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Volumn 74, Issue 5, 1996, Pages 434-443

Tumour necrosis factor-alpha (TNF-α): The good, the bad and potentially very effective

Author keywords

Antineoplastic; Cytotoxicity; Inflammation; Receptors; Side effects; Signal transduction; TNF mutants

Indexed keywords

RECOMBINANT TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR RECEPTOR;

EID: 0029830209     PISSN: 08189641     EISSN: None     Source Type: Journal    
DOI: 10.1038/icb.1996.73     Document Type: Review
Times cited : (105)

References (107)
  • 1
    • 0000161413 scopus 로고
    • The treatment of malignant tumors by repeated inoculations of erysipelas: With a report of ten original cases
    • Coley WB. The treatment of malignant tumors by repeated inoculations of erysipelas: with a report of ten original cases. Am. J. Med. Sci. 1893; 105: 487-511.
    • (1893) Am. J. Med. Sci. , vol.105 , pp. 487-511
    • Coley, W.B.1
  • 3
    • 0021836738 scopus 로고
    • Purification of cachectin, a lipoprotein lipase-suppressing hormone secreted by endotoxin-induced RAW 264.7 cells
    • Beutler B, Mahoney J, Le Trang N, Pekala P, Cerami A. Purification of cachectin, a lipoprotein lipase-suppressing hormone secreted by endotoxin-induced RAW 264.7 cells. J. Exp. Med. 1985; 161: 984-95.
    • (1985) J. Exp. Med. , vol.161 , pp. 984-995
    • Beutler, B.1    Mahoney, J.2    Le Trang, N.3    Pekala, P.4    Cerami, A.5
  • 4
    • 0022371461 scopus 로고
    • Identity of tumour necrosis factor and the macrophage secreted factor cachectin
    • Beutler B, Greenwald D, Hulmes JD et al. Identity of tumour necrosis factor and the macrophage secreted factor cachectin. Nature 1985; 316: 552-4.
    • (1985) Nature , vol.316 , pp. 552-554
    • Beutler, B.1    Greenwald, D.2    Hulmes, J.D.3
  • 5
    • 0021681058 scopus 로고
    • Human tumour necrosis factor: Precursor structure, expression and homology to lymphotoxin
    • Pennica D, Nedwin GE, Hayflick JF et al. Human tumour necrosis factor: Precursor structure, expression and homology to lymphotoxin. Nature 1984; 312: 724-9.
    • (1984) Nature , vol.312 , pp. 724-729
    • Pennica, D.1    Nedwin, G.E.2    Hayflick, J.F.3
  • 7
    • 0027397580 scopus 로고
    • Association of tumor necrosis factor (TNF) and class II major histocompatibility complex alleles with the secretion of TNF-α an TNF-β by human mononuclear cells: A possible link to insulin-dependent diabetes mellitus
    • Pociot F, Briant L, Jongeneel CV et al. Association of tumor necrosis factor (TNF) and class II major histocompatibility complex alleles with the secretion of TNF-α an TNF-β by human mononuclear cells: A possible link to insulin-dependent diabetes mellitus. Eur. J. Immunol. 1993; 23: 224-31.
    • (1993) Eur. J. Immunol. , vol.23 , pp. 224-231
    • Pociot, F.1    Briant, L.2    Jongeneel, C.V.3
  • 8
    • 0028157286 scopus 로고
    • A genetic association between systemic lupus erythematosus and tumor necrosis factor alpha
    • Wilson AG, Gordon C, di Giovine FS et al. A genetic association between systemic lupus erythematosus and tumor necrosis factor alpha. Eur. J. Immunol. 1994; 24: 191-5.
    • (1994) Eur. J. Immunol. , vol.24 , pp. 191-195
    • Wilson, A.G.1    Gordon, C.2    Di Giovine, F.S.3
  • 10
    • 0028466705 scopus 로고
    • Protection against a lethal dose of endotoxin by an inhibitor of tumour necrosis factor processing
    • Mohler KM, Sleath PR, Fitzner JN et al. Protection against a lethal dose of endotoxin by an inhibitor of tumour necrosis factor processing. Nature 1994; 370: 218-20.
    • (1994) Nature , vol.370 , pp. 218-220
    • Mohler, K.M.1    Sleath, P.R.2    Fitzner, J.N.3
  • 11
    • 0024357657 scopus 로고
    • The structure of tumor necrosis factor-α at 2.6 Å resolution: Implications for receptor binding
    • Eck MJ, Sprang SR. The structure of tumor necrosis factor-α at 2.6 Å resolution: Implications for receptor binding. J. Biol. Chem. 1989; 264: 17 595-605.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17595-17605
    • Eck, M.J.1    Sprang, S.R.2
  • 12
  • 13
    • 0025179011 scopus 로고
    • Mutational analysis of structure-activity relationships in human tumour necrosis factor-alpha
    • Yamagishi J, Kawashima H, Matsuo N et al. Mutational analysis of structure-activity relationships in human tumour necrosis factor-alpha. Protein Engineering 1990; 3: 713-19.
    • (1990) Protein Engineering , vol.3 , pp. 713-719
    • Yamagishi, J.1    Kawashima, H.2    Matsuo, N.3
  • 14
    • 0026058148 scopus 로고
    • Localization of the active site of human tumour necrosis factor (hTNF) by mutational analysis
    • Van Ostade X, Tavernier J, Prangé T, Fiers W. Localization of the active site of human tumour necrosis factor (hTNF) by mutational analysis. EMBO. J. 1991; 10: 827-36.
    • (1991) EMBO. J. , vol.10 , pp. 827-836
    • Van Ostade, X.1    Tavernier, J.2    Prangé, T.3    Fiers, W.4
  • 15
    • 0024448122 scopus 로고
    • Two different cell types have different major receptors for human tumor necrosis factor (TNFα)
    • Hohmann H-P, Remy R, Brockhaus M, Van Loon APGM. Two different cell types have different major receptors for human tumor necrosis factor (TNFα). J. Biol. Chem. 1989; 264: 14927-34.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14927-14934
    • Hohmann, H.-P.1    Remy, R.2    Brockhaus, M.3    Van Loon, A.P.G.M.4
  • 17
    • 0025463156 scopus 로고
    • Two human TNF receptors have similar extracellular, but distinct intracellular, domain sequences
    • Dembic Z, Loetscher H, Gublcr U et al. Two human TNF receptors have similar extracellular, but distinct intracellular, domain sequences. Cytokine 1990; 2: 231-7.
    • (1990) Cytokine , vol.2 , pp. 231-237
    • Dembic, Z.1    Loetscher, H.2    Gublcr, U.3
  • 18
    • 0025269050 scopus 로고
    • Molecular cloning and expression of the human 55 kd tumor necrosis factor receptor
    • Loetscher H, Pan Y-CE, Lahm H-W et al. Molecular cloning and expression of the human 55 kd tumor necrosis factor receptor. Cell 1990; 61: 351-9.
    • (1990) Cell , vol.61 , pp. 351-359
    • Loetscher, H.1    Pan, Y.-C.E.2    Lahm, H.-W.3
  • 19
    • 0025711127 scopus 로고
    • Molecular cloning and expression of a receptor for human tumor necrosis factor
    • Schall TJ, Lewis M, Koller KJ et al. Molecular cloning and expression of a receptor for human tumor necrosis factor. Cell 1990; 61: 361-70.
    • (1990) Cell , vol.61 , pp. 361-370
    • Schall, T.J.1    Lewis, M.2    Koller, K.J.3
  • 20
    • 0025313006 scopus 로고
    • A receptor for tumor necrosis factor defines an unusual family of cellular and viral proteins
    • Smith CA, Davis T, Anderson D et al. A receptor for tumor necrosis factor defines an unusual family of cellular and viral proteins. Science 1990; 248: 1019-23.
    • (1990) Science , vol.248 , pp. 1019-1023
    • Smith, C.A.1    Davis, T.2    Anderson, D.3
  • 21
    • 0026056106 scopus 로고
    • Human neutrophil elastase releases a ligand-binding fragment from the 75-kDa tumor necrosis factor (TNF) receptor
    • Porteu F, Brockhaus M, Wallach D, Engelmann H, Nathan CF. Human neutrophil elastase releases a ligand-binding fragment from the 75-kDa tumor necrosis factor (TNF) receptor. J Biol. Chem. 1991; 266: 18 846-53.
    • (1991) J Biol. Chem. , vol.266 , pp. 18846-18853
    • Porteu, F.1    Brockhaus, M.2    Wallach, D.3    Engelmann, H.4    Nathan, C.F.5
  • 22
    • 0025609639 scopus 로고
    • Expression of the types a and B tumor necrosis factor (TNF) receptors is independently regulated, and both receptors mediate activation of the transcription factor NF-κB
    • Hohmann H-P, Brockhaus M, Baeuerle PA, Remy R, Kolbeck R, Van Loon APGM. Expression of the types A and B tumor necrosis factor (TNF) receptors is independently regulated, and both receptors mediate activation of the transcription factor NF-κB. J. Biol. Chem. 1990; 265: 22 409-17.
    • (1990) J. Biol. Chem. , vol.265 , pp. 22409-22417
    • Hohmann, H.-P.1    Brockhaus, M.2    Baeuerle, P.A.3    Remy, R.4    Kolbeck, R.5    Van Loon, A.P.G.M.6
  • 23
    • 0025167639 scopus 로고
    • Binding and regulation of cellular functions by monoclonal antibodies against human tumor necrosis factor receptors
    • Shalaby MR, Sundan A, Loetscher H, Brockhaus M, Lesslauer W, Espevik T. Binding and regulation of cellular functions by monoclonal antibodies against human tumor necrosis factor receptors. J. Exp. Med. 1990; 172: 1517-20.
    • (1990) J. Exp. Med. , vol.172 , pp. 1517-1520
    • Shalaby, M.R.1    Sundan, A.2    Loetscher, H.3    Brockhaus, M.4    Lesslauer, W.5    Espevik, T.6
  • 24
    • 0027512562 scopus 로고
    • Tumor necrosis factor α (TNF-α)-induced cell adhesion to human endothelial cells is under dominant control of one TNF receptor type, TNF-R55
    • Mackay F, Loetscher H, Stueber D, Gehr G, Lesslauer W. Tumor necrosis factor α (TNF-α)-induced cell adhesion to human endothelial cells is under dominant control of one TNF receptor type, TNF-R55. J. Exp. Med. 1993; 177: 1277-86.
    • (1993) J. Exp. Med. , vol.177 , pp. 1277-1286
    • Mackay, F.1    Loetscher, H.2    Stueber, D.3    Gehr, G.4    Lesslauer, W.5
  • 25
    • 0027732688 scopus 로고
    • Tumor necrosis factor activates human endothelial cells through the p55 tumor necrosis factor receptor but the p75 receptor contributes to activation at low tumor necrosis factor concentration
    • Slowik MR, De Luca LG, Fiers W, Pober JS. Tumor necrosis factor activates human endothelial cells through the p55 tumor necrosis factor receptor but the p75 receptor contributes to activation at low tumor necrosis factor concentration. Am. J. Pathol. 1993; 143: 1724-30.
    • (1993) Am. J. Pathol. , vol.143 , pp. 1724-1730
    • Slowik, M.R.1    De Luca, L.G.2    Fiers, W.3    Pober, J.S.4
  • 26
    • 0025756330 scopus 로고
    • Cloning and expression of cDNAs for two distinct murine tumor necrosis factor receptors demonstrate one receptor is species specific
    • Lewis M, Tartaglia LA, Lee A et al. Cloning and expression of cDNAs for two distinct murine tumor necrosis factor receptors demonstrate one receptor is species specific. Proc. Natl Acad. Sci. USA 1991; 88: 2830-4.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 2830-2834
    • Lewis, M.1    Tartaglia, L.A.2    Lee, A.3
  • 27
    • 0026757715 scopus 로고
    • Selective species specificity of tumour necrosis factor for toxicity in the mouse
    • Brouckaert P, Libert C, Everaerdt B, Fiers W. Selective species specificity of tumour necrosis factor for toxicity in the mouse. Lymphokine. Cytokine Res. 1992; 11: 193-6.
    • (1992) Lymphokine. Cytokine Res. , vol.11 , pp. 193-196
    • Brouckaert, P.1    Libert, C.2    Everaerdt, B.3    Fiers, W.4
  • 28
    • 0025082527 scopus 로고
    • Antibodies to a soluble form of a tumor necrosis factor (TNF) receptor have TNF-like activity
    • Engelmann H, Holtmann H, Brakebusch C et al. Antibodies to a soluble form of a tumor necrosis factor (TNF) receptor have TNF-like activity. J. Biol. Chem. 1990; 265: 14497-504.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14497-14504
    • Engelmann, H.1    Holtmann, H.2    Brakebusch, C.3
  • 29
    • 0345036008 scopus 로고
    • Recombinant 55-kDa tumor necrosis factor (TNF) receptor: Stoichiometry of binding to TNFα and TNFβ and inhibition of TNF activity
    • Loetscher H, Gentz R, Zulauf M et al. Recombinant 55-kDa tumor necrosis factor (TNF) receptor: Stoichiometry of binding to TNFα and TNFβ and inhibition of TNF activity. J. Biol. Chem. 1991; 266: 18 324-9.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18324-18329
    • Loetscher, H.1    Gentz, R.2    Zulauf, M.3
  • 30
    • 0026511772 scopus 로고
    • Characterization of a recombinant extracellular domain of the type 1 tumor necrosis factor receptor: Evidence for tumor necrosis factor-α induced receptor aggregation
    • Pennica D, Kohr WJ, Fendly BM et al. Characterization of a recombinant extracellular domain of the type 1 tumor necrosis factor receptor: Evidence for tumor necrosis factor-α induced receptor aggregation. Biochem. 1992; 31: 1134-41.
    • (1992) Biochem. , vol.31 , pp. 1134-1141
    • Pennica, D.1    Kohr, W.J.2    Fendly, B.M.3
  • 32
    • 0026768768 scopus 로고
    • Functional characterization of the human tumor necrosis factor receptor p75 in a transfected rat/mouse T cell hybridoma
    • Vandenabeele P, Declercq W, Vercammen D et al. Functional characterization of the human tumor necrosis factor receptor p75 in a transfected rat/mouse T cell hybridoma. J. Exp. Med. 1992; 176: 1015-24.
    • (1992) J. Exp. Med. , vol.176 , pp. 1015-1024
    • Vandenabeele, P.1    Declercq, W.2    Vercammen, D.3
  • 33
    • 84996060132 scopus 로고
    • Structural aspects of TNF binding to its receptors: Evidence for segregated complexes. 4th Int. TNF Congress (May 2-6, 1992; Veldhoven)
    • Loetscher H, Banner D, Brockhaus M et al. Structural aspects of TNF binding to its receptors: Evidence for segregated complexes. 4th Int. TNF Congress (May 2-6, 1992; Veldhoven). Eur. Cytokine Network 1992; 3: 136.
    • (1992) Eur. Cytokine Network , vol.3 , pp. 136
    • Loetscher, H.1    Banner, D.2    Brockhaus, M.3
  • 34
    • 0027211704 scopus 로고
    • Crystal structure of the soluble human 55 kd TNF receptor-human TNFβ complex: Implications for TNF receptor activation
    • Banner DW, D'Arcy A, Janes W et al. Crystal structure of the soluble human 55 kd TNF receptor-human TNFβ complex: Implications for TNF receptor activation. Cell 1993; 73:431-45.
    • (1993) Cell , vol.73 , pp. 431-445
    • Banner, D.W.1    D'Arcy, A.2    Janes, W.3
  • 35
    • 0028277663 scopus 로고
    • Unraveling function in the TNF ligand and receptor families
    • Beutler B, van Huffel C. Unraveling function in the TNF ligand and receptor families. Science 1994; 264: 667-8.
    • (1994) Science , vol.264 , pp. 667-668
    • Beutler, B.1    Van Huffel, C.2
  • 36
    • 0027982497 scopus 로고
    • A family of ligands for the TNF receptor superfamily
    • Cosman D. A family of ligands for the TNF receptor superfamily. Stem Cells 1994; 12: 440-55.
    • (1994) Stem Cells , vol.12 , pp. 440-455
    • Cosman, D.1
  • 37
    • 0028353492 scopus 로고
    • The TNF receptor superfamily of cellular and viral proteins: Activation, costimulation, and death
    • Smith CA, Farrah T, Goodwin RG. The TNF receptor superfamily of cellular and viral proteins: Activation, costimulation, and death. Cell 1994; 76: 959-62.
    • (1994) Cell , vol.76 , pp. 959-962
    • Smith, C.A.1    Farrah, T.2    Goodwin, R.G.3
  • 38
    • 0025816054 scopus 로고
    • T2 open reading frame from the Shope fibroma virus encodes a soluble form of the TNF receptor
    • Smith CA, Davis T, Wignall J et al. T2 open reading frame from the Shope fibroma virus encodes a soluble form of the TNF receptor. Biochem. Biophys. Res. Commun. 1991; 176: 335-42.
    • (1991) Biochem. Biophys. Res. Commun. , vol.176 , pp. 335-342
    • Smith, C.A.1    Davis, T.2    Wignall, J.3
  • 39
    • 0019389782 scopus 로고
    • Production of an antitumour cytotoxin by human monocytes
    • Matthews N. Production of an antitumour cytotoxin by human monocytes. Immunology 1981; 44: 135-42.
    • (1981) Immunology , vol.44 , pp. 135-142
    • Matthews, N.1
  • 40
    • 0026717674 scopus 로고
    • The pathophysiology of tumor necrosis factors
    • Vassalli P. The pathophysiology of tumor necrosis factors. Annu. Rev: Immunol. 1992; 10: 411-52.
    • (1992) Annu. Rev: Immunol. , vol.10 , pp. 411-452
    • Vassalli, P.1
  • 42
    • 0028244816 scopus 로고
    • Tumor necrosis factor: A pleiotropic cytokine and therapeutic target
    • Tracey KJ, Cerami A. Tumor necrosis factor: A pleiotropic cytokine and therapeutic target. Annu. Rew. Med. 1994; 45: 491-503.
    • (1994) Annu. Rew. Med. , vol.45 , pp. 491-503
    • Tracey, K.J.1    Cerami, A.2
  • 43
    • 0022382737 scopus 로고
    • Recombinant human tumor necrosis factor-α: Effects on proliferation of normal and transformed cells in vitro
    • Sugarman BJ, Aggarwal BB, Hass PE et al. Recombinant human tumor necrosis factor-α: Effects on proliferation of normal and transformed cells in vitro. Science 1985; 230: 943-5.
    • (1985) Science , vol.230 , pp. 943-945
    • Sugarman, B.J.1    Aggarwal, B.B.2    Hass, P.E.3
  • 44
    • 0022607023 scopus 로고
    • Fibroblast growth-enhancing activity of tumor necrosis factor and its relationship to other polypeptide growth factors
    • Vilcek J, Palombella VJ, Henriksen-DeStefano D et al Fibroblast growth-enhancing activity of tumor necrosis factor and its relationship to other polypeptide growth factors. J. Exp. Med. 1986; 163: 632-43.
    • (1986) J. Exp. Med. , vol.163 , pp. 632-643
    • Vilcek, J.1    Palombella, V.J.2    Henriksen-DeStefano, D.3
  • 45
    • 0022633381 scopus 로고
    • Recombinant tumour necrosis factor: Its effect and its synergism with interferon-γ on a variety of normal and transformed human cell lines
    • Fransen L, Van der Heyden J, Ruysschaert R, Fiers W. Recombinant tumour necrosis factor: Its effect and its synergism with interferon-γ on a variety of normal and transformed human cell lines. Eur. J. Cancer. Clin. Oncol. 1986; 22: 419-26.
    • (1986) Eur. J. Cancer. Clin. Oncol. , vol.22 , pp. 419-426
    • Fransen, L.1    Van Der Heyden, J.2    Ruysschaert, R.3    Fiers, W.4
  • 46
    • 0000070029 scopus 로고
    • Tumor necrosis factor
    • Pick (ed.) New York: Academic Press
    • Ruff MR, Gifford GE. Tumor necrosis factor. In: Pick (ed.) Lymphokines. Vol. 2. New York: Academic Press, 1981: 235-75.
    • (1981) Lymphokines , vol.2 , pp. 235-275
    • Ruff, M.R.1    Gifford, G.E.2
  • 47
    • 0023926860 scopus 로고
    • Sensitization and desensitization to lethal effects of tumor necrosis factor and IL-1
    • Wallach D, Holtmann H, Engelmann H, Nophar Y. Sensitization and desensitization to lethal effects of tumor necrosis factor and IL-1. J. Immunol. 1988; 140: 2994-9.
    • (1988) J. Immunol. , vol.140 , pp. 2994-2999
    • Wallach, D.1    Holtmann, H.2    Engelmann, H.3    Nophar, Y.4
  • 48
    • 0024428198 scopus 로고
    • Manganous Superoxide dismutase is essential for cellular resistance to cytotoxicity of tumor necrosis factor
    • Wong GHW. Elwell JH, Oberley LW, Goeddel DV. Manganous Superoxide dismutase is essential for cellular resistance to cytotoxicity of tumor necrosis factor. Cell 1989; 58: 923-31.
    • (1989) Cell , vol.58 , pp. 923-931
    • Wong, G.H.W.1    Elwell, J.H.2    Oberley, L.W.3    Goeddel, D.V.4
  • 49
    • 0022578633 scopus 로고
    • Stimulation of neutrophils by tumor necrosis factor
    • Klebanoff SJ, Vadas MA, Harlan JM et al. Stimulation of neutrophils by tumor necrosis factor. J. Immunol. 1986; 136: 4220-5.
    • (1986) J. Immunol. , vol.136 , pp. 4220-4225
    • Klebanoff, S.J.1    Vadas, M.A.2    Harlan, J.M.3
  • 50
    • 0023838743 scopus 로고
    • Recombinant human tumor necrosis factor-α: Regulation of N-formylmethionylleucylphenylalanine receptor affinity and function on human neutrophils
    • Atkinson YH, Marasco WA, Lopez AF, Vadas MA. Recombinant human tumor necrosis factor-α: Regulation of N-formylmethionylleucylphenylalanine receptor affinity and function on human neutrophils. J Clin. Invest. 1988; 81: 759-65.
    • (1988) J Clin. Invest. , vol.81 , pp. 759-765
    • Atkinson, Y.H.1    Marasco, W.A.2    Lopez, A.F.3    Vadas, M.A.4
  • 51
    • 0023609324 scopus 로고
    • Tumour necrosis factor/cachectin stimulates peritoneal macrophages, polymorphonuclear neutrophils, and vascular endothelial cells to synthesize and release platelet-activating factor
    • Camussi G, Bussolino F, Salvidio G, Baglioni C. Tumour necrosis factor/cachectin stimulates peritoneal macrophages, polymorphonuclear neutrophils, and vascular endothelial cells to synthesize and release platelet-activating factor. J. Exp. Med. 1987; 166: 1390-404.
    • (1987) J. Exp. Med. , vol.166 , pp. 1390-1404
    • Camussi, G.1    Bussolino, F.2    Salvidio, G.3    Baglioni, C.4
  • 52
    • 0025237812 scopus 로고
    • Human tumour necrosis factor-alpha (TNF-α) directly stimulates arachidonic acid release in human neutrophils
    • Atkinson YH, Murray AW, Krilis S, Vadas MA, Lopez AF. Human tumour necrosis factor-alpha (TNF-α) directly stimulates arachidonic acid release in human neutrophils. Immunology 1990; 70: 82-7.
    • (1990) Immunology , vol.70 , pp. 82-87
    • Atkinson, Y.H.1    Murray, A.W.2    Krilis, S.3    Vadas, M.A.4    Lopez, A.F.5
  • 54
    • 0142164496 scopus 로고
    • Stimulation of the adherence of neutrophils to umbilical vein endothelium by human recombinant tumor necrosis factor
    • Gamble JR, Harlan JM, Klebanoff SJ, Vadas MA. Stimulation of the adherence of neutrophils to umbilical vein endothelium by human recombinant tumor necrosis factor. Proc. Natl Acad. Sci. USA 1985; 82: 8667-71.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 8667-8671
    • Gamble, J.R.1    Harlan, J.M.2    Klebanoff, S.J.3    Vadas, M.A.4
  • 55
    • 0024601050 scopus 로고
    • Endothelial leukocyte adhesion molecule 1: An inducible receptor for neutrophils related to complement regulatory proteins and lectins
    • Bcvilacqua MP, Stengelin S, Gimbrone MA, Seed B. Endothelial leukocyte adhesion molecule 1: An inducible receptor for neutrophils related to complement regulatory proteins and lectins. Science 1989; 243: 1160-5.
    • (1989) Science , vol.243 , pp. 1160-1165
    • Bcvilacqua, M.P.1    Stengelin, S.2    Gimbrone, M.A.3    Seed, B.4
  • 56
    • 0024512985 scopus 로고
    • Endothelial cell gene expression of a neutrophil chemotactic factor by TNF-α. LPS and IL-1β
    • Stricter RM, Kunkel SL, Showell HJ et al. Endothelial cell gene expression of a neutrophil chemotactic factor by TNF-α. LPS and IL-1β. Science 1989; 243: 1467-9.
    • (1989) Science , vol.243 , pp. 1467-1469
    • Stricter, R.M.1    Kunkel, S.L.2    Showell, H.J.3
  • 57
    • 0026095304 scopus 로고
    • Regulation of transendothelial neutrophil migration by endogenous interleukin-8
    • Huber AR, Kunkel SL, Todd III RF, Weiss SJ. Regulation of transendothelial neutrophil migration by endogenous interleukin-8. Science 1991; 254: 99-102.
    • (1991) Science , vol.254 , pp. 99-102
    • Huber, A.R.1    Kunkel, S.L.2    Todd III., R.F.3    Weiss, S.J.4
  • 58
  • 59
    • 0026569208 scopus 로고
    • Neutrophil migration across monolayers of cytokine-prestimulated endothelial cells: A role for platelet-activating factor and IL-8
    • Kuijpers TW, Hakkert BC, Hart MHL, Roos D. Neutrophil migration across monolayers of cytokine-prestimulated endothelial cells: A role for platelet-activating factor and IL-8. J. Cell. Biol. 1992; 117: 565-72.
    • (1992) J. Cell. Biol. , vol.117 , pp. 565-572
    • Kuijpers, T.W.1    Hakkert, B.C.2    Hart, M.H.L.3    Roos, D.4
  • 60
    • 0024421453 scopus 로고
    • Ncutrophil-activating pcptide-1/interleukin 8. a novel cytokine that activates neutrophils
    • Baggiolini M, Walz A, Kunkcl SL. Ncutrophil-activating pcptide-1/interleukin 8. a novel cytokine that activates neutrophils. J. Clin. Invest. 1989; 84: 1045-9.
    • (1989) J. Clin. Invest. , vol.84 , pp. 1045-1049
    • Baggiolini, M.1    Walz, A.2    Kunkcl, S.L.3
  • 61
    • 0028333052 scopus 로고
    • Tumor necrosis factor receptor-mediated signaling pathways
    • Heller RA, Kronke M. Tumor necrosis factor receptor-mediated signaling pathways. J. Cell. Biol. 1994; 126: 5-9.
    • (1994) J. Cell. Biol. , vol.126 , pp. 5-9
    • Heller, R.A.1    Kronke, M.2
  • 63
    • 0027994349 scopus 로고
    • The sphingomyelin cycle and the second messenger function of ceramide
    • Hannun YA. The sphingomyelin cycle and the second messenger function of ceramide. J. Biol. Chem. 1994; 269: 3125-8.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3125-3128
    • Hannun, Y.A.1
  • 64
    • 0027968517 scopus 로고
    • Renaturation and tumor necrosis factor-α stimulation of a 97-kDa ceramide-activatcd protein kinase
    • Liu J, Mathias S, Yang Z, Kolesnick R. Renaturation and tumor necrosis factor-α stimulation of a 97-kDa ceramide-activatcd protein kinase. J. Biol. Chem. 1994; 269: 3047-52.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3047-3052
    • Liu, J.1    Mathias, S.2    Yang, Z.3    Kolesnick, R.4
  • 67
    • 0019961652 scopus 로고
    • How is the level of free arachidonic acid controlled in mammalian cells?
    • Irvine RF. How is the level of free arachidonic acid controlled in mammalian cells? Biochem. J. 1982; 204: 3-16.
    • (1982) Biochem. J. , vol.204 , pp. 3-16
    • Irvine, R.F.1
  • 68
    • 0022555858 scopus 로고
    • Platelet activating factor: A biologically active phosphoglyceride
    • Hanahan DJ. Platelet activating factor: A biologically active phosphoglyceride. Annu. Rev. Biochem. 1986; 55: 483-509.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 483-509
    • Hanahan, D.J.1
  • 69
    • 0028096691 scopus 로고
    • Physical and functional association of a serine-threonine protein kinase to the cytoplasmic domain of the p80 form of the human tumor necrosis factor receptor in human histiocytic lymphoma U-937 cells
    • Darnay BG, Reddy SAG, Aggarwal BB. Physical and functional association of a serine-threonine protein kinase to the cytoplasmic domain of the p80 form of the human tumor necrosis factor receptor in human histiocytic lymphoma U-937 cells. J. Biol. Chem. 1994; 269: 19 687-90.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19687-19690
    • Darnay, B.G.1    Reddy, S.A.G.2    Aggarwal, B.B.3
  • 70
    • 0028114055 scopus 로고
    • Identification of a protein kinase associated with the cytoplasmic domain of the p60 tumor necrosis factor receptor
    • Darnay BG, Reddy SAG, Aggarwal BB. Identification of a protein kinase associated with the cytoplasmic domain of the p60 tumor necrosis factor receptor. J. Biol. Chem. 1994; 269: 20 299-304.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20299-20304
    • Darnay, B.G.1    Sag, R.2    Aggarwal, B.B.3
  • 71
    • 0028871365 scopus 로고
    • Casein Kinase-1 phosphorylates the p75 tumor necrosis factor receptor and negatively regulates tumor necrosis factor signaling for apoptosis
    • Beyaert R, Vanhaesebroeck B, Declercq W et al. Casein Kinase-1 phosphorylates the p75 tumor necrosis factor receptor and negatively regulates tumor necrosis factor signaling for apoptosis. J. Biol. Chem. 1995; 270: 23 293-9.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23293-23299
    • Beyaert, R.1    Vanhaesebroeck, B.2    Declercq, W.3
  • 72
    • 0028124428 scopus 로고
    • A novel family of putative signal transducers associated with the cytoplasmic domain of the 75kDa tumor necrosis factor receptor
    • Rothc M, Wong SC, Henzel WJ, Goeddel DV. A novel family of putative signal transducers associated with the cytoplasmic domain of the 75kDa tumor necrosis factor receptor. Cell 1994; 78: 681-92.
    • (1994) Cell , vol.78 , pp. 681-692
    • Rothc, M.1    Wong, S.C.2    Henzel, W.J.3    Goeddel, D.V.4
  • 73
    • 0028954475 scopus 로고
    • Identification of a protein with homology to hsp90 that binds the type 1 tumor necrosis factor receptor
    • Song HY, Dunbar JD, Zhang YX, Guo D, Donner DB. Identification of a protein with homology to hsp90 that binds the type 1 tumor necrosis factor receptor. J. Biol. Chem. 1995: 270: 3574-81.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3574-3581
    • Song, H.Y.1    Dunbar, J.D.2    Zhang, Y.X.3    Guo, D.4    Donner, D.B.5
  • 74
    • 0029007855 scopus 로고
    • The TNF receptor 1-associated protein TRADD signals cell death and NF-κB activation
    • Hsu H, Xiong J, Goeddel DV. The TNF receptor 1-associated protein TRADD signals cell death and NF-κB activation. Cell 1995; 81: 495-504.
    • (1995) Cell , vol.81 , pp. 495-504
    • Hsu, H.1    Xiong, J.2    Goeddel, D.V.3
  • 75
    • 0029054725 scopus 로고
    • RIP: A novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death
    • Stanger BZ, Leder P., Lee T-H., Kim E, Seed B. RIP: A novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death. Cell 1995; 81: 513-23.
    • (1995) Cell , vol.81 , pp. 513-523
    • Stanger, B.Z.1    Leder, P.2    Lee, T.-H.3    Seed B, K.E.4
  • 76
    • 0024950718 scopus 로고
    • Tumour necrosis factor: Clinical relevance
    • Jones AL, Selby P. Tumour necrosis factor: Clinical relevance. Cancer Surveys 1989; 8: 817-36.
    • (1989) Cancer Surveys , vol.8 , pp. 817-836
    • Jones, A.L.1    Selby, P.2
  • 78
    • 0002133990 scopus 로고
    • Tumor necrosis factor: Clinical applications
    • DeVita Jr VT, Hellman S, Rosenberg SA (eds) Philadelphia: JB Lippincott Co.
    • Alexander RB, Rosenberg SA. Tumor necrosis factor: Clinical applications. In: DeVita Jr VT, Hellman S, Rosenberg SA (eds) The Biologic Therapy of Cancer Philadelphia: JB Lippincott Co., 1991; 378-92.
    • (1991) The Biologic Therapy of Cancer , pp. 378-392
    • Alexander, R.B.1    Rosenberg, S.A.2
  • 79
    • 0025963321 scopus 로고
    • Clinical studies with TNF
    • Taguchi T, Sohmura Y. Clinical studies with TNF. Biotherapy 1991; 3: 177-86.
    • (1991) Biotherapy , vol.3 , pp. 177-186
    • Taguchi, T.1    Sohmura, Y.2
  • 80
    • 0026444304 scopus 로고
    • Recombinant human TNF-α: Preclinical studies and results from early clinical trials
    • Aggarwal BB, Vilcek J (eds) New York: Marcel Dekker Inc
    • Saks S, Rosenblum M. Recombinant human TNF-α: Preclinical studies and results from early clinical trials. In: Aggarwal BB, Vilcek J (eds) Tumor Necrosis Factors: Structure, Function, and Mechanism of Action. New York: Marcel Dekker Inc, 1992; 567-87.
    • (1992) Tumor Necrosis Factors: Structure, Function, and Mechanism of Action , pp. 567-587
    • Saks, S.1    Rosenblum, M.2
  • 82
    • 0002834130 scopus 로고
    • Tumour necrosis factor
    • Sims E (ed.) Oxford: IRL press
    • Fiers W. Tumour necrosis factor. In: Sims E (ed.) The Natural Immune System: Humoral Factors Oxford: IRL press, 1993; 65-119.
    • (1993) The Natural Immune System: Humoral Factors , pp. 65-119
    • Fiers, W.1
  • 83
    • 0026531756 scopus 로고
    • High-dose recombinant tumor necrosis factor alpha in combination with interferon gamma and melphalan in isolation perfusion of the limbs for melanoma and sarcoma
    • Lienard D, Ewalenko P, Delmotte J-J, Renard N, Lejeune FJ. High-dose recombinant tumor necrosis factor alpha in combination with interferon gamma and melphalan in isolation perfusion of the limbs for melanoma and sarcoma. J. Clin. Oncol. 1992; 10: 52-60.
    • (1992) J. Clin. Oncol. , vol.10 , pp. 52-60
    • Lienard, D.1    Ewalenko, P.2    Delmotte, J.-J.3    Renard, N.4    Lejeune, F.J.5
  • 84
    • 0013601339 scopus 로고
    • The toxic effects of tumor necrosis factor in vivo and their prevention by cyclooxygenase inhibitors
    • Kettlehut IC, Fiers W, Goldberg AL. The toxic effects of tumor necrosis factor in vivo and their prevention by cyclooxygenase inhibitors. Proc. Natl Acad. Sci. USA 1987; 84: 4273-7.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 4273-4277
    • Kettlehut, I.C.1    Fiers, W.2    Goldberg, A.L.3
  • 85
    • 0025341034 scopus 로고
    • Manipulation of oxygen radical-scavenging capacity in mice alters host sensitivity to tumor necrosis factor toxicity but does not interfere with its antitumor efficacy
    • Hauser GJ, McIntosh JK, Travis WD, Rosenberg SA. Manipulation of oxygen radical-scavenging capacity in mice alters host sensitivity to tumor necrosis factor toxicity but does not interfere with its antitumor efficacy. Cancer Res. 1990; 50: 3503-8.
    • (1990) Cancer Res. , vol.50 , pp. 3503-3508
    • Hauser, G.J.1    McIntosh, J.K.2    Travis, W.D.3    Rosenberg, S.A.4
  • 86
    • 0023722960 scopus 로고
    • Effects of scavengers of oxygen-derived free radicals on mortality in endotoxin-challenged mice
    • Broner CW, Shenep JL, Stidham GL, Stokes DC, Hildner WK. Effects of scavengers of oxygen-derived free radicals on mortality in endotoxin-challenged mice. Crit. Care Med. 1988; 16: 848-51.
    • (1988) Crit. Care Med. , vol.16 , pp. 848-851
    • Broner, C.W.1    Shenep, J.L.2    Stidham, G.L.3    Stokes, D.C.4    Hildner, W.K.5
  • 87
    • 0023831176 scopus 로고
    • Preventive effects of severals chemicals against lethality of recombinant human tumor necrosis factor
    • Satomi N, Sakurai A, Haranaka R, Haranaka K. Preventive effects of severals chemicals against lethality of recombinant human tumor necrosis factor. J Biol. Resp. Modif. 1988; 7: 54-64.
    • (1988) J Biol. Resp. Modif. , vol.7 , pp. 54-64
    • Satomi, N.1    Sakurai, A.2    Haranaka, R.3    Haranaka, K.4
  • 88
    • 0023028369 scopus 로고
    • Shock and tissue injury induced by recombinant human cachectin
    • Tracey KJ, Beutler B, Lowry SF. Shock and tissue injury induced by recombinant human cachectin. Science 1986; 234: 470-4.
    • (1986) Science , vol.234 , pp. 470-474
    • Tracey, K.J.1    Beutler, B.2    Lowry, S.F.3
  • 90
    • 0027382150 scopus 로고
    • Human tumor necrosis factor α (TNFα) mutants with exclusive specificity for the 55-kDa or 75-kDa TNF receptors
    • Loetscher H, Stueber D, Banner D, Mackay F, Lesslauer W. Human tumor necrosis factor α (TNFα) mutants with exclusive specificity for the 55-kDa or 75-kDa TNF receptors. J. Biol. Chem. 1993; 268: 26350-7.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26350-26357
    • Loetscher, H.1    Stueber, D.2    Banner, D.3    Mackay, F.4    Lesslauer, W.5
  • 91
    • 0027392199 scopus 로고
    • Human TNF mutants with selective activity on the p55 receptor
    • Van Ostade X, Vandenabeele P, Everaerdt B et al. Human TNF mutants with selective activity on the p55 receptor. Nature 1993; 361: 266-9.
    • (1993) Nature , vol.361 , pp. 266-269
    • Van Ostade, X.1    Vandenabeele, P.2    Everaerdt, B.3
  • 92
    • 0028269860 scopus 로고
    • Human tumour necrosis factor mutants with preferential binding to and activity on either the R55 or R75 receptor
    • Van Ostade X, Vandenabeele P, Tavernier J, Fiers W. Human tumour necrosis factor mutants with preferential binding to and activity on either the R55 or R75 receptor. Eur. J. Biochem. 1994; 220: 771-9.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 771-779
    • Van Ostade, X.1    Vandenabeele, P.2    Tavernier, J.3    Fiers, W.4
  • 93
    • 0028176580 scopus 로고
    • Dissociation of TNF-α cytotoxic and proinflammatory activities by p55 receptor- and p75 receptor-selective TNF-α mutants
    • Barbara JAJ, Smith WB, Gamble JR et al. Dissociation of TNF-α cytotoxic and proinflammatory activities by p55 receptor- and p75 receptor-selective TNF-α mutants. EMBO J. 1994; 13: 843-50.
    • (1994) EMBO J. , vol.13 , pp. 843-850
    • Barbara, J.A.J.1    Smith, W.B.2    Gamble, J.R.3
  • 94
    • 0025098536 scopus 로고
    • Characterization of binding and biological effects of monoclonal antibodies against a human tumor necrosis receptor
    • Espevik T, Brockhaus M, Loetscher H, Nonstad U, Shalaby R. Characterization of binding and biological effects of monoclonal antibodies against a human tumor necrosis receptor. J. Exp. Med. 1990; 171: 415-26.
    • (1990) J. Exp. Med. , vol.171 , pp. 415-426
    • Espevik, T.1    Brockhaus, M.2    Loetscher, H.3    Nonstad, U.4    Shalaby, R.5
  • 95
    • 0025107818 scopus 로고
    • Identification of a 60-kD tumor necrosis factor (TNF) receptor as the major signal transducing component in TNF responses
    • Thoma B, Grell M, Pfizenmaier K, Scheurich P. Identification of a 60-kD tumor necrosis factor (TNF) receptor as the major signal transducing component in TNF responses. J. Exp. Med. 1990; 172: 1019-23.
    • (1990) J. Exp. Med. , vol.172 , pp. 1019-1023
    • Thoma, B.1    Grell, M.2    Pfizenmaier, K.3    Scheurich, P.4
  • 96
    • 0026563754 scopus 로고    scopus 로고
    • Cytoplasmic truncation of the p55 tumour necrosis factor (TNF) receptor abolishes signalling, but not induced shedding of the receptor
    • Brakebusch C, Nophar Y, Kemper O, Engelmann H, Wallach D. Cytoplasmic truncation of the p55 tumour necrosis factor (TNF) receptor abolishes signalling, but not induced shedding of the receptor. EMBO J. 11: 943-50.
    • EMBO J. , vol.11 , pp. 943-950
    • Brakebusch, C.1    Nophar, Y.2    Kemper, O.3    Engelmann, H.4    Wallach, D.5
  • 97
    • 0026744103 scopus 로고
    • Tumor necrosis factor receptor signaling: A dominant negative mutation suppresses the activation of the 55-kDa tumor necrosis factor receptor
    • Tartaglia LA, Goeddel DV. Tumor necrosis factor receptor signaling: A dominant negative mutation suppresses the activation of the 55-kDa tumor necrosis factor receptor. J. Biol. Chem. 1992; 267: 4304-7.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4304-4307
    • Tartaglia, L.A.1    Goeddel, D.V.2
  • 98
    • 0026751717 scopus 로고
    • The p70 tumor necrosis factor receptor mediates cytotoxicity
    • Heller RA, Song K, Fan N, Chang DJ. The p70 tumor necrosis factor receptor mediates cytotoxicity. Cell 1992; 70: 47-56.
    • (1992) Cell , vol.70 , pp. 47-56
    • Heller, R.A.1    Song, K.2    Fan, N.3    Chang, D.J.4
  • 99
    • 0028225351 scopus 로고
    • Evidence that tumor necrosis factor a (TNF)-induced activation of neutrophil respiratory burst on biologic surfaces is mediated by the p55 TNF receptor
    • Menegazzi R, Cramer R, Patriarca P, Scheurich P, Dri P. Evidence that tumor necrosis factor a (TNF)-induced activation of neutrophil respiratory burst on biologic surfaces is mediated by the p55 TNF receptor. Blood 1994; 84: 287-93.
    • (1994) Blood , vol.84 , pp. 287-293
    • Menegazzi, R.1    Cramer, R.2    Patriarca, P.3    Scheurich, P.4    Dri, P.5
  • 100
    • 0028143149 scopus 로고
    • Functional activities of receptors for tumor necrosis factor-α on human vascular endothelial cells
    • Paleolog EM. Delasalle S-AJ, Buurman WA, Feldmann M. Functional activities of receptors for tumor necrosis factor-α on human vascular endothelial cells. Blood 1994; 84: 2578-90.
    • (1994) Blood , vol.84 , pp. 2578-2590
    • Paleolog, E.M.1    Delasalle, S.-A.J.2    Buurman, W.A.3    Feldmann, M.4
  • 102
    • 0028866022 scopus 로고
    • The transmembrane form of tumor necrosis factor is the prime activating ligand of the 80 kDa tumor necrosis factor receptor
    • Grell M, Douni E, Wajant H et al. The transmembrane form of tumor necrosis factor is the prime activating ligand of the 80 kDa tumor necrosis factor receptor. Cell 1995; 83: 793-802.
    • (1995) Cell , vol.83 , pp. 793-802
    • Grell, M.1    Douni, E.2    Wajant, H.3
  • 103
    • 0027297663 scopus 로고
    • Mice deficient for the 55 kd tumor necrosis factor receptor are resistant to endotoxic shock, yet succumb to L. monocytogenes infection
    • Pfeffer K, Matsuyama T, Kündig TM et al. Mice deficient for the 55 kd tumor necrosis factor receptor are resistant to endotoxic shock, yet succumb to L. monocytogenes infection. Cell 1993; 73: 457-67.
    • (1993) Cell , vol.73 , pp. 457-467
    • Pfeffer, K.1    Matsuyama, T.2    Kündig, T.M.3
  • 104
    • 0027327619 scopus 로고
    • Mice lacking the tumour necrosis factor receptor 1 are resistant to TNF-mediated toxicity but highly susceptible to infection by Listeria monocytogenes
    • Rothe J, Lesslauer W, Lötscher H et al. Mice lacking the tumour necrosis factor receptor 1 are resistant to TNF-mediated toxicity but highly susceptible to infection by Listeria monocytogenes. Nature 1993; 364: 798-802.
    • (1993) Nature , vol.364 , pp. 798-802
    • Rothe, J.1    Lesslauer, W.2    Lötscher, H.3
  • 105
    • 0028063303 scopus 로고
    • Decreased sensitivity to tumour-necrosis factor but normal T-cell development in TNF receptor-2-deficient mice
    • Erickson SL, de Sauvage FJ, Kikly K et al. Decreased sensitivity to tumour-necrosis factor but normal T-cell development in TNF receptor-2-deficient mice. Nature 1994; 372: 560-3.
    • (1994) Nature , vol.372 , pp. 560-563
    • Erickson, S.L.1    De Sauvage, F.J.2    Kikly, K.3
  • 106
    • 0028203560 scopus 로고
    • A human tumor necrosis factor (TNF) a mutant that binds exclusively to the p55 TNF receptor produces toxicity in the baboon
    • Van Zee KJ, Stackpole SA, Montegut WJ et al. A human tumor necrosis factor (TNF) a mutant that binds exclusively to the p55 TNF receptor produces toxicity in the baboon. J. Exp. Med. 1994; 179: 1185-91.
    • (1994) J. Exp. Med. , vol.179 , pp. 1185-1191
    • Van Zee, K.J.1    Stackpole, S.A.2    Montegut, W.J.3
  • 107
    • 0027245985 scopus 로고
    • Influence of nephrectomy on tumor necrosis factor clearance in a murine model
    • Bemelmans MHA, Gouma DJ, Buurman WA. Influence of nephrectomy on tumor necrosis factor clearance in a murine model. J. Immunol. 1993; 150: 2007-17.
    • (1993) J. Immunol. , vol.150 , pp. 2007-2017
    • Bemelmans, M.H.A.1    Gouma, D.J.2    Buurman, W.A.3


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