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Volumn 7, Issue 6, 1997, Pages 427-431

A matrix metalloproteinase inhibitor prevents processing of tumor necrosis factor α (TNFα) and abrogates endotoxin-induced lethality

Author keywords

[No Author keywords available]

Indexed keywords

DIPEPTIDE; ENDOTOXIN; ILOMASTAT; METALLOPROTEINASE; PROTEINASE INHIBITOR; TUMOR NECROSIS FACTOR ALPHA;

EID: 0031154408     PISSN: 10732322     EISSN: None     Source Type: Journal    
DOI: 10.1097/00024382-199706000-00007     Document Type: Article
Times cited : (77)

References (29)
  • 1
    • 0026717674 scopus 로고
    • The pathophysiology of tumor necrosis factors
    • Vassalli P: The pathophysiology of tumor necrosis factors. Annu Rev Immunol 10:411-452, 1992.
    • (1992) Annu Rev Immunol , vol.10 , pp. 411-452
    • Vassalli, P.1
  • 2
    • 0025284616 scopus 로고
    • The biologic characteristics of cytokines and their implication in surgical injury
    • Fong Y, Moldawer LL, Shires GT, and Lowry SF: The biologic characteristics of cytokines and their implication in surgical injury. Surg Gynecol Obstet 170:363-378, 1990.
    • (1990) Surg Gynecol Obstet , vol.170 , pp. 363-378
    • Fong, Y.1    Moldawer, L.L.2    Shires, G.T.3    Lowry, S.F.4
  • 3
    • 0025258906 scopus 로고
    • Requirement of endogenous tumor necrosis factor/cachectin for recovery from experimental peritonitis
    • Echtenacher B, Falk W, Mannel DN, Krammer PH: Requirement of endogenous tumor necrosis factor/cachectin for recovery from experimental peritonitis. J Immunol 145:3762-3766, 1990.
    • (1990) J Immunol , vol.145 , pp. 3762-3766
    • Echtenacher, B.1    Falk, W.2    Mannel, D.N.3    Krammer, P.H.4
  • 4
    • 0026436958 scopus 로고
    • Role of TNF in resistance to bacteria
    • Havell EA: Role of TNF in resistance to bacteria. Immunol Ser 56:341-363, 1992.
    • (1992) Immunol Ser , vol.56 , pp. 341-363
    • Havell, E.A.1
  • 6
    • 0024281428 scopus 로고
    • A novel form of TNF/cachectin is a cell surface cytotoxic transmembrane protein: Ramifications for the complex physiology of TNF
    • Kriegler M, Perez C, DeFay K, Albert I, Lu SD: A novel form of TNF/cachectin is a cell surface cytotoxic transmembrane protein: Ramifications for the complex physiology of TNF. Cell 53:45-53, 1988.
    • (1988) Cell , vol.53 , pp. 45-53
    • Kriegler, M.1    Perez, C.2    DeFay, K.3    Albert, I.4    Lu, S.D.5
  • 7
    • 0025149247 scopus 로고
    • A nonsecretable cell surface mutant of tumor necrosis factor (TNF) kills by cell-to-cell contact
    • Perez C, Albert I, DeFay K, Zachariades N, Gooding L, Kriegler M: A nonsecretable cell surface mutant of tumor necrosis factor (TNF) kills by cell-to-cell contact. Cell 63:251-258, 1990.
    • (1990) Cell , vol.63 , pp. 251-258
    • Perez, C.1    Albert, I.2    DeFay, K.3    Zachariades, N.4    Gooding, L.5    Kriegler, M.6
  • 8
    • 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 83:793-802, 1995.
    • (1995) Cell , vol.83 , pp. 793-802
    • Grell, M.1    Douni, E.2    Wajant, H.3
  • 9
    • 0028485654 scopus 로고
    • Processing of tumour necrosis factor-α precursor by metalloproteinases
    • Gearing AJH, Beckett P, Chrostodoulou M, et al: Processing of tumour necrosis factor-α precursor by metalloproteinases. Nature 370:555-557, 1994.
    • (1994) Nature , vol.370 , pp. 555-557
    • Gearing, A.J.H.1    Beckett, P.2    Chrostodoulou, M.3
  • 10
    • 0028483534 scopus 로고
    • Regulation of tumour necrosis factor-α processing by a metalloproteinase inhibitor
    • McGeehan GM, Becherer JD, Bast Jr RC, et al: Regulation of tumour necrosis factor-α processing by a metalloproteinase inhibitor. Nature 370:558-560, 1994.
    • (1994) Nature , vol.370 , pp. 558-560
    • McGeehan, G.M.1    Becherer, J.D.2    Bast Jr., R.C.3
  • 11
    • 0026768692 scopus 로고
    • Inhibition of human skin fibroblast collagenase, thermolysin, and Pseudomonas aeruginosa elastase by peptide hydroxamic acids
    • Grobelny D, Poncz L, Galardy RE: Inhibition of human skin fibroblast collagenase, thermolysin, and Pseudomonas aeruginosa elastase by peptide hydroxamic acids. Biochemistry 31:7152, 1991.
    • (1991) Biochemistry , vol.31 , pp. 7152
    • Grobelny, D.1    Poncz, L.2    Galardy, R.E.3
  • 12
    • 0026463072 scopus 로고
    • Treatment of alkali-injured rabbit corneas with a synthetic inhibitor of matrix metalloproteinases
    • Schultz GS, Strelow S, Stern GA, et al: Treatment of alkali-injured rabbit corneas with a synthetic inhibitor of matrix metalloproteinases. Invest Ophthalmol Vis Sci 33:3325-3331, 1992.
    • (1992) Invest Ophthalmol Vis Sci , vol.33 , pp. 3325-3331
    • Schultz, G.S.1    Strelow, S.2    Stern, G.A.3
  • 13
    • 0027944171 scopus 로고
    • Reversal of experimental autoimmune encephalomyelitis with a hydroxamate inhibitor of matrix metalloproteases
    • Gijbels K, Galardy R, Steinman L: Reversal of experimental autoimmune encephalomyelitis with a hydroxamate inhibitor of matrix metalloproteases. J Clin Invest 94:2177-2182, 1994.
    • (1994) J Clin Invest , vol.94 , pp. 2177-2182
    • Gijbels, K.1    Galardy, R.2    Steinman, L.3
  • 14
    • 27644454859 scopus 로고
    • A matrix metalloprotease inhibitor improves cardiovascular and hepatocellular function following hemorrhage and resuscitation
    • Wang P, Ba ZF, Galardy RE, Chaudry IH: A matrix metalloprotease inhibitor improves cardiovascular and hepatocellular function following hemorrhage and resuscitation. Shock 3(Suppl 2):35-36, 1995.
    • (1995) Shock , vol.3 , Issue.2 SUPPL. , pp. 35-36
    • Wang, P.1    Ba, Z.F.2    Galardy, R.E.3    Chaudry, I.H.4
  • 15
    • 0027516460 scopus 로고
    • Protective role of interleukin 6 in the lipopolysaccharide-galactosamine septic shock model
    • Barton BE, Jackson JV: Protective role of interleukin 6 in the lipopolysaccharide-galactosamine septic shock model. Infect Immun 61:1496-1499, 1993.
    • (1993) Infect Immun , vol.61 , pp. 1496-1499
    • Barton, B.E.1    Jackson, J.V.2
  • 16
    • 0022972464 scopus 로고
    • A highly sensitive cell line, WEHI 164 clone 13, for measuring cytotoxic factor/tumor necrosis factor from human monocytes
    • Espevik T, Nissen Meyer J: A highly sensitive cell line, WEHI 164 clone 13, for measuring cytotoxic factor/tumor necrosis factor from human monocytes. J Immunol Methods 95:99-105, 1986.
    • (1986) J Immunol Methods , vol.95 , pp. 99-105
    • Espevik, T.1    Nissen Meyer, J.2
  • 17
    • 0026741275 scopus 로고
    • Tumor necrosis factor soluble receptors circulate during experimental and clinical inflammation and can protect against excessive tumor necrosis factor alpha in vitro and in vivo
    • Van Zee KJ, Kohno T, Fischer E, Rock CS, Moldawer LL, Lowry SF: Tumor necrosis factor soluble receptors circulate during experimental and clinical inflammation and can protect against excessive tumor necrosis factor alpha in vitro and in vivo. Proc Natl Acad Sci USA 89:4845-4849, 1992.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 4845-4849
    • Van Zee, K.J.1    Kohno, T.2    Fischer, E.3    Rock, C.S.4    Moldawer, L.L.5    Lowry, S.F.6
  • 18
    • 0029922017 scopus 로고    scopus 로고
    • A genomic polymorphism within the tumor necrosis locus influences plasma tumor necrosis factor concentrations and outcome of patients with severe sepsis
    • Stuber F, Petersen M, Bokelmann F, Schade U: A genomic polymorphism within the tumor necrosis locus influences plasma tumor necrosis factor concentrations and outcome of patients with severe sepsis. Crit Care Med 24:381-384, 1996.
    • (1996) Crit Care Med , vol.24 , pp. 381-384
    • Stuber, F.1    Petersen, M.2    Bokelmann, F.3    Schade, U.4
  • 20
    • 0028287014 scopus 로고
    • Lipopolysaccharide LPS-mediated soluble TNF receptor release and TNF receptor expression by monocytes. Role of CD14, LPS binding protein, and bactericidal/permeability-increasing protein
    • Leeuwenberg JF, Dentener MA, Buurman WA: Lipopolysaccharide LPS-mediated soluble TNF receptor release and TNF receptor expression by monocytes. Role of CD14, LPS binding protein, and bactericidal/permeability-increasing protein. J Immunol 152:5070-5076, 1994.
    • (1994) J Immunol , vol.152 , pp. 5070-5076
    • Leeuwenberg, J.F.1    Dentener, M.A.2    Buurman, W.A.3
  • 21
    • 0028919856 scopus 로고
    • A metalloprotease inhibitor blocks shedding of the 80-kD TNF receptor and TNF processing in T lymphocytes
    • Crowe PD, Walter BN, Mohler KM, Otten Evans C, Black RA, Ware CF: A metalloprotease inhibitor blocks shedding of the 80-kD TNF receptor and TNF processing in T lymphocytes. J Exp Med 181:1205-1210, 1995.
    • (1995) J Exp Med , vol.181 , pp. 1205-1210
    • Crowe, P.D.1    Walter, B.N.2    Mohler, K.M.3    Otten Evans, C.4    Black, R.A.5    Ware, C.F.6
  • 22
    • 0028799113 scopus 로고
    • A metalloprotease inhibitor blocks shedding of the IL-6 receptor and the p 60 TNF receptor
    • Mullberg J, Durie FH, Otten Evans C, et al: A metalloprotease inhibitor blocks shedding of the IL-6 receptor and the p 60 TNF receptor. J Immunol 155:5198-5205, 1995.
    • (1995) J Immunol , vol.155 , pp. 5198-5205
    • Mullberg, J.1    Durie, F.H.2    Otten Evans, C.3
  • 23
    • 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, Lotscher 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 364:798-802, 1993.
    • (1993) Nature , vol.364 , pp. 798-802
    • Rothe, J.1    Lesslauer, W.2    Lotscher, H.3
  • 24
    • 0027196986 scopus 로고
    • Mechanisms of endotoxin shock and endotoxin hypersensitivity
    • Galanos C, Freudenberg MA: Mechanisms of endotoxin shock and endotoxin hypersensitivity. Immunobiology 187:346-356, 1993.
    • (1993) Immunobiology , vol.187 , pp. 346-356
    • Galanos, C.1    Freudenberg, M.A.2
  • 25
    • 0025903905 scopus 로고
    • Tumor necrosis factor alpha mediates lethal activity of killed Gram-negative and Gram-positive bacteria in D-galactosamine-treated mice
    • Freudenberg MA, Galanos C: Tumor necrosis factor alpha mediates lethal activity of killed Gram-negative and Gram-positive bacteria in D-galactosamine-treated mice. Infect Immun 59:2110-2115, 1991.
    • (1991) Infect Immun , vol.59 , pp. 2110-2115
    • Freudenberg, M.A.1    Galanos, C.2
  • 26
    • 0030638944 scopus 로고    scopus 로고
    • Involvement of 26 kD cell-associated TNF in experimental hepatitis and exacerbation of liver injury with a matrix metalloproteinase inhibitor
    • Solorzano CC, Ksontini R, Pruitt JH, et al: Involvement of 26 kD cell-associated TNF in experimental hepatitis and exacerbation of liver injury with a matrix metalloproteinase inhibitor. J Immunol 158:414-419, 1997.
    • (1997) J Immunol , vol.158 , pp. 414-419
    • Solorzano, C.C.1    Ksontini, R.2    Pruitt, J.H.3
  • 27
    • 0028203560 scopus 로고
    • A human tumor necrosis factor (TNF) α mutant that binds exclusively to the p 55 TNF receptor produces toxicity in the baboon
    • Van Zee KJ, Stackpole SA, Montegut WJ, et al: A human tumor necrosis factor (TNF) α mutant that binds exclusively to the p 55 TNF receptor produces toxicity in the baboon. J Exp Med 179:1185-1191, 1994.
    • (1994) J Exp Med , vol.179 , pp. 1185-1191
    • Van Zee, K.J.1    Stackpole, S.A.2    Montegut, W.J.3
  • 28
    • 0027512562 scopus 로고
    • Tumor necrosis factor alpha (TNF-alpha)-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 alpha (TNF-alpha)-induced cell adhesion to human endothelial cells is under dominant control of one TNF receptor type, TNF-R55. J Exp Med 177:1277-1286, 1993.
    • (1993) J Exp Med , vol.177 , pp. 1277-1286
    • Mackay, F.1    Loetscher, H.2    Stueber, D.3    Gehr, G.4    Lesslauer, W.5
  • 29
    • 0027521134 scopus 로고
    • Stimulation of human T-cell proliferation by specific activation of the 75-kDa tumor necrosis factor receptor
    • Tartaglia LA, Goeddel DV, Reynolds C, et al: Stimulation of human T-cell proliferation by specific activation of the 75-kDa tumor necrosis factor receptor. J Immunol 151:4637-4641, 1993.
    • (1993) J Immunol , vol.151 , pp. 4637-4641
    • Tartaglia, L.A.1    Goeddel, D.V.2    Reynolds, C.3


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