메뉴 건너뛰기




Volumn 22, Issue 3, 1998, Pages 156-166

The role of cytokines in the catabolic consequences of infection and injury

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ADRENALIN; CATECHOLAMINE; CYTOKINE; GAMMA INTERFERON; GLUCOCORTICOID; GLUCOCORTICOID ANTAGONIST; GLUTAMINE; INSULIN; INTERLEUKIN 1; INTERLEUKIN 6; MIFEPRISTONE; SOMATOMEDIN; TUMOR NECROSIS FACTOR; UBIQUITIN;

EID: 0031945999     PISSN: 01486071     EISSN: None     Source Type: Journal    
DOI: 10.1177/0148607198022003156     Document Type: Review
Times cited : (151)

References (159)
  • 1
    • 0022411888 scopus 로고
    • Passive immunization against cachectin/tumor necrosis factor protects mice from lethal effects of endotoxin
    • Beutler B, Milsark IW, Cerami AC: Passive immunization against cachectin/tumor necrosis factor protects mice from lethal effects of endotoxin. Science 229:869-871, 1985
    • (1985) Science , vol.229 , pp. 869-871
    • Beutler, B.1    Milsark, I.W.2    Cerami, A.C.3
  • 2
    • 0023491364 scopus 로고
    • Anti-cachectin/TNF monoclonal antibodies prevent septic shock during lethal bacteremia
    • Tracey KJ, Hesse DG, Manogue KR, et al: Anti-cachectin/TNF monoclonal antibodies prevent septic shock during lethal bacteremia. Nature 330:662-664, 1987
    • (1987) Nature , vol.330 , pp. 662-664
    • Tracey, K.J.1    Hesse, D.G.2    Manogue, K.R.3
  • 3
    • 0025721017 scopus 로고
    • Protection against endotoxic shock by a tumor necrosis factor immunoadhesin
    • Ashkenazi A, Marsters SA, Capon DJ, et al: Protection against endotoxic shock by a tumor necrosis factor immunoadhesin. Proc Natl Acad Sci USA 88:10535-10539, 1991
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10535-10539
    • Ashkenazi, A.1    Marsters, S.A.2    Capon, D.J.3
  • 4
    • 0025943512 scopus 로고
    • Recombinant soluble tumor necrosis factor receptor proteins protect mice from lipopolysaccharide-induced lethality
    • Lesslauer W, Tabuchi H, Gentz R, et al: Recombinant soluble tumor necrosis factor receptor proteins protect mice from lipopolysaccharide-induced lethality. Eur J Immunol 21:2883-2886, 1991
    • (1991) Eur J Immunol , vol.21 , pp. 2883-2886
    • Lesslauer, W.1    Tabuchi, H.2    Gentz, R.3
  • 5
    • 0026596020 scopus 로고
    • T cell-mediated lethal shock triggered in mice by the superantigen staphylococcal enterotoxin B: Critical role of tumor necrosis factor
    • Miethke T, Wahl C, Heeg K, et al: T cell-mediated lethal shock triggered in mice by the superantigen staphylococcal enterotoxin B: Critical role of tumor necrosis factor. J Exp Med 175:91-98, 1992
    • (1992) J Exp Med , vol.175 , pp. 91-98
    • Miethke, T.1    Wahl, C.2    Heeg, K.3
  • 6
    • 0027327619 scopus 로고
    • Mice lacking the tumor 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 tumor 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    Lötscher, H.3
  • 7
    • 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 73:457-467, 1993
    • (1993) Cell , vol.73 , pp. 457-467
    • Pfeffer, K.1    Matsuyama, T.2    Kündig, T.M.3
  • 8
    • 0023638415 scopus 로고
    • Tumor secreting human TNFa/cachectin induce cachexia in mice
    • Oliff A, Defeo-Jones D, Boyer M, et al: Tumor secreting human TNFa/cachectin induce cachexia in mice. Cell 50:555-563, 1987
    • (1987) Cell , vol.50 , pp. 555-563
    • Oliff, A.1    Defeo-Jones, D.2    Boyer, M.3
  • 9
    • 0025639022 scopus 로고
    • Metabolic effects of cachectin/tumor necrosis factor are modified by site of production
    • Tracey KJ, Morgello S, Koplin B, et al: Metabolic effects of cachectin/tumor necrosis factor are modified by site of production. J Clin Invest 86:2014-2024, 1990
    • (1990) J Clin Invest , vol.86 , pp. 2014-2024
    • Tracey, K.J.1    Morgello, S.2    Koplin, B.3
  • 10
    • 0030011283 scopus 로고    scopus 로고
    • Tumor necrosis factor-α inhibits collagen α1(I) gene expression and wound healing in a murine model of cachexia
    • Buck M, Houglum K, Chojkier M: Tumor necrosis factor-α inhibits collagen α1(I) gene expression and wound healing in a murine model of cachexia. Am J Pathol 149:195-204, 1996
    • (1996) Am J Pathol , vol.149 , pp. 195-204
    • Buck, M.1    Houglum, K.2    Chojkier, M.3
  • 11
    • 0024547167 scopus 로고
    • Infusion of tumor necrosis factor/cachectin promotes muscle catabolism in the rat. A synergistic effect with interleukin 1
    • Flores EA, Bistrian BR, Pomposelli JJ, et al: Infusion of tumor necrosis factor/cachectin promotes muscle catabolism in the rat. A synergistic effect with interleukin 1. J Clin Invest 83:1614-1622, 1989
    • (1989) J Clin Invest , vol.83 , pp. 1614-1622
    • Flores, E.A.1    Bistrian, B.R.2    Pomposelli, J.J.3
  • 12
    • 0023947951 scopus 로고
    • 2 production in rat skeletal muscle in fever is signaled by a macrophage product distinct from interleukin 1 or other known monokines
    • 2 production in rat skeletal muscle in fever is signaled by a macrophage product distinct from interleukin 1 or other known monokines. J Clin Invest 81: 1378-1383, 1988
    • (1988) J Clin Invest , vol.81 , pp. 1378-1383
    • Goldberg, A.L.1    Kettelhut, I.C.2    Furuno, K.3
  • 13
    • 0025777448 scopus 로고
    • Interleukin-1 and interleukin-1 antagonism
    • Dinarello CE: Interleukin-1 and interleukin-1 antagonism. Blood 77:1627-1652, 1991
    • (1991) Blood , vol.77 , pp. 1627-1652
    • Dinarello, C.E.1
  • 14
    • 0025225333 scopus 로고
    • Interleukin-1 receptor antagonist reduces mortality from endotoxin shock
    • Ohlsson K, Björk P, Bergenfeldt M, et al: Interleukin-1 receptor antagonist reduces mortality from endotoxin shock. Nature 248:550-552, 1990
    • (1990) Nature , vol.248 , pp. 550-552
    • Ohlsson, K.1    Björk, P.2    Bergenfeldt, M.3
  • 15
    • 0025904893 scopus 로고
    • A recombinant human receptor antagonist to interleukin 1 improves survival after lethal endotoxemia in mice
    • Alexander RH, Doherty GM, Buresh CM, et al: A recombinant human receptor antagonist to interleukin 1 improves survival after lethal endotoxemia in mice. J Exp Med 173:1029-1032, 1991
    • (1991) J Exp Med , vol.173 , pp. 1029-1032
    • Alexander, R.H.1    Doherty, G.M.2    Buresh, C.M.3
  • 16
    • 0023146694 scopus 로고
    • Purified interleukin-1 (TL-1) from human monocytes stimulates acute-phase protein synthesis by rodent hepatocytes in vitro
    • Gauldie J, Sauder DN, McAdam KPWJ, et al: Purified interleukin-1 (TL-1) from human monocytes stimulates acute-phase protein synthesis by rodent hepatocytes in vitro. Immunology 60:203-207, 1987
    • (1987) Immunology , vol.60 , pp. 203-207
    • Gauldie, J.1    Sauder, D.N.2    McAdam, K.P.W.J.3
  • 17
    • 0023230528 scopus 로고
    • Interleukin 1 induces interleukin 1. II. Recombinant human interleukin 1 induces interleukin 1 production by adult human vascular endothelial cells
    • Warner SJC, Auger KR, Libby P: Interleukin 1 induces interleukin 1. II. Recombinant human interleukin 1 induces interleukin 1 production by adult human vascular endothelial cells. J Immunol 139:1911-1917, 1987
    • (1987) J Immunol , vol.139 , pp. 1911-1917
    • Warner, S.J.C.1    Auger, K.R.2    Libby, P.3
  • 18
    • 0022472749 scopus 로고
    • Tumor necrosis factor (cachectin) is an endogenous pyrogen and induces production of interleukin 1
    • Dinarello CA, Cannon JG, Wolff HA, et al: Tumor necrosis factor (cachectin) is an endogenous pyrogen and induces production of interleukin 1. J Exp Med 163:1433-1450, 1986
    • (1986) J Exp Med , vol.163 , pp. 1433-1450
    • Dinarello, C.A.1    Cannon, J.G.2    Wolff, H.A.3
  • 19
    • 0022982147 scopus 로고
    • γ interferon enhances macrophage transcription of the tumor necrosis factor/cachectin, interleukin 1 and urokinase genes which are controlled by short-lived repressors
    • Collait MA, Belin D, Vassalli J-D, et al: γ interferon enhances macrophage transcription of the tumor necrosis factor/cachectin, interleukin 1 and urokinase genes which are controlled by short-lived repressors. J Exp Med 164:2113-2118, 1986
    • (1986) J Exp Med , vol.164 , pp. 2113-2118
    • Collait, M.A.1    Belin, D.2    Vassalli, J.-D.3
  • 20
    • 0024353592 scopus 로고
    • Spontaneous and LPS-stimulated production of intracellular IL-1βby sinovial macrophages in rheumatoid arthritis is inhibited by IFN-γ
    • Ruschen S, Lemm G, Warnatz H: Spontaneous and LPS-stimulated production of intracellular IL-1βby sinovial macrophages in rheumatoid arthritis is inhibited by IFN-γ. Clin Exp Immunol 76:246-251, 1989
    • (1989) Clin Exp Immunol , vol.76 , pp. 246-251
    • Ruschen, S.1    Lemm, G.2    Warnatz, H.3
  • 21
    • 0023719001 scopus 로고
    • IL-1 induces IL-1. III. Specific inhibition of IL-1 production by IFN-γ
    • Ghezzi P, Dinarello CA-IL-1 induces IL-1. III. Specific inhibition of IL-1 production by IFN-γ. J Immunol 140:4238-4244, 1988
    • (1988) J Immunol , vol.140 , pp. 4238-4244
    • Ghezzi, P.1    Dinarello, C.A.2
  • 22
    • 0023574619 scopus 로고
    • Glucocorticoids inhibit transcriptional and post-transcriptional expression of interleukin-1 in U937 cells
    • Knudsen PJ, Dinarello CA, Strom TB: Glucocorticoids inhibit transcriptional and post-transcriptional expression of interleukin-1 in U937 cells. J Immunol 139:4129-4134, 1987
    • (1987) J Immunol , vol.139 , pp. 4129-4134
    • Knudsen, P.J.1    Dinarello, C.A.2    Strom, T.B.3
  • 23
    • 0022973486 scopus 로고
    • Prostaglandins inhibit posttranscriptional interleukin-1 synthesis by increasing intracellular cyclic adenosine monophosphate
    • Knudsen PJ, Dinarello CA, Strom TB: Prostaglandins inhibit posttranscriptional interleukin-1 synthesis by increasing intracellular cyclic adenosine monophosphate. J Immunol 137: 3189-3194, 1984
    • (1984) J Immunol , vol.137 , pp. 3189-3194
    • Knudsen, P.J.1    Dinarello, C.A.2    Strom, T.B.3
  • 24
    • 0020678196 scopus 로고
    • Stimulation of muscle protein degradation and prostaglandin E, release by leukocytic pyrogen (interleukin-1): A mechanism for the increased degradation of muscle protein during fever
    • Baracos V, Rodemann HP, Dinarello C A, et al: Stimulation of muscle protein degradation and prostaglandin E, release by leukocytic pyrogen (interleukin-1): A mechanism for the increased degradation of muscle protein during fever. New Engl J Med 308:553-558, 1983
    • (1983) New Engl J Med , vol.308 , pp. 553-558
    • Baracos, V.1    Rodemann, H.P.2    Dinarello, C.A.3
  • 25
    • 0026793224 scopus 로고
    • Muscle protein breakdown during endotoxemia in rats after treatment with interleukin-1 receptor antagonist (IL-1ra)
    • Zamir O, Hasselgren PO, O'Brien W, et al: Muscle protein breakdown during endotoxemia in rats after treatment with interleukin-1 receptor antagonist (IL-1ra). Ann Surg 216:381-387, 1992
    • (1992) Ann Surg , vol.216 , pp. 381-387
    • Zamir, O.1    Hasselgren, P.O.2    O'Brien, W.3
  • 26
    • 0027421831 scopus 로고
    • Interleukin-6 in biology and medicine
    • Akira S, Taga T, Kishimoto T: Interleukin-6 in biology and medicine. Adv Immunol 54:1-78, 1993
    • (1993) Adv Immunol , vol.54 , pp. 1-78
    • Akira, S.1    Taga, T.2    Kishimoto, T.3
  • 28
    • 0028328436 scopus 로고
    • Impaired immune and acute-phase responses in interleukin-6-deficient mice
    • Kopf M, Baumman H, Freer G, et al: Impaired immune and acute-phase responses in interleukin-6-deficient mice. Nature 368:339-342, 1992
    • (1992) Nature , vol.368 , pp. 339-342
    • Kopf, M.1    Baumman, H.2    Freer, G.3
  • 29
    • 0023676538 scopus 로고
    • Interleukin-6 stimulates the secretion of adrenocorticotropic hormone in conscious moving rats
    • Naitoh Y, Fukata J, Tominaga T, et al: Interleukin-6 stimulates the secretion of adrenocorticotropic hormone in conscious moving rats. Biochem Biophys Res Commun 155:1459-1463, 1988
    • (1988) Biochem Biophys Res Commun , vol.155 , pp. 1459-1463
    • Naitoh, Y.1    Fukata, J.2    Tominaga, T.3
  • 30
    • 0026464718 scopus 로고
    • Functional inhibition of hematopoietic and neurotrophic cytokines by blocking the interleukin 6 signal transducer gp130
    • Taga T, Narazaki M, Yasukawa K, et al: Functional inhibition of hematopoietic and neurotrophic cytokines by blocking the interleukin 6 signal transducer gp130. Proc Natl Acad Sci USA 89:10988-11001, 1992
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10988-11001
    • Taga, T.1    Narazaki, M.2    Yasukawa, K.3
  • 31
    • 0027731546 scopus 로고
    • Plasma cytokine and endotoxin levels correlate with survival in patients with the sepsis syndrome
    • Casey LC, Balk RA, Bone RC: Plasma cytokine and endotoxin levels correlate with survival in patients with the sepsis syndrome. Ann Intern Med 119:771-778, 1993
    • (1993) Ann Intern Med , vol.119 , pp. 771-778
    • Casey, L.C.1    Balk, R.A.2    Bone, R.C.3
  • 32
    • 0026689535 scopus 로고
    • Evidence for the involvement of interleukin 6 in experimental cancer cachexia
    • Strassman G, Fong M, Kenney JS, et al: Evidence for the involvement of interleukin 6 in experimental cancer cachexia. J Clin Invest 89:1681-1684, 1992
    • (1992) J Clin Invest , vol.89 , pp. 1681-1684
    • Strassman, G.1    Fong, M.2    Kenney, J.S.3
  • 33
    • 0027165260 scopus 로고
    • Cachexia and the acute-phase protein response in inflammation are regulated by interleukin-6
    • Oldenburg HS, Rogy MA, Lazarus DD, et al: Cachexia and the acute-phase protein response in inflammation are regulated by interleukin-6. Eur J Immunol 23:1889-1894, 1993
    • (1993) Eur J Immunol , vol.23 , pp. 1889-1894
    • Oldenburg, H.S.1    Rogy, M.A.2    Lazarus, D.D.3
  • 34
    • 0024373591 scopus 로고
    • Circulating interleukin-6 during a continuous infusion of tumor necrosis factor and interferon-γ
    • Brouckaert P, Spriggs DR, Demetri G, et al: Circulating interleukin-6 during a continuous infusion of tumor necrosis factor and interferon-γ. J Exp Med 169:2257-2262, 1989
    • (1989) J Exp Med , vol.169 , pp. 2257-2262
    • Brouckaert, P.1    Spriggs, D.R.2    Demetri, G.3
  • 35
    • 0024476714 scopus 로고
    • IL-6/IFN-β-2 as a circulating hormone. Induction by cytokine administration in humans
    • Jablons DM, Mule JJ, McIntosh JK, et al: IL-6/IFN-β-2 as a circulating hormone. Induction by cytokine administration in humans. J Immunol 142:1542-1547, 1989
    • (1989) J Immunol , vol.142 , pp. 1542-1547
    • Jablons, D.M.1    Mule, J.J.2    McIntosh, J.K.3
  • 36
    • 0027411525 scopus 로고
    • The molecular cell biology of interferon-γ and its receptor
    • Farrar MA, Schreiber RD: The molecular cell biology of interferon-γ and its receptor. Annu Rev Immunol 11:571-611, 1993
    • (1993) Annu Rev Immunol , vol.11 , pp. 571-611
    • Farrar, M.A.1    Schreiber, R.D.2
  • 37
    • 0017844472 scopus 로고
    • The genetic mapping of a defective LPS response gene in C3H/HeJ mice
    • Watson J, Kelly K, Largen M, et al: The genetic mapping of a defective LPS response gene in C3H/HeJ mice. J Immunol 120:422-424, 1978
    • (1978) J Immunol , vol.120 , pp. 422-424
    • Watson, J.1    Kelly, K.2    Largen, M.3
  • 38
    • 0018204171 scopus 로고
    • Genetic basis for unresponsiveness to lipopolysaccharide in C57BL/10Cr mice
    • Coutinho A, Meo T: Genetic basis for unresponsiveness to lipopolysaccharide in C57BL/10Cr mice. Immunogenetics 7:17-24, 1978
    • (1978) Immunogenetics , vol.7 , pp. 17-24
    • Coutinho, A.1    Meo, T.2
  • 39
    • 7144255953 scopus 로고
    • Interferon-gamma, a mediator of infection-induced sensitization towards endotoxin
    • Dosen J, Alvarez CR, Munford RS, et al (eds). Excerpta Medica, Amsterdam
    • Freudenberg MA, Katschinski T, Kumazawa Y, et al: Interferon-gamma, a mediator of infection-induced sensitization towards endotoxin. IN Bacterial Endotoxins: Recognition and Effector Mechanisms, Dosen J, Alvarez CR, Munford RS, et al (eds). Excerpta Medica, Amsterdam, 1993, pp 197-209
    • (1993) Bacterial Endotoxins: Recognition and Effector Mechanisms , pp. 197-209
    • Freudenberg, M.A.1    Katschinski, T.2    Kumazawa, Y.3
  • 40
    • 0026716499 scopus 로고
    • Gamma interferon mediates Propionibacterium acnes-induced hypersensitivity to lipopolysaccharide in mice
    • Katschinski T, Galanos C, Coumbos A, et al: Gamma interferon mediates Propionibacterium acnes-induced hypersensitivity to lipopolysaccharide in mice. Infect Immun 60:1994-2001, 1992
    • (1992) Infect Immun , vol.60 , pp. 1994-2001
    • Katschinski, T.1    Galanos, C.2    Coumbos, A.3
  • 41
    • 0025904702 scopus 로고
    • Regulation of gamma interferon production by natural killer cells in scid mice: Roles of tumor necrosis factor and bacterial stimuli
    • Wherry JC, Schreiber RD, Unanue ER: Regulation of gamma interferon production by natural killer cells in scid mice: Roles of tumor necrosis factor and bacterial stimuli. Infect Immun 59:1709-1715, 1991
    • (1991) Infect Immun , vol.59 , pp. 1709-1715
    • Wherry, J.C.1    Schreiber, R.D.2    Unanue, E.R.3
  • 42
    • 0028918544 scopus 로고
    • Interferon, a cofactor in the Interferon γ production induced by Gram-negative bacteria in mice
    • Yaegashi Y, Nielsen P, Sing A, et al: Interferon, a cofactor in the Interferon γ production induced by Gram-negative bacteria in mice. J Exp Med 181:953-960, 1995
    • (1995) J Exp Med , vol.181 , pp. 953-960
    • Yaegashi, Y.1    Nielsen, P.2    Sing, A.3
  • 43
    • 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
  • 44
    • 0026050286 scopus 로고
    • Gamma Interferon production in endotoxin-responder and non-responder mice during infection
    • Freudenberg MA, Kumazawa Y, Meding S, et al: Gamma Interferon production in endotoxin-responder and non-responder mice during infection. Infect Immun 59:3484-3491, 1991
    • (1991) Infect Immun , vol.59 , pp. 3484-3491
    • Freudenberg, M.A.1    Kumazawa, Y.2    Meding, S.3
  • 45
    • 0025134961 scopus 로고
    • The role of IFN-γ in the pathology of experimental endotoxemia
    • Heinzel FP: The role of IFN-γ in the pathology of experimental endotoxemia. J Immunol 145:2920-2924, 1990
    • (1990) J Immunol , vol.145 , pp. 2920-2924
    • Heinzel, F.P.1
  • 46
    • 0026661026 scopus 로고
    • Evidence for IFN-γ as a mediator of the lethality of endotoxin and tumor necrosis factor-α
    • Doherty GM, Lange JR, Langstem HN, et al: Evidence for IFN-γ as a mediator of the lethality of endotoxin and tumor necrosis factor-α. J Immunol 149:1666-1670, 1992
    • (1992) J Immunol , vol.149 , pp. 1666-1670
    • Doherty, G.M.1    Lange, J.R.2    Langstem, H.N.3
  • 47
    • 0028724185 scopus 로고
    • Participation of IFN-γ in the pathogenesis of LPS lethality
    • Bucklin SE, Russell SW, Morrison DC: Participation of IFN-γ in the pathogenesis of LPS lethality. Prog Clin Biol Res 338:399-406, 1994
    • (1994) Prog Clin Biol Res , vol.338 , pp. 399-406
    • Bucklin, S.E.1    Russell, S.W.2    Morrison, D.C.3
  • 48
    • 0027177874 scopus 로고
    • IFN-γ involvement in the severity of gram-negative infections in mice
    • Kohler J, Heumann D, Garotta G, et al: IFN-γ involvement in the severity of gram-negative infections in mice. J Immunol 151:916-921, 1993
    • (1993) J Immunol , vol.151 , pp. 916-921
    • Kohler, J.1    Heumann, D.2    Garotta, G.3
  • 49
    • 0026627926 scopus 로고
    • Role of interferon-γ in experimental Gram-negative sepsis
    • Silva AT, Cohen J: Role of interferon-γ in experimental Gram-negative sepsis. J Infect Dis 166:331-335, 1992
    • (1992) J Infect Dis , vol.166 , pp. 331-335
    • Silva, A.T.1    Cohen, J.2
  • 50
    • 0025365576 scopus 로고
    • Interferon-γ, a mediator of lethal lipopolysaccharide-induced Schwartzman-like shock reactions in mice
    • Heremans H, Van Damme J, Dillen C, et al: Interferon-γ, a mediator of lethal lipopolysaccharide-induced Schwartzman-like shock reactions in mice. J Exp Med 171:1853-1869, 1990
    • (1990) J Exp Med , vol.171 , pp. 1853-1869
    • Heremans, H.1    Van Damme, J.2    Dillen, C.3
  • 51
    • 0027291984 scopus 로고
    • Modification of the anti-CD3-induced cytokine release syndrome by anti-interferon-γ or anti-interleukin-6 antibody treatment protective effects and biphasic changes in blood cytokine levels
    • Matthys P, Dillen C, Proost P, et al: Modification of the anti-CD3-induced cytokine release syndrome by anti-interferon-γ or anti-interleukin-6 antibody treatment protective effects and biphasic changes in blood cytokine levels. Eur J Immunol 23:2209-2216, 1993
    • (1993) Eur J Immunol , vol.23 , pp. 2209-2216
    • Matthys, P.1    Dillen, C.2    Proost, P.3
  • 52
    • 0028222122 scopus 로고
    • Interferon γ receptor deficient mice are resistant to endotoxic shock
    • Car BD, Eng VM, Schyder B, et al: Interferon γ receptor deficient mice are resistant to endotoxic shock. J Exp Med 179:1437-1444, 1994
    • (1994) J Exp Med , vol.179 , pp. 1437-1444
    • Car, B.D.1    Eng, V.M.2    Schyder, B.3
  • 53
    • 0027260588 scopus 로고
    • Mice that lack the interferon-γ receptor have profoundly altered responses to infection with bacillus Calmette-Guerin and subsequent challenge with lipopolysaccharide
    • Kamijo R, Le J, Shapiro D, et al: Mice that lack the interferon-γ receptor have profoundly altered responses to infection with bacillus Calmette-Guerin and subsequent challenge with lipopolysaccharide. J Exp Med 178:1435-1440, 1993
    • (1993) J Exp Med , vol.178 , pp. 1435-1440
    • Kamijo, R.1    Le, J.2    Shapiro, D.3
  • 54
    • 0027464928 scopus 로고
    • Immune response in mice that lack the interferon-γ receptor
    • Huang S, Hendricks W, Althage A, et al: Immune response in mice that lack the interferon-γ receptor. Science 259:1742-1745, 1993
    • (1993) Science , vol.259 , pp. 1742-1745
    • Huang, S.1    Hendricks, W.2    Althage, A.3
  • 55
    • 0010228473 scopus 로고
    • Requirement of endogenous interferon-γ production for resolution of Listeria monocytogenes infection
    • Buchmeier NA, Schreiber RD: Requirement of endogenous interferon-γ production for resolution of Listeria monocytogenes infection. Proc Natl Acad Sci USA 82:7404-7408, 1985
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 7404-7408
    • Buchmeier, N.A.1    Schreiber, R.D.2
  • 56
    • 0028972007 scopus 로고
    • Impact of interferon-γ receptor deficiency on experimental Staphylococcus aureus septicemia and arthritis
    • Zhao Y-X, Tarkowski A: Impact of interferon-γ receptor deficiency on experimental Staphylococcus aureus septicemia and arthritis. J Immunol 155:5736-5742, 1995
    • (1995) J Immunol , vol.155 , pp. 5736-5742
    • Zhao, Y.-X.1    Tarkowski, A.2
  • 57
    • 0027360333 scopus 로고
    • An essential role for interferon gamma in resistance to Mycobacterium tuberculosis infection
    • Flynn JL, Chan J, Triebold KJ, et al: An essential role for interferon gamma in resistance to Mycobacterium tuberculosis infection. J Exp Med 178:2249-2254, 1993
    • (1993) J Exp Med , vol.178 , pp. 2249-2254
    • Flynn, J.L.1    Chan, J.2    Triebold, K.J.3
  • 58
    • 0027267486 scopus 로고
    • Generation of nitric oxide and induction of major histocompatibility complex class II antigen in macrophages from mice lacking the interferon y receptor
    • Kamijo R, Shapiro D, Le J, et al: Generation of nitric oxide and induction of major histocompatibility complex class II antigen in macrophages from mice lacking the interferon y receptor. Proc Natl Acad Sci USA 90:6626-6630, 1993
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 6626-6630
    • Kamijo, R.1    Shapiro, D.2    Le, J.3
  • 59
    • 0025070203 scopus 로고
    • The toxicity of staphylococcal enterotoxin B in mice is mediated by T cells
    • Marrack P, Blackmail M, Kushnir E, et al: The toxicity of staphylococcal enterotoxin B in mice is mediated by T cells. J Exp Med 171:455-464, 1990
    • (1990) J Exp Med , vol.171 , pp. 455-464
    • Marrack, P.1    Blackmail, M.2    Kushnir, E.3
  • 60
    • 0028008599 scopus 로고
    • Hepatic injury and lethal shock in galactosamine-sensitized mice induced by the superantigen staphylococcal enterotoxin B
    • Nagaki M, Muto Y, Ohnishi H, et al: Hepatic injury and lethal shock in galactosamine-sensitized mice induced by the superantigen staphylococcal enterotoxin B. Gastroenterology 106:450-458, 1994
    • (1994) Gastroenterology , vol.106 , pp. 450-458
    • Nagaki, M.1    Muto, Y.2    Ohnishi, H.3
  • 61
    • 0028937828 scopus 로고
    • Anti-gamma interferon and anti-interleukin-6 antibodies affect staphylococcal enterotoxin B-induced weight loss, hypoglycemia, and cytokine release in D-galactosamine-sensitized and unsensitized mice
    • Matthys P, Mitera T, Heremans H, et al: Anti-gamma interferon and anti-interleukin-6 antibodies affect staphylococcal enterotoxin B-induced weight loss, hypoglycemia, and cytokine release in D-galactosamine-sensitized and unsensitized mice. Infect Immun 63:1158-1164, 1995
    • (1995) Infect Immun , vol.63 , pp. 1158-1164
    • Matthys, P.1    Mitera, T.2    Heremans, H.3
  • 62
    • 0025887050 scopus 로고
    • Severe cachexia in mice inoculated with interferon-γ-producing tumor cells
    • Matthys P, Dijkmans R, Proost P, et al: Severe cachexia in mice inoculated with interferon-γ-producing tumor cells. Int J Cancer 49:77-82, 1991
    • (1991) Int J Cancer , vol.49 , pp. 77-82
    • Matthys, P.1    Dijkmans, R.2    Proost, P.3
  • 63
    • 0025865707 scopus 로고
    • The roles of γ-interferon and tumor necrosis factor a in an experimental model of cancer cachexia
    • Langstein HN, Doherty GM, Fraker DL, et al: The roles of γ-interferon and tumor necrosis factor a in an experimental model of cancer cachexia. Cancer Res 51:2302-2306, 1991
    • (1991) Cancer Res , vol.51 , pp. 2302-2306
    • Langstein, H.N.1    Doherty, G.M.2    Fraker, D.L.3
  • 64
    • 0026032432 scopus 로고
    • Anti-interferon-γ antibody treatment, growth of Lewis lung tumours in mice and tumour-associated cachexia
    • Matthys P, Heremans H, Opdenakker G, et al: Anti-interferon-γ antibody treatment, growth of Lewis lung tumours in mice and tumour-associated cachexia. Eur J Cancer 27:182-189, 1991
    • (1991) Eur J Cancer , vol.27 , pp. 182-189
    • Matthys, P.1    Heremans, H.2    Opdenakker, G.3
  • 65
    • 0025173973 scopus 로고
    • Phase II study of recombinant human interferon gamma for treatment of cutaneous T-cell lymphoma
    • Kaplan EH, Rosen ST, Norris DB, et al: Phase II study of recombinant human interferon gamma for treatment of cutaneous T-cell lymphoma. J Natl Cancer Inst 82:208-212, 1990
    • (1990) J Natl Cancer Inst , vol.82 , pp. 208-212
    • Kaplan, E.H.1    Rosen, S.T.2    Norris, D.B.3
  • 66
    • 0022643568 scopus 로고
    • Clinical and immunological evaluation of 20 patients with advanced colorectal cancer treated with high dose recombinant leukocyte interferon-αA (rIFN-αa)
    • Eggermont AM, Weimar W, Tank B, et al: Clinical and immunological evaluation of 20 patients with advanced colorectal cancer treated with high dose recombinant leukocyte interferon-αA (rIFN-αa). Cancer Immunol Immunother 21:81-84, 1986
    • (1986) Cancer Immunol Immunother , vol.21 , pp. 81-84
    • Eggermont, A.M.1    Weimar, W.2    Tank, B.3
  • 67
    • 0023759444 scopus 로고
    • A phase I study of recombinant interleukin 2 plus recombinant β-interferon
    • Krigel RL, Padavic-Shaller KA, Rudolph AR, et al: A phase I study of recombinant interleukin 2 plus recombinant β-interferon. Cancer Res 48:3875-3881, 1988
    • (1988) Cancer Res , vol.48 , pp. 3875-3881
    • Krigel, R.L.1    Padavic-Shaller, K.A.2    Rudolph, A.R.3
  • 68
    • 0022376371 scopus 로고
    • Proteolysis of skeletal muscle in response to acute elevation of plasma cortisol in man
    • Legaspi A, Albert JD, Calvano SE, et al: Proteolysis of skeletal muscle in response to acute elevation of plasma cortisol in man. Surg Forum 36:16-18, 1985
    • (1985) Surg Forum , vol.36 , pp. 16-18
    • Legaspi, A.1    Albert, J.D.2    Calvano, S.E.3
  • 69
    • 0023261107 scopus 로고
    • Sensitivity of myofibrillar protein to glucocorticoid-induced muscle proteolysis
    • Kayali AG, Young VR, Goodman MN: Sensitivity of myofibrillar protein to glucocorticoid-induced muscle proteolysis. Am J Physiol 252:E621-626, 1987
    • (1987) Am J Physiol , vol.252
    • Kayali, A.G.1    Young, V.R.2    Goodman, M.N.3
  • 70
    • 0025293425 scopus 로고
    • Corticosterone alone does not explain increased muscle proteolysis in septic rats
    • Hall-Angeras M, Hasseigren PO, Fischer JE: Corticosterone alone does not explain increased muscle proteolysis in septic rats. J Surg Res 48:368-372, 1990
    • (1990) J Surg Res , vol.48 , pp. 368-372
    • Hall-Angeras, M.1    Hasseigren, P.O.2    Fischer, J.E.3
  • 71
    • 0024386017 scopus 로고
    • Total and myofibrillar protein breakdown in different types of rat skeletal muscle: Effects of sepsis and regulation by insulin
    • Hasselgren PO, James JH, Benson DW, et al: Total and myofibrillar protein breakdown in different types of rat skeletal muscle: Effects of sepsis and regulation by insulin. Metabolism 38:634-640, 1989
    • (1989) Metabolism , vol.38 , pp. 634-640
    • Hasselgren, P.O.1    James, J.H.2    Benson, D.W.3
  • 72
    • 0001506616 scopus 로고
    • Cushing's syndrome
    • De Groot L, et al (eds), WB Saunders, Philadelphia
    • Nelson DH: Cushing's syndrome. IN Endocrinology, Vol II, De Groot L, et al (eds), WB Saunders, Philadelphia, 1989, pp 1660-1675
    • (1989) Endocrinology , vol.2 , pp. 1660-1675
    • Nelson, D.H.1
  • 73
    • 0023555212 scopus 로고
    • Interaction among hepatocyte-stimulating factors, interleukin-1, and glucocorticoids for regulation of acute phase proteins in human hepatoma (Hep G2) cells
    • Baumann H, Richards C, Gauldie J: Interaction among hepatocyte-stimulating factors, interleukin-1, and glucocorticoids for regulation of acute phase proteins in human hepatoma (Hep G2) cells. J Immunol 139:4122-4128, 1987
    • (1987) J Immunol , vol.139 , pp. 4122-4128
    • Baumann, H.1    Richards, C.2    Gauldie, J.3
  • 74
    • 0025761863 scopus 로고
    • Effect of the glucocorticoid receptor antagonist RU 38486 on muscle protein breakdown in sepsis
    • Hall-Angeras M, Zamir O, Hasselgren PO, et al: Effect of the glucocorticoid receptor antagonist RU 38486 on muscle protein breakdown in sepsis. Surgery 109:468-473, 1991
    • (1991) Surgery , vol.109 , pp. 468-473
    • Hall-Angeras, M.1    Zamir, O.2    Hasselgren, P.O.3
  • 75
    • 0025836449 scopus 로고
    • The effect of interleukin-1α and the glucocorticoid receptor blocker RU 38486 on total and myofibrillar protein breakdown in skeletal muscle
    • Zamir O, Hasselgren PO, von Allmen D, et al: The effect of interleukin-1α and the glucocorticoid receptor blocker RU 38486 on total and myofibrillar protein breakdown in skeletal muscle. J Surg Res 50:579-583, 1991
    • (1991) J Surg Res , vol.50 , pp. 579-583
    • Zamir, O.1    Hasselgren, P.O.2    Von Allmen, D.3
  • 76
    • 0027252612 scopus 로고
    • Effects of tumor necrosis factor or interleukin-1 on muscle amino acid uptake and the role of glucocorticoids
    • Zamir O, Hasselgren O, James H, et al: Effects of tumor necrosis factor or interleukin-1 on muscle amino acid uptake and the role of glucocorticoids. Surg Gynecol Obstet 177:27-32, 1993
    • (1993) Surg Gynecol Obstet , vol.177 , pp. 27-32
    • Zamir, O.1    Hasselgren, O.2    James, H.3
  • 77
    • 0002708343 scopus 로고    scopus 로고
    • RI 38486: An original multifaceted antihormone in vivo
    • Agarwal MK (ed), Walter de Gruyter, Hawthorne, NY
    • Philibert D: RI 38486: An original multifaceted antihormone in vivo. IN Adrenal Steroid Antagonism, Agarwal MK (ed), Walter de Gruyter, Hawthorne, NY, pp 77-100
    • Adrenal Steroid Antagonism , pp. 77-100
    • Philibert, D.1
  • 78
    • 0028116641 scopus 로고
    • Antioxidant: A new role for RU-486 and related compounds
    • Parthasarathy S, Morales AJ, Murphy AA: Antioxidant: A new role for RU-486 and related compounds. J Clin Invest 94:1990-1995, 1994
    • (1994) J Clin Invest , vol.94 , pp. 1990-1995
    • Parthasarathy, S.1    Morales, A.J.2    Murphy, A.A.3
  • 79
    • 0029071646 scopus 로고
    • Functions of the proteasome: The lysis at the end of the tunnel
    • Goldberg AL: Functions of the proteasome: The lysis at the end of the tunnel. Science 268:522-523, 1995
    • (1995) Science , vol.268 , pp. 522-523
    • Goldberg, A.L.1
  • 80
    • 0030593939 scopus 로고    scopus 로고
    • Mechanisms of muscle wasting. The role of the ubiquitin-proteasome pathway
    • Mitch WE, Goldberg AL: Mechanisms of muscle wasting. The role of the ubiquitin-proteasome pathway. N Engl J Med 335:1897-1905, 1996
    • (1996) N Engl J Med , vol.335 , pp. 1897-1905
    • Mitch, W.E.1    Goldberg, A.L.2
  • 81
    • 0029040739 scopus 로고
    • Activation of the ATP-ubiquitin-proteasome pathway in skeletal muscle of cachectic rats bearing a hepatoma
    • Baracos VE, DeVivo C, Hoyle DHR, et al: Activation of the ATP-ubiquitin-proteasome pathway in skeletal muscle of cachectic rats bearing a hepatoma Am J Physiol 268:E996-1006, 1995
    • (1995) Am J Physiol , vol.268
    • Baracos, V.E.1    DeVivo, C.2    Hoyle, D.H.R.3
  • 82
    • 0027972943 scopus 로고
    • Acidosis and glucocorticoids concomitantly increase ubiquitin and proteasome subunit mRNA in rat muscle
    • Price SR, England BK, Bailey JL, et al: Acidosis and glucocorticoids concomitantly increase ubiquitin and proteasome subunit mRNA in rat muscle. Am J Physiol 267:C955-960, 1994
    • (1994) Am J Physiol , vol.267
    • Price, S.R.1    England, B.K.2    Bailey, J.L.3
  • 83
    • 0029861468 scopus 로고    scopus 로고
    • Muscle wasting in insulinopenic rats results from the activation of the ATP-dependent, ubiquitin-proteasome proteolytic pathway by a mechanism including gene transcription
    • Price SR, Bailey JL, Wan X, et al: Muscle wasting in insulinopenic rats results from the activation of the ATP-dependent, ubiquitin-proteasome proteolytic pathway by a mechanism including gene transcription. J Clin Invest 98:1703-1708, 1996
    • (1996) J Clin Invest , vol.98 , pp. 1703-1708
    • Price, S.R.1    Bailey, J.L.2    Wan, X.3
  • 84
    • 0029655707 scopus 로고    scopus 로고
    • Necessary but not sufficient: The role of glucocorticoids in the acidosis-induced increase in levels of mRNAs encoding proteins of the ATP-dependent proteolytic pathway in rat muscle
    • Price SR, Bailey JL, England BK: Necessary but not sufficient: The role of glucocorticoids in the acidosis-induced increase in levels of mRNAs encoding proteins of the ATP-dependent proteolytic pathway in rat muscle. Miner Electrolyte Metab 22:72-75, 1996
    • (1996) Miner Electrolyte Metab , vol.22 , pp. 72-75
    • Price, S.R.1    Bailey, J.L.2    England, B.K.3
  • 85
    • 0029983847 scopus 로고    scopus 로고
    • 3H1 myocytes require an interaction between glucocorticoids and acidification
    • 3H1 myocytes require an interaction between glucocorticoids and acidification. Proc Natl Acad Sci USA 93:1967-1971, 1996
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1967-1971
    • Isozaki, Y.1    Mitch, W.E.2    England, B.K.3
  • 86
    • 0027973469 scopus 로고
    • Sepsis stimulates nonlysosomal, energy dependent proteolysis and increases ubiquitin mRNA levels in rat skeletal muscle
    • Tiao GT, Fagan JM, Samuels N, et al: Sepsis stimulates nonlysosomal, energy dependent proteolysis and increases ubiquitin mRNA levels in rat skeletal muscle. J Clin Invest 94:2255-2264, 1994
    • (1994) J Clin Invest , vol.94 , pp. 2255-2264
    • Tiao, G.T.1    Fagan, J.M.2    Samuels, N.3
  • 87
    • 0030051797 scopus 로고    scopus 로고
    • Energy-ubiquitin-dependent muscle proteolysis during sepsis in rats is regulated by glucocorticoids
    • Tiao GT, Fagan J, Roegner V, et al: Energy-ubiquitin-dependent muscle proteolysis during sepsis in rats is regulated by glucocorticoids. J Clin Invest 97:339-348, 1996
    • (1996) J Clin Invest , vol.97 , pp. 339-348
    • Tiao, G.T.1    Fagan, J.2    Roegner, V.3
  • 88
    • 0031018516 scopus 로고    scopus 로고
    • Sepsis is associated with increased mRNAs of the ubiquitin-proteasome proteolytic pathway in human skeletal muscle
    • Tiao GT, Hoblet S, Wang JJ, et al: Sepsis is associated with increased mRNAs of the ubiquitin-proteasome proteolytic pathway in human skeletal muscle. J Clin Invest 99:163-168, 1997
    • (1997) J Clin Invest , vol.99 , pp. 163-168
    • Tiao, G.T.1    Hoblet, S.2    Wang, J.J.3
  • 89
    • 0028007982 scopus 로고
    • 14-kDa ubiquitin-conjugating enzyme: Sructure of the rat gene and regulation upon fasting and by insulin
    • Wing SS, Banville D: 14-kDa ubiquitin-conjugating enzyme: Sructure of the rat gene and regulation upon fasting and by insulin. Am J Physiol 267:E39-48, 1994
    • (1994) Am J Physiol , vol.267
    • Wing, S.S.1    Banville, D.2
  • 90
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko A, Ciechanover A: The ubiquitin system for protein degradation. Annu Rev Biochem 61:761-807, 1992
    • (1992) Annu Rev Biochem , vol.61 , pp. 761-807
    • Hershko, A.1    Ciechanover, A.2
  • 91
    • 0029174397 scopus 로고
    • The 20S/26S proteasomal pathway of protein degradation in muscle liver
    • Dahlmann B, Kuehn L: The 20S/26S proteasomal pathway of protein degradation in muscle liver. Mol Biol Rep 21:57-62, 1995
    • (1995) Mol Biol Rep , vol.21 , pp. 57-62
    • Dahlmann, B.1    Kuehn, L.2
  • 92
    • 0029174327 scopus 로고
    • Catalytic components of proteasomes and the regulation of proteinase activity
    • Rivett AJ, Mason GGF, Thomson S, et al: Catalytic components of proteasomes and the regulation of proteinase activity. Mol Biol Rep 21:35-41, 1995
    • (1995) Mol Biol Rep , vol.21 , pp. 35-41
    • Rivett, A.J.1    Mason, G.G.F.2    Thomson, S.3
  • 93
    • 0029597841 scopus 로고
    • Ubiquitin gene expression in skeletal muscle is increased during sepsis: Involvement of TNFα but not IL-1
    • Garciá-Martinez C, Llovera M, Agell N, et al: Ubiquitin gene expression in skeletal muscle is increased during sepsis: Involvement of TNFα but not IL-1. Biochem Biophys Res Commun 217:839-844, 1995
    • (1995) Biochem Biophys Res Commun , vol.217 , pp. 839-844
    • Garciá-Martinez, C.1    Llovera, M.2    Agell, N.3
  • 94
    • 0029883726 scopus 로고    scopus 로고
    • 2+-activated, and ubiquitin-proteasome protelytic pathways
    • 2+-activated, and ubiquitin-proteasome protelytic pathways. J Clin Invest 97:1610-1617, 1996
    • (1996) J Clin Invest , vol.97 , pp. 1610-1617
    • Voisin, L.1    Breuilé, D.2    Combaret, L.3
  • 95
    • 0024206530 scopus 로고
    • Endocrine regulation of protein breakdown in skeletal muscle
    • Kettelhut IC, Wing SS, Goldberg AL: Endocrine regulation of protein breakdown in skeletal muscle. Diabet Metab Rev 4:751-772, 1988
    • (1988) Diabet Metab Rev , vol.4 , pp. 751-772
    • Kettelhut, I.C.1    Wing, S.S.2    Goldberg, A.L.3
  • 96
    • 0026773948 scopus 로고
    • Cytokines, muscle proteolysis, and the catabolic response to infection and inflammation
    • Bistrian BR, Schwarte J, Istfan NW: Cytokines, muscle proteolysis, and the catabolic response to infection and inflammation. Proc Soc Exp Biol Med 200:220-223, 1992
    • (1992) Proc Soc Exp Biol Med , vol.200 , pp. 220-223
    • Bistrian, B.R.1    Schwarte, J.2    Istfan, N.W.3
  • 97
    • 13344270347 scopus 로고    scopus 로고
    • Metabolic changes in rats during a continuous infusion of recombinant interleukin 1
    • Ling PR, Schwartz JH, Jeevanandam M, et al: Metabolic changes in rats during a continuous infusion of recombinant interleukin 1. Am J Physiol 270:E-305-312, 1996
    • (1996) Am J Physiol , vol.270
    • Ling, P.R.1    Schwartz, J.H.2    Jeevanandam, M.3
  • 98
    • 0030888377 scopus 로고    scopus 로고
    • Mechanisms of host wasting induced by administration of cytokines in rats
    • Ling PR, Schwartz JH, Bistrian BR: Mechanisms of host wasting induced by administration of cytokines in rats. Am J Physiol 272: E333-339, 1997
    • (1997) Am J Physiol , vol.272
    • Ling, P.R.1    Schwartz, J.H.2    Bistrian, B.R.3
  • 99
    • 0025306999 scopus 로고
    • Cachectic effects of recombinant human tumor necrosis factor in rats
    • Darling G, Fraker DL, Jensen JC, et al: Cachectic effects of recombinant human tumor necrosis factor in rats. Cancer Res 50:4008-4013, 1990
    • (1990) Cancer Res , vol.50 , pp. 4008-4013
    • Darling, G.1    Fraker, D.L.2    Jensen, J.C.3
  • 100
    • 0026557647 scopus 로고
    • Evidence that tumor necrosis factor participates in the regulation of muscle proteolysis during sepsis
    • Zamir O, Hasselgren PO, Kunkel SL, et al: Evidence that tumor necrosis factor participates in the regulation of muscle proteolysis during sepsis. Arch Surg 127:170-174, 1992
    • (1992) Arch Surg , vol.127 , pp. 170-174
    • Zamir, O.1    Hasselgren, P.O.2    Kunkel, S.L.3
  • 101
    • 0028180058 scopus 로고
    • Reduced muscle protein breakdown in septic rats following treatment with interleukin-1 receptor antagonist
    • Zamir O, O'Brien W, Thompson R, et al: Reduced muscle protein breakdown in septic rats following treatment with interleukin-1 receptor antagonist. Int J Biochem 26:943-950, 1994
    • (1994) Int J Biochem , vol.26 , pp. 943-950
    • Zamir, O.1    O'Brien, W.2    Thompson, R.3
  • 102
    • 0028201322 scopus 로고
    • Interleukin-6 induces skeletal muscle protein breakdown in rats
    • Goodman MN: Interleukin-6 induces skeletal muscle protein breakdown in rats. Proc Soc Exp Biol Med 205:182-185, 1994
    • (1994) Proc Soc Exp Biol Med , vol.205 , pp. 182-185
    • Goodman, M.N.1
  • 103
    • 0028789750 scopus 로고
    • Interleukin-6 induces proteolysis by activating intracellular proteases (cathepsin B and L, proteasomes) in C2C12 myotubes
    • Ebisui C, Tsujinaka T, Morimoto T, et al: Interleukin-6 induces proteolysis by activating intracellular proteases (cathepsin B and L, proteasomes) in C2C12 myotubes. Clin Sci 89:431-439, 1995
    • (1995) Clin Sci , vol.89 , pp. 431-439
    • Ebisui, C.1    Tsujinaka, T.2    Morimoto, T.3
  • 104
    • 0025896935 scopus 로고
    • Chinese hamster ovary cells transfected with the murine IL-6 gene cause hypercalcemia as well as cachexia, leukocytosis and thrombocytosis in tumor bearing nude mice
    • Black K, Garrett IR, Mundy GR: Chinese hamster ovary cells transfected with the murine IL-6 gene cause hypercalcemia as well as cachexia, leukocytosis and thrombocytosis in tumor bearing nude mice. Endocrinology 128:2657-2659, 1991
    • (1991) Endocrinology , vol.128 , pp. 2657-2659
    • Black, K.1    Garrett, I.R.2    Mundy, G.R.3
  • 105
    • 0028966015 scopus 로고
    • Muscle undergoes atrophy in association with increase of lysosomal cathepsin activity in interleukin-6 transgenic mice
    • Tsujinaka T, Ebisui C, Fujita J, et al: Muscle undergoes atrophy in association with increase of lysosomal cathepsin activity in interleukin-6 transgenic mice. Biochem Biophys Res Commun 207:168-174, 1995
    • (1995) Biochem Biophys Res Commun , vol.207 , pp. 168-174
    • Tsujinaka, T.1    Ebisui, C.2    Fujita, J.3
  • 106
    • 13344261948 scopus 로고    scopus 로고
    • Interleukin 6 receptor antibody inhibits muscle atrophy and modulates proteolytic systems in interleukin 6 transgenic mice
    • Tsujinaka T, Fujita J, Ebisui C, et al: Interleukin 6 receptor antibody inhibits muscle atrophy and modulates proteolytic systems in interleukin 6 transgenic mice. J Clin Invest 97:244-249, 1996
    • (1996) J Clin Invest , vol.97 , pp. 244-249
    • Tsujinaka, T.1    Fujita, J.2    Ebisui, C.3
  • 107
    • 0030058649 scopus 로고    scopus 로고
    • Interleukin (IL)-6 gene expression in the central nervous system is necessary for fever response to lipopolysaccharide or IL-1β: A study on IL-6-deficient mice
    • Chai Z, Gatti S, Toniatti C, et al: Interleukin (IL)-6 gene expression in the central nervous system is necessary for fever response to lipopolysaccharide or IL-1β: A study on IL-6-deficient mice. J Exp Med 183:311-316, 1996
    • (1996) J Exp Med , vol.183 , pp. 311-316
    • Chai, Z.1    Gatti, S.2    Toniatti, C.3
  • 108
    • 0027984754 scopus 로고
    • Defective inflammatory response in interleukin-6-deficient mice
    • Fattori E, Capelletti M, Costa P, et al: Defective inflammatory response in interleukin-6-deficient mice. J Exp Med 1994;180:1243-1250, 1994
    • (1994) J Exp Med 1994 , vol.180 , pp. 1243-1250
    • Fattori, E.1    Capelletti, M.2    Costa, P.3
  • 109
    • 0030938914 scopus 로고    scopus 로고
    • Sickness behavior in mice deficient in interleukin-6 during turpentine abscess and influenza pneumonitis
    • Kozak W, Poli V, Soszynski D, et al: Sickness behavior in mice deficient in interleukin-6 during turpentine abscess and influenza pneumonitis. Am J Physiol 272:R661-630, 1997
    • (1997) Am J Physiol , vol.272
    • Kozak, W.1    Poli, V.2    Soszynski, D.3
  • 110
    • 0029885829 scopus 로고    scopus 로고
    • Anti-TNF treatment reverts increased muscle ubiquitin gene expression in tumour-bearing rats
    • Llovera M, Carbó N, Garciá-Marti ez C, et al: Anti-TNF treatment reverts increased muscle ubiquitin gene expression in tumour-bearing rats. Biochem Biophys Res Commun 221:653-655, 1996
    • (1996) Biochem Biophys Res Commun , vol.221 , pp. 653-655
    • Llovera, M.1    Carbó, N.2    Garciá-Marti ez, C.3
  • 111
    • 0024989574 scopus 로고
    • Interaction between corticosterone and tumor necrosis factor stimulated protein breakdown in rat skeletal muscle, similar to sepsis
    • Hall-Agnerås M, Angerås U, Zamir O, et al: Interaction between corticosterone and tumor necrosis factor stimulated protein breakdown in rat skeletal muscle, similar to sepsis. Surgery 108:460-466, 1990
    • (1990) Surgery , vol.108 , pp. 460-466
    • Hall-Agnerås, M.1    Angerås, U.2    Zamir, O.3
  • 112
    • 0025190405 scopus 로고
    • Are the catabolic effects of tumor necrosis factor mediated by glucocorticoids?
    • Mealy K, van Lanschot JJB, Robinson BG, et al: Are the catabolic effects of tumor necrosis factor mediated by glucocorticoids? Arch Surg 125:42-48, 1990
    • (1990) Arch Surg , vol.125 , pp. 42-48
    • Mealy, K.1    Van Lanschot, J.J.B.2    Robinson, B.G.3
  • 113
    • 0028347823 scopus 로고
    • Pharmacological interference with cancer cachexia
    • Tessitore L, Costelli P, Baccino FM: Pharmacological interference with cancer cachexia. Biochem J 299:71-78, 1994
    • (1994) Biochem J , vol.299 , pp. 71-78
    • Tessitore, L.1    Costelli, P.2    Baccino, F.M.3
  • 114
    • 0028587742 scopus 로고
    • Tumor necrosis factor a: A key component of the obesity-diabetes link
    • Hotamisligil GS, Spiegelman BM. Tumor necrosis factor a: A key component of the obesity-diabetes link. Diabetes 1994;43:1271-1278
    • (1994) Diabetes , vol.43 , pp. 1271-1278
    • Hotamisligil, G.S.1    Spiegelman, B.M.2
  • 115
    • 0030028606 scopus 로고    scopus 로고
    • The expression of TNFα by human muscle. Relationship to insulin resistance
    • Saghizadeh M, Ong JM, Garvey WT, et al: The expression of TNFα by human muscle. Relationship to insulin resistance. J Clin Invest 97:1111-1116, 1996
    • (1996) J Clin Invest , vol.97 , pp. 1111-1116
    • Saghizadeh, M.1    Ong, J.M.2    Garvey, W.T.3
  • 116
    • 0027130313 scopus 로고
    • Pentoxifylline decreases body weight loss and muscle protein wasting characteristics of sepsis
    • Breuillé D, Farge MC, Rose F, et al: Pentoxifylline decreases body weight loss and muscle protein wasting characteristics of sepsis. Am J Physiol 265:E660-666, 1993
    • (1993) Am J Physiol , vol.265
    • Breuillé, D.1    Farge, M.C.2    Rose, F.3
  • 117
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing of the NF-κB1 precursor protein and the activation of NF-KB
    • Palombella VJ, Rando OJ, Goldberg AL, et al: The ubiquitin-proteasome pathway is required for processing of the NF-κB1 precursor protein and the activation of NF-KB. Cell 78:773-785, 1994
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3
  • 118
    • 0026549669 scopus 로고
    • Tumor necrosis factor impairs insulin action on peripheral glucose disposal and hepatic glucose output
    • Lang CH, Dobrescu C, Bagby GJ: Tumor necrosis factor impairs insulin action on peripheral glucose disposal and hepatic glucose output. Endocrinology 130:43-52, 1992
    • (1992) Endocrinology , vol.130 , pp. 43-52
    • Lang, C.H.1    Dobrescu, C.2    Bagby, G.J.3
  • 119
    • 0026331897 scopus 로고
    • Effects of recombinant IGF-I on protein and glucose metabolism in rTNF-infused lambs
    • Douglas RG, Gluckman PD, Breier BH, et al: Effects of recombinant IGF-I on protein and glucose metabolism in rTNF-infused lambs. Am J Physiol 261:E606-612, 1991
    • (1991) Am J Physiol , vol.261
    • Douglas, R.G.1    Gluckman, P.D.2    Breier, B.H.3
  • 120
    • 0002370948 scopus 로고
    • Insulin resistance in man
    • Rifkin H, Porte D Jr (eds), Elsevier, NY
    • Olefsky JM, Molina JM: Insulin resistance in man. IN Diabetes Mellitus, 4th ed, Rifkin H, Porte D Jr (eds), Elsevier, NY, 1990, pp 121-153
    • (1990) Diabetes Mellitus, 4th Ed , pp. 121-153
    • Olefsky, J.M.1    Molina, J.M.2
  • 121
    • 0030056373 scopus 로고    scopus 로고
    • Epinephrine inhibits tumor necrosis factor a and potentiates interleukin 10 production during human endotoxemia
    • van der Poll T, Coyle SM, Barbosa K, et al: Epinephrine inhibits tumor necrosis factor a and potentiates interleukin 10 production during human endotoxemia. J Clin Invest 97:713-719, 1996
    • (1996) J Clin Invest , vol.97 , pp. 713-719
    • Van Der Poll, T.1    Coyle, S.M.2    Barbosa, K.3
  • 122
    • 0029846566 scopus 로고    scopus 로고
    • Acute effect of epinephrine on muscle proteolysis in perfused rat hindquarters
    • Kadowaki M, Kamata T, Noguchi T: Acute effect of epinephrine on muscle proteolysis in perfused rat hindquarters. Am J Physiol 270:E961-967, 1996
    • (1996) Am J Physiol , vol.270
    • Kadowaki, M.1    Kamata, T.2    Noguchi, T.3
  • 124
    • 0027478964 scopus 로고
    • 2-adrenergic agonist, reverses muscle wasting due to scald injury in the rat
    • 2-adrenergic agonist, reverses muscle wasting due to scald injury in the rat. Burns 19:26-34, 1994
    • (1994) Burns , vol.19 , pp. 26-34
    • Martineau, L.1    Little, R.A.2    Rothwell, N.J.3
  • 125
    • 0028916883 scopus 로고
    • 2-adrenergic agonist (clenbuterol). Role of the ATP-ubiquitin-dependent proteolytic pathway
    • 2-adrenergic agonist (clenbuterol). Role of the ATP-ubiquitin-dependent proteolytic pathway. J Clin Invest 95:2367-2372, 1995
    • (1995) J Clin Invest , vol.95 , pp. 2367-2372
    • Costelli, P.1    Garciá-Marti ez, C.2    Llovera, M.3
  • 126
    • 0029085801 scopus 로고
    • Interleukin-1 receptor antagonist (IL-1ra) is unable to reverse cachexia in rats bearing an ascites hepatoma (Yoshida AH-130)
    • Costelli P, Carbó N, Garciá-Marti ez C, et al: Interleukin-1 receptor antagonist (IL-1ra) is unable to reverse cachexia in rats bearing an ascites hepatoma (Yoshida AH-130). Cancer Lett 95:33-38, 1995
    • (1995) Cancer Lett , vol.95 , pp. 33-38
    • Costelli, P.1    Carbó, N.2    Garciá-Marti ez, C.3
  • 127
    • 0028114904 scopus 로고
    • Interleukin-1 receptor antagonist prevents sepsis-induced inhibition of protein synthesis
    • Cooney RN, Owens F, Jurasinki C, et al: Interleukin-1 receptor antagonist prevents sepsis-induced inhibition of protein synthesis. Am J Physiol 267:E636-64, 1994
    • (1994) Am J Physiol , vol.267
    • Cooney, R.N.1    Owens, F.2    Jurasinki, C.3
  • 128
    • 0028886248 scopus 로고
    • Insulin-like growth factor I accelerates protein synthesis in skeletal muscle during sepsis
    • Jurasinki CV, Vary TC: Insulin-like growth factor I accelerates protein synthesis in skeletal muscle during sepsis. Am J Physiol 269:E977-981, 1995
    • (1995) Am J Physiol , vol.269
    • Jurasinki, C.V.1    Vary, T.C.2
  • 129
    • 0029984415 scopus 로고    scopus 로고
    • IL-1 receptor antagonist attenuates sepsis-induced alterations in the IGF system and protein synthesis
    • Lang CH, Fan J, Cooney RN, et al: IL-1 receptor antagonist attenuates sepsis-induced alterations in the IGF system and protein synthesis. Am J Physiol 270:E430-437, 1996
    • (1996) Am J Physiol , vol.270
    • Lang, C.H.1    Fan, J.2    Cooney, R.N.3
  • 130
    • 0029340530 scopus 로고
    • Modulation of inflammation-induced changes in insulin-like growth factor (IGF)-I and IGF binding protein-1 by anti-TNF antibody
    • Fan J, Li YH, Bagby GJ, et al: Modulation of inflammation-induced changes in insulin-like growth factor (IGF)-I and IGF binding protein-1 by anti-TNF antibody. Shock 4:21-26, 1995
    • (1995) Shock , vol.4 , pp. 21-26
    • Fan, J.1    Li, Y.H.2    Bagby, G.J.3
  • 131
    • 0028202862 scopus 로고
    • Differential tissue regulation of insulin-like growth factor-I content and binding proteins after endotoxin
    • Fan J, Molina PE, Gelato MC, et al: Differential tissue regulation of insulin-like growth factor-I content and binding proteins after endotoxin. Endocrinology 134:1685-1692, 1994.
    • (1994) Endocrinology , vol.134 , pp. 1685-1692
    • Fan, J.1    Molina, P.E.2    Gelato, M.C.3
  • 132
    • 0028945843 scopus 로고
    • Alterations in the insulin-like growth factor system in trauma patients
    • Wojnar MM, Fan J, Frost RA, et al: Alterations in the insulin-like growth factor system in trauma patients. Am J Physiol 268:R970-977, 1995
    • (1995) Am J Physiol , vol.268
    • Wojnar, M.M.1    Fan, J.2    Frost, R.A.3
  • 133
    • 0027934598 scopus 로고
    • Differential effects of thermal injury on circulating insulin-like growth factor binding proteins in burn patients
    • Ghahary A, Fu S, Shen YJ, et al: Differential effects of thermal injury on circulating insulin-like growth factor binding proteins in burn patients. Mol Cell Biochem 135:171-180, 1994
    • (1994) Mol Cell Biochem , vol.135 , pp. 171-180
    • Ghahary, A.1    Fu, S.2    Shen, Y.J.3
  • 134
    • 0028789723 scopus 로고
    • Regulation of insulin-like growth factor (IGF)-I and IGF-binding proteins by tumor necrosis factor
    • Fan J, Char D, Bagby GJ, et al: Regulation of insulin-like growth factor (IGF)-I and IGF-binding proteins by tumor necrosis factor. Am J Physiol 269:R1204-1212, 1995
    • (1995) Am J Physiol , vol.269
    • Fan, J.1    Char, D.2    Bagby, G.J.3
  • 135
    • 0030004837 scopus 로고
    • Regulation of insulin-growth factor (IGF)-I mRNA and peptide, and IGF-I binding proteins by interleukin-1
    • Fan J, Wojnar MM, Theodorakis M, et al: Regulation of insulin-growth factor (IGF)-I mRNA and peptide, and IGF-I binding proteins by interleukin-1. Am J Physiol 270:R621-629, 1995
    • (1995) Am J Physiol , vol.270
    • Fan, J.1    Wojnar, M.M.2    Theodorakis, M.3
  • 136
    • 0028219050 scopus 로고
    • Insulin-like growth factor-1 and insulin resistance in skeletal muscle of adult and old rats
    • Dardevet D, Sornet C, Attaix D, et al: Insulin-like growth factor-1 and insulin resistance in skeletal muscle of adult and old rats. Endocrinology 134:1475-1484, 1994
    • (1994) Endocrinology , vol.134 , pp. 1475-1484
    • Dardevet, D.1    Sornet, C.2    Attaix, D.3
  • 137
    • 0028507737 scopus 로고
    • Effects of serum and insulin-like growth factor I on protein degradation and protease gene expression in rat L8 myotubes
    • Hong DH, Forsberg NE: Effects of serum and insulin-like growth factor I on protein degradation and protease gene expression in rat L8 myotubes. J Anim Sci 72:2279-2288, 1994
    • (1994) J Anim Sci , vol.72 , pp. 2279-2288
    • Hong, D.H.1    Forsberg, N.E.2
  • 138
    • 0029819257 scopus 로고    scopus 로고
    • Regulation of peptide-chain initiation in muscle during sepsis by interleukin-1 receptor antagonist
    • Vary TC, Voisin L, Cooney RN: Regulation of peptide-chain initiation in muscle during sepsis by interleukin-1 receptor antagonist. Am J Physiol 271:E513-520, 1996
    • (1996) Am J Physiol , vol.271
    • Vary, T.C.1    Voisin, L.2    Cooney, R.N.3
  • 139
    • 0029881920 scopus 로고
    • Prevention of skeletal muscle catabolism in sepsis does not impair visceral protein metabolism
    • Cooney RN, Owens E, Slaymaker D, et al: Prevention of skeletal muscle catabolism in sepsis does not impair visceral protein metabolism. Am J Physiol 270:E621-326, 1995
    • (1995) Am J Physiol , vol.270
    • Cooney, R.N.1    Owens, E.2    Slaymaker, D.3
  • 140
    • 0029771630 scopus 로고    scopus 로고
    • Central interleukin-1 partially mediates endotoxin-induced changes in glucose metabolism
    • Lang CH, Cooney R, Vary TC: Central interleukin-1 partially mediates endotoxin-induced changes in glucose metabolism. Am J Physiol 271:E309-316, 1996
    • (1996) Am J Physiol , vol.271
    • Lang, C.H.1    Cooney, R.2    Vary, T.C.3
  • 141
    • 0016054255 scopus 로고
    • Insulin in the regulation of protein turnover in heart and skeletal muscle
    • Jefferson LS, Rannels DE, Munger BL, et al: Insulin in the regulation of protein turnover in heart and skeletal muscle. Fed Proc 33:1098-1104, 1974
    • (1974) Fed Proc , vol.33 , pp. 1098-1104
    • Jefferson, L.S.1    Rannels, D.E.2    Munger, B.L.3
  • 142
    • 0016431688 scopus 로고
    • Effects of insulin, glucose and amino acids on protein turnover in rat diaphragm
    • Fulks R, Li JB, Goldberg AL: Effects of insulin, glucose and amino acids on protein turnover in rat diaphragm. J Biol Chem 250:290-298, 1975
    • (1975) J Biol Chem , vol.250 , pp. 290-298
    • Fulks, R.1    Li, J.B.2    Goldberg, A.L.3
  • 143
    • 0016288682 scopus 로고
    • The actions of insulin, trypsin and electrical stimulation on amino acid transport in muscle
    • Narahara HT, Holloszy JO: The actions of insulin, trypsin and electrical stimulation on amino acid transport in muscle. J Biol Chem 249:5435-5443, 1974
    • (1974) J Biol Chem , vol.249 , pp. 5435-5443
    • Narahara, H.T.1    Holloszy, J.O.2
  • 144
    • 0019959162 scopus 로고
    • Muscle protein breakdown in uncontrolled diabetes as assessed by urinary 3-methylhistidine excretion
    • Marchesini G, Forlani G, Zoli M, et al: Muscle protein breakdown in uncontrolled diabetes as assessed by urinary 3-methylhistidine excretion. Diabetologia 23:456-458, 1982
    • (1982) Diabetologia , vol.23 , pp. 456-458
    • Marchesini, G.1    Forlani, G.2    Zoli, M.3
  • 145
    • 0019302317 scopus 로고
    • Muscle protein catabolism in diabetes: 3-Methylhistidine excretion in the spontaneously diabetic BB rat
    • Nakhooda AF, Wei CN, Marliss EB: Muscle protein catabolism in diabetes: 3-Methylhistidine excretion in the spontaneously diabetic BB rat. Metab Clin Exp 29:1272-1277, 1980
    • (1980) Metab Clin Exp , vol.29 , pp. 1272-1277
    • Nakhooda, A.F.1    Wei, C.N.2    Marliss, E.B.3
  • 146
    • 0024442483 scopus 로고
    • Skeletal muscle proteolysis in rats with acute streptozocin-induced diabetes
    • Smith OLK, Wong CY, Gelfand RA: Skeletal muscle proteolysis in rats with acute streptozocin-induced diabetes. Diabetes 38:1117-1122, 1989
    • (1989) Diabetes , vol.38 , pp. 1117-1122
    • Smith, O.L.K.1    Wong, C.Y.2    Gelfand, R.A.3
  • 147
    • 0025322546 scopus 로고
    • Influence of glucocorticoids on skeletal muscle proteolysis in normal and diabetic-adrenalectomized eviscerated rats
    • Smith OLK, Wong CY, Gelfand RA: Influence of glucocorticoids on skeletal muscle proteolysis in normal and diabetic-adrenalectomized eviscerated rats. Metabolism 39:641-646, 1990
    • (1990) Metabolism , vol.39 , pp. 641-646
    • Smith, O.L.K.1    Wong, C.Y.2    Gelfand, R.A.3
  • 148
    • 0029794194 scopus 로고    scopus 로고
    • Euglycemic hyperinsulinemia and hyperaminoacidemia decrease skeletal muscle ubiquitin mRNA in goats
    • Larbaud D, Debras E, Taillander D, et al: Euglycemic hyperinsulinemia and hyperaminoacidemia decrease skeletal muscle ubiquitin mRNA in goats. Am J Physiol 271:E505-512, 1996
    • (1996) Am J Physiol , vol.271
    • Larbaud, D.1    Debras, E.2    Taillander, D.3
  • 149
    • 0028362194 scopus 로고
    • Tumor necrosis factor a inhibits signaling from the insulin receptor
    • Hotamisligil GS, Murray DL, Choy LN, et al: Tumor necrosis factor a inhibits signaling from the insulin receptor. Proc Natl Acad Sci USA 91:4854-4858, 1994
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4854-4858
    • Hotamisligil, G.S.1    Murray, D.L.2    Choy, L.N.3
  • 150
    • 0024336307 scopus 로고
    • Monokine regulation of glucose transporter mRNA in L6 myotubes
    • Cornelius P, Lee MD, Marlowe M: Monokine regulation of glucose transporter mRNA in L6 myotubes. Biochem Biophys Res Commun 165:429-436, 1989
    • (1989) Biochem Biophys Res Commun , vol.165 , pp. 429-436
    • Cornelius, P.1    Lee, M.D.2    Marlowe, M.3
  • 151
    • 0028031569 scopus 로고
    • Reduced tyrosine kinase activity of the insulin receptor in obesity-diabetes: Central role of tumor necrosis factor a
    • Hotamisligil GS, Budavari A, Murray DL, et al: Reduced tyrosine kinase activity of the insulin receptor in obesity-diabetes: Central role of tumor necrosis factor a. J Clin Invest 94:1543-1549, 1994
    • (1994) J Clin Invest , vol.94 , pp. 1543-1549
    • Hotamisligil, G.S.1    Budavari, A.2    Murray, D.L.3
  • 152
    • 0023795075 scopus 로고
    • Relationship between glutamine concentration and protein synthesis in rat skeletal muscle
    • Jepson MM, Bates PC, Broadbent P, et al: Relationship between glutamine concentration and protein synthesis in rat skeletal muscle. Am J Physiol 255:E166-172, 1988
    • (1988) Am J Physiol , vol.255
    • Jepson, M.M.1    Bates, P.C.2    Broadbent, P.3
  • 153
    • 0024238924 scopus 로고
    • Murine glutamine synthetase: Cloning developmental, regulation and glucocorticoid inducibility
    • Magnuson SR, Young AP: Murine glutamine synthetase: Cloning developmental, regulation and glucocorticoid inducibility. Dev Biol 130:536-542, 1988
    • (1988) Dev Biol , vol.130 , pp. 536-542
    • Magnuson, S.R.1    Young, A.P.2
  • 154
    • 0024454645 scopus 로고
    • Glutamine-containing dipeptides as infusion substrates in the septic state
    • Karner J, Roth E, Ollenschlager G, et al: Glutamine-containing dipeptides as infusion substrates in the septic state. Surgery 1989;106:893-900, 1989
    • (1989) Surgery 1989 , vol.106 , pp. 893-900
    • Karner, J.1    Roth, E.2    Ollenschlager, G.3
  • 155
    • 0029994477 scopus 로고    scopus 로고
    • Glutamine interferes with glucocorticoid-induced expression of glutamine synthetase in skeletal muscle
    • Hickson RC, Wegrzyn LE, Osborne DF, et al: Glutamine interferes with glucocorticoid-induced expression of glutamine synthetase in skeletal muscle. Am J Physiol 270:E912-917, 1996
    • (1996) Am J Physiol , vol.270
    • Hickson, R.C.1    Wegrzyn, L.E.2    Osborne, D.F.3
  • 156
    • 0020699776 scopus 로고
    • Muscle proteolysis induced by a circulating peptide in patients with sepsis or trauma
    • Clowes GHC Jr, George BC, Villee CA Jr, et al: Muscle proteolysis induced by a circulating peptide in patients with sepsis or trauma. N Engl J Med 308:545-552, 1983
    • (1983) N Engl J Med , vol.308 , pp. 545-552
    • Ghc Jr., C.1    George, B.C.2    Villee Jr., C.A.3
  • 157
    • 0028962849 scopus 로고
    • Purification and characterization of a lipid-mobilizing factor associated with cachexia-inducing tumors in mice and humans
    • McDevitt TM, Todorov PT, Beck SA: Purification and characterization of a lipid-mobilizing factor associated with cachexia-inducing tumors in mice and humans. Cancer Res 55:1458-1463, 1995
    • (1995) Cancer Res , vol.55 , pp. 1458-1463
    • McDevitt, T.M.1    Todorov, P.T.2    Beck, S.A.3
  • 158
    • 0030063921 scopus 로고    scopus 로고
    • Characterization of a cancer cachectin factor
    • Todorov P, Cariuk P, McDevitt T, et al: Characterization of a cancer cachectin factor. Nature 379:739-742, 1996
    • (1996) Nature , vol.379 , pp. 739-742
    • Todorov, P.1    Cariuk, P.2    McDevitt, T.3
  • 159
    • 0026503828 scopus 로고
    • The mechanisms and functions of ATP-dependent proteases in bacterial and animals cells
    • Goldberg AL: The mechanisms and functions of ATP-dependent proteases in bacterial and animals cells. Eur J Biochem 203:9-23, 1992
    • (1992) Eur J Biochem , vol.203 , pp. 9-23
    • Goldberg, A.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.