) Science , vol.269 , pp. 1424-1427
    • Rothe, M1    Sarma, V2    Dixit, VM3    Goedell, DV4
  • 14
    • 0029786648 scopus 로고    scopus 로고
    • C/EBP-β/LAP controls downregulation of albumin gene transcription during liver regeneration
    • C Trautwein T Rakemann A Pietrangelo J Plümpe G Montosi MP Manns C/EBP-β/LAP controls downregulation of albumin gene transcription during liver regeneration J Biol Chem 271 1996 22262 22270
    • (1996) J Biol Chem , vol.271 , pp. 22262-22270
    • Trautwein, C1    Rakemann, T2    Pietrangelo, A3    Plümpe, J4    Montosi, G5    Manns, MP6
  • 15
    • 0029041670 scopus 로고
    • Transactivation of LAP/NF-IL6 is mediated by an acidic domain in the N-terminal part of the protein
    • C Trautwein D Walker J Plümpe MP Manns Transactivation of LAP/NF-IL6 is mediated by an acidic domain in the N-terminal part of the protein J Biol Chem 270 1995 15130 15136
    • (1995) J Biol Chem , vol.270 , pp. 15130-15136
    • Trautwein, C1    Walker, D2    Plümpe, J3    Manns, MP4
  • 16
    • 0027186357 scopus 로고
    • Transactivation by LAP/NF-IL6 is enhanced by phosphorylation of its activation domain
    • C Trautwein C Caelles P van der Geer T Hunter M Karin M Chojkier Transactivation by LAP/NF-IL6 is enhanced by phosphorylation of its activation domain Nature 364 1993 544 547
    • (1993) Nature , vol.364 , pp. 544-547
    • Trautwein, C1    Caelles, C2    van der Geer, P3    Hunter, T4    Karin, M5    Chojkier, M6
  • 17
    • 0027190740 scopus 로고
    • Lack of surface expression for the B-cell autoepitope of cytochrome P450 IID6 evidenced by flow cytometry
    • C Trautwein G Gerken H Löhr K-H Meyer zum Büschenfelde MP Manns Lack of surface expression for the B-cell autoepitope of cytochrome P450 IID6 evidenced by flow cytometry Z Gastroenterol 31 1993 225 230
    • (1993) Z Gastroenterol , vol.31 , pp. 225-230
    • Trautwein, C1    Gerken, G2    Löhr, H3    Meyer zum Büschenfelde, K-H4    Manns, MP5
  • 18
    • 0029165071 scopus 로고
    • Methods for analyzing c-Jun kinase
    • JK Westwick DA Brenner Methods for analyzing c-Jun kinase Methods Enzymol 255 1995 342 359
    • (1995) Methods Enzymol , vol.255 , pp. 342-359
    • Westwick, JK1    Brenner, DA2
  • 19
    • 0030041536 scopus 로고    scopus 로고
    • Persistent activation of c-Jun N-terminal kinase 1 (JNK1) in γ radiation-induced apoptosis
    • Y-R Chen CF Meyer TH Tan Persistent activation of c-Jun N-terminal kinase 1 (JNK1) in γ radiation-induced apoptosis J Biol Chem 271 1996 631 634
    • (1996) J Biol Chem , vol.271 , pp. 631-634
    • Chen, Y-R1    Meyer, CF2    Tan, TH3
  • 21
    • 0030038488 scopus 로고    scopus 로고
    • Fas ligation induces apoptosis and Jun kinase activation independently of CD45 and Lck in human T cells
    • KM Latinis GA Koretzky Fas ligation induces apoptosis and Jun kinase activation independently of CD45 and Lck in human T cells Blood 87 1996 871 875
    • (1996) Blood , vol.87 , pp. 871-875
    • Latinis, KM1    Koretzky, GA2
  • 22
    • 0029761702 scopus 로고    scopus 로고
    • Signal-transducing protein phosphorylation cascades mediated by Ras/Rho proteins in the mammalian cell: the potential for multiplex signalling
    • DT Denhardt Signal-transducing protein phosphorylation cascades mediated by Ras/Rho proteins in the mammalian cell: the potential for multiplex signalling Biochem J 318 1996 729 747
    • (1996) Biochem J , vol.318 , pp. 729-747
    • Denhardt, DT1
  • 23
    • 0026636883 scopus 로고
    • Control of transcription factor activity by protein phosphorylation
    • T Hunter M Karin Control of transcription factor activity by protein phosphorylation Cell 70 1992 375 387
    • (1992) Cell , vol.70 , pp. 375-387
    • Hunter, T1    Karin, M2
  • 24
    • 0024276523 scopus 로고
    • The jun proto-oncogene is positively autoregulated by its product, Jun/AP-1
    • P Angel K Hattori T Smeal M Karin The jun proto-oncogene is positively autoregulated by its product, Jun/AP-1 Cell 55 1988 875 885
    • (1988) Cell , vol.55 , pp. 875-885
    • Angel, P1    Hattori, K2    Smeal, T3    Karin, M4
  • 25
    • 0030017301 scopus 로고    scopus 로고
    • Interferon gamma plays a critical role in T cell-dependent liver injury in mice initiated by concanavalin A
    • S Küsters F Gantner G Künstle G Tiegs Interferon gamma plays a critical role in T cell-dependent liver injury in mice initiated by concanavalin A Gastroenterology 111 1996 462 471
    • (1996) Gastroenterology , vol.111 , pp. 462-471
    • Küsters, S1    Gantner, F2    Künstle, G3    Tiegs, G4
  • 26
    • 85119792049 scopus 로고    scopus 로고
    • The role of membrane-bound TNF in concanavalin A-induced T cell-dependent liver injury in mice (abstr)
    • S Küsters M Grell G Künstle G Kollias H Blüthmann G Tiegs The role of membrane-bound TNF in concanavalin A-induced T cell-dependent liver injury in mice (abstr) Arch Pharm 355 1997 R85
    • (1997) Arch Pharm , vol.355 , pp. R85
    • Küsters, S1    Grell, M2    Künstle, G3    Kollias, G4    Blüthmann, H5    Tiegs, G6
  • 28
    • 0028880006 scopus 로고
    • Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis
    • Z Xia M Dickens Raingeaud RJ Davis ME Greenberg Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis Science 270 1995 1326 1331
    • (1995) Science , vol.270 , pp. 1326-1331
    • Xia, Z1    Dickens, M2    Raingeaud3    Davis, RJ4    Greenberg, ME5
  • 31
    • 0029858387 scopus 로고    scopus 로고
    • TNF- and cancer therapy-induced apoptosis: potentiation by inhibition of NF-κB
    • CH Wang MW Mayo AS Baldwin TNF- and cancer therapy-induced apoptosis: potentiation by inhibition of NF-κB Science 274 1996 784 787
    • (1996) Science , vol.274 , pp. 784-787
    • Wang, CH1    Mayo, MW2    Baldwin, AS3
  • 32
    • 0029976817 scopus 로고    scopus 로고
    • An essential role for NF-κB in preventing TNF-α-induced cell death
    • AA Beg D Baltimore An essential role for NF-κB in preventing TNF-α-induced cell death Science 274 1996 782 784
    • (1996) Science , vol.274 , pp. 782-784
    • Beg, AA1    Baltimore, D2
  • 34
    • 0030098001 scopus 로고    scopus 로고
    • Liver regeneration 4: transcriptional control of liver regeneration
    • R Taub Liver regeneration 4: transcriptional control of liver regeneration FASEB J 10 1996 413 427
    • (1996) FASEB J , vol.10 , pp. 413-427
    • Taub, R1
  • 35
    • 0029059060 scopus 로고
    • Embryonic lethality and liver degeneration in mice lacking the RelA component of NF-kappa B
    • AA Beg WC Sha RT Bronson S Gosh D Baltimore Embryonic lethality and liver degeneration in mice lacking the RelA component of NF-kappa B Nature 376 1995 167 170
    • (1995) Nature , vol.376 , pp. 167-170
    • Beg, AA1    Sha, WC2    Bronson, RT3    Gosh, S4    Baltimore, D5
  • 36
    • 0029799912 scopus 로고    scopus 로고
    • Transcriptionally active Stat1 is required for the antiproliferative effects of both interferon α and interferon γ
    • JF Bromberg CM Horvath Z Wen RD Schreiber JE Darnell Transcriptionally active Stat1 is required for the antiproliferative effects of both interferon α and interferon γ Proc Natl Acad Sci 93 1996 7673 7678
    • (1996) Proc Natl Acad Sci , vol.93 , pp. 7673-7678
    • Bromberg, JF1    Horvath, CM2    Wen, Z3    Schreiber, RD4    Darnell, JE5
  • 38
    • 0028097822 scopus 로고
    • Purification and characterization of the Fasligand that induces apoptosis
    • T Suda S Nagata Purification and characterization of the Fasligand that induces apoptosis J Exp Med 179 1994 873 879
    • (1994) J Exp Med , vol.179 , pp. 873-879
    • Suda, T1    Nagata, S2
  • 39
    • 0029026548 scopus 로고
    • FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis
    • AM Chinnaiyan K O'Rourke M Tewari VM Dixit 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, AM1    O'Rourke, K2    Tewari, M3    Dixit, VM4


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