메뉴 건너뛰기




Volumn 19, Issue 2, 1999, Pages 141-156

Cytokines and the hepatic acute-phase response

Author keywords

Acute phase response; Cytokines; Inflammation; Liver

Indexed keywords

CYTOKINE; CYTOKINE RECEPTOR; INTERLEUKIN 1; INTERLEUKIN 6; LIVER ENZYME; PLASMA PROTEIN;

EID: 0032771993     PISSN: 02728087     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-2007-1007106     Document Type: Review
Times cited : (259)

References (173)
  • 1
    • 0020000298 scopus 로고
    • The phenomenon of the acute phase response
    • Kushner I. The phenomenon of the acute phase response. Ann NY Acad Sci 1982;289:39-48
    • (1982) Ann NY Acad Sci , vol.289 , pp. 39-48
    • Kushner, I.1
  • 3
    • 84909857011 scopus 로고
    • Sites of SAA/AA synthesis
    • Marrink J, Van Rijswijk MH, eds. Dordrecht: Martinus Nijhoff
    • Sipe J, Ramadori G. Sites of SAA/AA synthesis. In: Marrink J, Van Rijswijk MH, eds. Amyloidosis. Dordrecht: Martinus Nijhoff, 1986:319-327
    • (1986) Amyloidosis , pp. 319-327
    • Sipe, J.1    Ramadori, G.2
  • 4
    • 0022179342 scopus 로고
    • Expression and regulation of the murine serum amyloid A (SAA) gene in extrahepatic sites
    • Ramadori G, Sipe JD, Colten HR. Expression and regulation of the murine serum amyloid A (SAA) gene in extrahepatic sites. J Immunol 1985;135:3645-3647
    • (1985) J Immunol , vol.135 , pp. 3645-3647
    • Ramadori, G.1    Sipe, J.D.2    Colten, H.R.3
  • 5
    • 0023608317 scopus 로고
    • Regulation of acute phase gene expression by inflammatory mediators
    • Fey GH, Fuller GM. Regulation of acute phase gene expression by inflammatory mediators. Mol Biol Med 1987;4:323-338
    • (1987) Mol Biol Med , vol.4 , pp. 323-338
    • Fey, G.H.1    Fuller, G.M.2
  • 6
    • 0025033030 scopus 로고
    • The acute phase response of the liver in inflammation
    • Fey GH, Gauldie J. The acute phase response of the liver in inflammation. Prog Liver Dis 1990;9:89-116
    • (1990) Prog Liver Dis , vol.9 , pp. 89-116
    • Fey, G.H.1    Gauldie, J.2
  • 7
    • 0000619771 scopus 로고
    • Definition and classification of acute phase proteins
    • Gordon AH, Koj A, eds. Amsterdam: Elsevier
    • Koj A. Definition and classification of acute phase proteins. In: Gordon AH, Koj A, eds. The Acute Phase Response to Injury and Infection. Amsterdam: Elsevier, 1985:139-144
    • (1985) The Acute Phase Response to Injury and Infection , pp. 139-144
    • Koj, A.1
  • 8
    • 0002798521 scopus 로고    scopus 로고
    • Acute phase reactants - Their synthesis, turnover and biological significance
    • Allison AC, ed. New York: Plenum
    • Koj A. Acute phase reactants - Their synthesis, turnover and biological significance. In: Allison AC, ed. Structure and Function of Plasma Proteins. Vol 1. New York: Plenum, 1997: 73-131
    • (1997) Structure and Function of Plasma Proteins , vol.1 , pp. 73-131
    • Koj, A.1
  • 9
    • 0022387743 scopus 로고
    • Pretranslational modulation of acute phase hepatic protein synthesis by murine recombinant interleukin-1 (IL-1) and purified human IL-1
    • Ramadori G, Sipe JD, Dinarello CA, et al. Pretranslational modulation of acute phase hepatic protein synthesis by murine recombinant interleukin-1 (IL-1) and purified human IL-1. J Exp Med 1985;162:930-942
    • (1985) J Exp Med , vol.162 , pp. 930-942
    • Ramadori, G.1    Sipe, J.D.2    Dinarello, C.A.3
  • 10
    • 0023432812 scopus 로고
    • Interferon beta 2/B-cell stimulatory factor type 2 shares identity with monocyte-derived hepatocyte-stimulating factor and regulates the major acute phase protein response in liver cells
    • Gauldie J, Richards C, Harnish D, et al. Interferon beta 2/B-cell stimulatory factor type 2 shares identity with monocyte-derived hepatocyte-stimulating factor and regulates the major acute phase protein response in liver cells. Proc Natl Acad Sci USA 1987;84:7251-7255
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 7251-7255
    • Gauldie, J.1    Richards, C.2    Harnish, D.3
  • 11
    • 0023880660 scopus 로고
    • Action of recombinant human interleukin 6, interleukin 1 beta and tumor necrosis factor alpha on the mRNA induction of acute-phase proteins
    • Andus T, Geiger T, Hirano T, et al. Action of recombinant human interleukin 6, interleukin 1 beta and tumor necrosis factor alpha on the mRNA induction of acute-phase proteins. Eur J Immunol 1988;18:739-746
    • (1988) Eur J Immunol , vol.18 , pp. 739-746
    • Andus, T.1    Geiger, T.2    Hirano, T.3
  • 12
    • 0024581491 scopus 로고
    • Interleukin-6 is the major regulator of acute phase protein synthesis in adult human hepatocytes
    • Castell JV, Gomez-Lechon MJ, David M, et al. Interleukin-6 is the major regulator of acute phase protein synthesis in adult human hepatocytes. FEBS Lett 1989;242:237-239
    • (1989) FEBS Lett , vol.242 , pp. 237-239
    • Castell, J.V.1    Gomez-Lechon, M.J.2    David, M.3
  • 13
    • 0023778137 scopus 로고
    • Interleukin 6 the third mediator of acute phase reaction, modulates hepatic protein synthesis in human and mouse. Comparison with interleukin 1β and tumor necrosis factor α
    • Ramadori G, Van Damme J, Rieder H, Meyer zum Büschenfelde KH. Interleukin 6 the third mediator of acute phase reaction, modulates hepatic protein synthesis in human and mouse. Comparison with interleukin 1β and tumor necrosis factor α. Eur J Immunol 1988;8:1259-1264
    • (1988) Eur J Immunol , vol.8 , pp. 1259-1264
    • Ramadori, G.1    Van Damme, J.2    Rieder, H.3    Meyer Zum Büschenfelde, K.H.4
  • 14
    • 0023941157 scopus 로고
    • Interaction of recombinant IL-1 and recombinant tumor necrosis factor in the induction of mouse acute phase proteins
    • Mortensen RF, Shapiro J, Lin BF, et al. Interaction of recombinant IL-1 and recombinant tumor necrosis factor in the induction of mouse acute phase proteins. J Immunol 1988;140:2260-2266
    • (1988) J Immunol , vol.140 , pp. 2260-2266
    • Mortensen, R.F.1    Shapiro, J.2    Lin, B.F.3
  • 16
    • 0031963046 scopus 로고    scopus 로고
    • The pathophysiologic roles of interleukin-6 in human diseases
    • Dimitris A, Papanicolau, Wilder RL, et al. The pathophysiologic roles of interleukin-6 in human diseases. Ann Intern Med 1998;128:127-137
    • (1998) Ann Intern Med , vol.128 , pp. 127-137
    • Dimitris, A.1    Papanicolau2    Wilder, R.L.3
  • 17
    • 0027973688 scopus 로고
    • Integration of function in the hepatic acinus: Intercellular communication in neural and humoral control of liver metabolism
    • Püschel G, Jungermann K. Integration of function in the hepatic acinus: Intercellular communication in neural and humoral control of liver metabolism. Prog Liv Dis 1994;12:19-46
    • (1994) Prog Liv Dis , vol.12 , pp. 19-46
    • Püschel, G.1    Jungermann, K.2
  • 18
    • 0027480233 scopus 로고
    • Characterization of interleukin-1 and interleukin-6 production by hepatic endothelial cells and macrophages
    • Feder LS, Todaro JA, Laskin DL. Characterization of interleukin-1 and interleukin-6 production by hepatic endothelial cells and macrophages. J Leukoc Biol 1993;53:126-132
    • (1993) J Leukoc Biol , vol.53 , pp. 126-132
    • Feder, L.S.1    Todaro, J.A.2    Laskin, D.L.3
  • 19
    • 85069255088 scopus 로고
    • Biologically active products of stimulated liver macrophages (Kupffer cells)
    • Decker K. Biologically active products of stimulated liver macrophages (Kupffer cells). Eur J Biochem 1990;11:367-373
    • (1990) Eur J Biochem , vol.11 , pp. 367-373
    • Decker, K.1
  • 20
    • 84936915523 scopus 로고
    • Hepatic intercellular communication in shock and inflammation
    • Clemens MG, Bauer M, Gingalewski C, et al. Hepatic intercellular communication in shock and inflammation. Shock 1994;2:1-9
    • (1994) Shock , vol.2 , pp. 1-9
    • Clemens, M.G.1    Bauer, M.2    Gingalewski, C.3
  • 21
    • 0028927057 scopus 로고
    • Hepatocyte-derived interleukin-6 and tumor-necrosis factor alpha mediate the lipopolysaccharide-induced acute-phase response and nitric oxide release by cultured rat hepatocytes
    • Saad B, Frei K, Scholl FA, et al. Hepatocyte-derived interleukin-6 and tumor-necrosis factor alpha mediate the lipopolysaccharide-induced acute-phase response and nitric oxide release by cultured rat hepatocytes. Eur J Biochem 1995;229:349-355
    • (1995) Eur J Biochem , vol.229 , pp. 349-355
    • Saad, B.1    Frei, K.2    Scholl, F.A.3
  • 22
    • 0030882523 scopus 로고    scopus 로고
    • Human hepatocytes express an array of proinflammatory cytokines after agonist stimulation or bacterial invasion
    • Rowell DL, Eckmann L, Dwinell MB, et al. Human hepatocytes express an array of proinflammatory cytokines after agonist stimulation or bacterial invasion. Am J Physiol 1997;273:G322-G332
    • (1997) Am J Physiol , vol.273
    • Rowell, D.L.1    Eckmann, L.2    Dwinell, M.B.3
  • 23
    • 0026834564 scopus 로고
    • Hepatic fibrogenesis: The puzzle of interacting cells, fibrogenic cytokines, regulatory loops, and extracellular matrix molecules
    • Gressner AM. Hepatic fibrogenesis: The puzzle of interacting cells, fibrogenic cytokines, regulatory loops, and extracellular matrix molecules. Z Gastroenterol 1992;30:5-16
    • (1992) Z Gastroenterol , vol.30 , pp. 5-16
    • Gressner, A.M.1
  • 24
    • 0026651763 scopus 로고
    • Alternative splicing products of the tenascin gene distinguish rat liver fat storing cells from arterial smooth muscle cells and skin fibroblasts
    • Schwögler S, Odenthal M, Meyer-zum-Buschenfelde KH, Ramadori G. Alternative splicing products of the tenascin gene distinguish rat liver fat storing cells from arterial smooth muscle cells and skin fibroblasts. Biochem Biophys Res Commun 1992;185:768-775
    • (1992) Biochem Biophys Res Commun , vol.185 , pp. 768-775
    • Schwögler, S.1    Odenthal, M.2    Meyer-Zum-Buschenfelde, K.H.3    Ramadori, G.4
  • 25
    • 0028997539 scopus 로고
    • Role of the myofibroblast differentiation during liver fibrosis
    • Desmouliere A, Tuchweber B, Gabbiani G. Role of the myofibroblast differentiation during liver fibrosis. J Hepatol 1995; 22:61-64
    • (1995) J Hepatol , vol.22 , pp. 61-64
    • Desmouliere, A.1    Tuchweber, B.2    Gabbiani, G.3
  • 26
    • 0030967254 scopus 로고    scopus 로고
    • Mast cells distribution in human liver disease and experimental rat liver fibrosis. Indications for mast cell participation in development of liver fibrosis
    • Armbrust T, Batusic D, Ringe B, Ramadori G. Mast cells distribution in human liver disease and experimental rat liver fibrosis. Indications for mast cell participation in development of liver fibrosis. J Hepatol 1997;26:1042-1054
    • (1997) J Hepatol , vol.26 , pp. 1042-1054
    • Armbrust, T.1    Batusic, D.2    Ringe, B.3    Ramadori, G.4
  • 27
    • 0031018997 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases in liver fibrosis
    • Iredale JP. Tissue inhibitors of metalloproteinases in liver fibrosis. Int J Biochem Cell Biol 1997;29:43-54
    • (1997) Int J Biochem Cell Biol , vol.29 , pp. 43-54
    • Iredale, J.P.1
  • 28
    • 0030762368 scopus 로고    scopus 로고
    • 4-treated rats by the weekly induction of acute phase response episodes: Upregulation of α1(I) procollagen and tissue inhibitor of metalloproteinase-1 mRNAs
    • 4-treated rats by the weekly induction of acute phase response episodes: Upregulation of α1(I) procollagen and tissue inhibitor of metalloproteinase-1 mRNAs. Biochim Biophys Acta 1997;1361:177-184
    • (1997) Biochim Biophys Acta , vol.1361 , pp. 177-184
    • Greenwel, P.1    Rojkind, M.2
  • 29
    • 0028985793 scopus 로고
    • Zonation of metabolism and gene expression in liver
    • Jungermann K. Zonation of metabolism and gene expression in liver. Histochem Cell Biol 1995;103:81-91
    • (1995) Histochem Cell Biol , vol.103 , pp. 81-91
    • Jungermann, K.1
  • 30
    • 0029800090 scopus 로고    scopus 로고
    • Zonation of parenchymal and non-parenchymal metabolism in liver
    • Jungermann K, Kietzmann T. Zonation of parenchymal and non-parenchymal metabolism in liver. Annu Rev Nutr 1996;16: 179-203
    • (1996) Annu Rev Nutr , vol.16 , pp. 179-203
    • Jungermann, K.1    Kietzmann, T.2
  • 31
    • 0027056698 scopus 로고
    • Functional hepatocellular heterogeneity for the production of plasma proteins
    • Feldmann G, Scoazec JY, Racine L, Bernuau D. Functional hepatocellular heterogeneity for the production of plasma proteins. Enzyme 1992;46:139-154
    • (1992) Enzyme , vol.46 , pp. 139-154
    • Feldmann, G.1    Scoazec, J.Y.2    Racine, L.3    Bernuau, D.4
  • 33
    • 0025190892 scopus 로고
    • Interleukin-6 and the acute phase response
    • Heinrich PC, Castell JV, Andus T. Interleukin-6 and the acute phase response. Biochem J 1990;265:621-636
    • (1990) Biochem J , vol.265 , pp. 621-636
    • Heinrich, P.C.1    Castell, J.V.2    Andus, T.3
  • 34
    • 0028845574 scopus 로고
    • Parenchymal and non-parenchymal liver cells and their interaction in the local immune response
    • Knolle P, Löhr H, Treichel U, et al. Parenchymal and non-parenchymal liver cells and their interaction in the local immune response. Z Gastroenterol 1995;33:613-620
    • (1995) Z Gastroenterol , vol.33 , pp. 613-620
    • Knolle, P.1    Löhr, H.2    Treichel, U.3
  • 36
    • 0024529891 scopus 로고
    • The complex pattern of cytokines in serum from patients with meningococcal septic shock. Association between interleukin 6, interleukin 1, and fatal outcome
    • Waage A, Brandtzaeg P, Halstensen A, et al. The complex pattern of cytokines in serum from patients with meningococcal septic shock. Association between interleukin 6, interleukin 1, and fatal outcome. J Exp Med 1989;169:333-338
    • (1989) J Exp Med , vol.169 , pp. 333-338
    • Waage, A.1    Brandtzaeg, P.2    Halstensen, A.3
  • 37
    • 0029831553 scopus 로고    scopus 로고
    • Interleukin 6 in the injured patient. Marker of injury or mediator of inflammation?
    • Biffl WL, Moore EE, Moore FA, Peterson VM. Interleukin 6 in the injured patient. Marker of injury or mediator of inflammation? Ann Surg 1996;224:647-664
    • (1996) Ann Surg , vol.224 , pp. 647-664
    • Biffl, W.L.1    Moore, E.E.2    Moore, F.A.3    Peterson, V.M.4
  • 38
    • 0028840191 scopus 로고
    • Viable rat Kupffer cells synthesize but not secrete Interleukin-1 - Indications for necrosis-induced maturation of Interleukin-1α, but not of Interleukin-1β
    • Armbrust T, Schmitt E, Ramadori G. Viable rat Kupffer cells synthesize but not secrete Interleukin-1 - Indications for necrosis-induced maturation of Interleukin-1α, but not of Interleukin-1β. Biochem Biophys Res Commun 1995;207:637-645
    • (1995) Biochem Biophys Res Commun , vol.207 , pp. 637-645
    • Armbrust, T.1    Schmitt, E.2    Ramadori, G.3
  • 39
    • 0028175838 scopus 로고
    • Interleukin 1β maturation and release in response to ATP and nigericin. Evidence that potassium depletion mediated by these agents is a necessary and common feature of their activity
    • Perregaux D, Gabel ChA. Interleukin 1β maturation and release in response to ATP and nigericin. Evidence that potassium depletion mediated by these agents is a necessary and common feature of their activity. J Biol Chem 1994;269:15195-15203
    • (1994) J Biol Chem , vol.269 , pp. 15195-15203
    • Perregaux, D.1    Gabel, Ch.A.2
  • 40
    • 0032031392 scopus 로고    scopus 로고
    • Post-translational processing of murine IL-1: Evidence that ATP-induced release of IL-1α and IL-1β occurs via a similar mechanism
    • Perregaux DG, Gabel ChA. Post-translational processing of murine IL-1: Evidence that ATP-induced release of IL-1α and IL-1β occurs via a similar mechanism. J Immunol 1998;160: 2469-2477
    • (1998) J Immunol , vol.160 , pp. 2469-2477
    • Perregaux, D.G.1    Gabel, C.2
  • 41
    • 0030952139 scopus 로고    scopus 로고
    • Induction of interleukin-1 and interleukin-1 receptor antagonist
    • Dinarello CA. Induction of interleukin-1 and interleukin-1 receptor antagonist. Semin Oncol 1997;24:S9-81-S9-93
    • (1997) Semin Oncol , vol.24
    • Dinarello, C.A.1
  • 43
    • 0027469531 scopus 로고
    • Reconstitution of the response to leukemia inhibitory factor, oncostatin M, and ciliary neurotrophic factor in hepatoma cells
    • Baumann H, Ziegler SF, Mosley B, et al. Reconstitution of the response to leukemia inhibitory factor, oncostatin M, and ciliary neurotrophic factor in hepatoma cells. J Biol Chcm 1993;268: 8414-8417
    • (1993) J Biol Chcm , vol.268 , pp. 8414-8417
    • Baumann, H.1    Ziegler, S.F.2    Mosley, B.3
  • 44
    • 0029084805 scopus 로고
    • Interleukin-6 family of cytokines and gp110
    • Kishimoto T, Akira S, Narazaki M, Taga-T. Interleukin-6 family of cytokines and gp110. Blood 1995;86:1243-1254
    • (1995) Blood , vol.86 , pp. 1243-1254
    • Kishimoto, T.1    Akira, S.2    Narazaki, M.3
  • 45
    • 0030045122 scopus 로고    scopus 로고
    • IL-6 cytokine family and signal transduction: A model of the cytokine system
    • Hibi M, Nukujima K, Hirano T. IL-6 cytokine family and signal transduction: A model of the cytokine system. J Mol Med 1996;74:1-12
    • (1996) J Mol Med , vol.74 , pp. 1-12
    • Hibi, M.1    Nukujima, K.2    Hirano, T.3
  • 46
    • 0027135969 scopus 로고
    • Divergent transforming growth factor-beta effects on IL-6 regulation of acute phase plasma proteins in rat hepatoma cells
    • Campos SP, Wang Y, Koj A, Baumann H. Divergent transforming growth factor-beta effects on IL-6 regulation of acute phase plasma proteins in rat hepatoma cells. J Immunol 1993;151: 7128-7137
    • (1993) J Immunol , vol.151 , pp. 7128-7137
    • Campos, S.P.1    Wang, Y.2    Koj, A.3    Baumann, H.4
  • 47
    • 0026458152 scopus 로고
    • Synthesis of tissue inhibitor of metalloproteinase-1 (TIMP-1) in human hepatoma cells (HepG2). Up-regulation by interleukin-6 and transforming growth factor beta 1
    • Kordula T, Guttgemann I, Rose-John S, et al. Synthesis of tissue inhibitor of metalloproteinase-1 (TIMP-1) in human hepatoma cells (HepG2). Up-regulation by interleukin-6 and transforming growth factor beta 1. FEBS Lett 1992;313:143-147
    • (1992) FEBS Lett , vol.313 , pp. 143-147
    • Kordula, T.1    Guttgemann, I.2    Rose-John, S.3
  • 48
    • 0029905271 scopus 로고    scopus 로고
    • The hepatocyle growth factor regulates the synthesis of acute-phase proteins in human hepatocytes: Divergent effect on interleukin-6-stimulated genes
    • Guillen MI, Gomez-Lechon MJ, Nakamura T, Castell JV. The hepatocyle growth factor regulates the synthesis of acute-phase proteins in human hepatocytes: Divergent effect on interleukin-6-stimulated genes. Hepatology 1996;23:1345-1352
    • (1996) Hepatology , vol.23 , pp. 1345-1352
    • Guillen, M.I.1    Gomez-Lechon, M.J.2    Nakamura, T.3    Castell, J.V.4
  • 49
    • 0030890352 scopus 로고    scopus 로고
    • Hepatocyte growth factor/scatter factor (HGF/SF) signals via the STAT3/ APRF transcription factor in human hepatoma cells and hepatocytes
    • Schaper F, Siewert E, Gomez-Lechon MJ, et al. Hepatocyte growth factor/scatter factor (HGF/SF) signals via the STAT3/ APRF transcription factor in human hepatoma cells and hepatocytes. FEBS Lett 1997;405:99-103
    • (1997) FEBS Lett , vol.405 , pp. 99-103
    • Schaper, F.1    Siewert, E.2    Gomez-Lechon, M.J.3
  • 50
    • 0030920217 scopus 로고    scopus 로고
    • Leptin receptor action in hepatic cells
    • Wang Y, Kuropatwinski KK, White DW, et al. Leptin receptor action in hepatic cells. J Biol Chem 1997;272:16216-16223
    • (1997) J Biol Chem , vol.272 , pp. 16216-16223
    • Wang, Y.1    Kuropatwinski, K.K.2    White, D.W.3
  • 51
    • 0022973587 scopus 로고
    • Transcriptional regulation of plasma protein synthesis during inflammation
    • Birch HE, Schreiber G. Transcriptional regulation of plasma protein synthesis during inflammation. J Biol Chem 1986;261: 8077-8080
    • (1986) J Biol Chem , vol.261 , pp. 8077-8080
    • Birch, H.E.1    Schreiber, G.2
  • 52
    • 0023228969 scopus 로고
    • Transcriptional regulation of genes encoding the acute-phase proteins CRP, SAA, and C3
    • Goldberger G, Bing DH, Sipe JD, et al. Transcriptional regulation of genes encoding the acute-phase proteins CRP, SAA, and C3. J Immunol 1987;138:3967-3971
    • (1987) J Immunol , vol.138 , pp. 3967-3971
    • Goldberger, G.1    Bing, D.H.2    Sipe, J.D.3
  • 53
    • 0023880660 scopus 로고
    • Action of recombinant human interleukin 6, interleukin 1 beta and tumor necrosis factor alpha on the mRNA induction of acute-phase proteins
    • Andus T, Geiger T, Hirano T, et al. Action of recombinant human interleukin 6, interleukin 1 beta and tumor necrosis factor alpha on the mRNA induction of acute-phase proteins. Eur J Immunol 1988;18:739-746
    • (1988) Eur J Immunol , vol.18 , pp. 739-746
    • Andus, T.1    Geiger, T.2    Hirano, T.3
  • 54
    • 0024245610 scopus 로고
    • Recombinant interleukin 6 regulates the transcriptional activation of a set of human acute phase genes
    • Morronc G, Ciliberto G, Oliviero S, et al. Recombinant interleukin 6 regulates the transcriptional activation of a set of human acute phase genes. J Biol Chem 1988;263:12554-12558
    • (1988) J Biol Chem , vol.263 , pp. 12554-12558
    • Morronc, G.1    Ciliberto, G.2    Oliviero, S.3
  • 55
    • 0031006421 scopus 로고    scopus 로고
    • Cytokines and the hepatic acute phase response
    • Moshage H. Cytokines and the hepatic acute phase response. J Pathol 1997;181:257-266
    • (1997) J Pathol , vol.181 , pp. 257-266
    • Moshage, H.1
  • 56
    • 0025307891 scopus 로고
    • Biosynthesis of lipopolysaccharide-binding protein in rabbit hepatocyies
    • Ramadori G, Meyer zum Büschenfelde KH, Tobias PS, et al. Biosynthesis of lipopolysaccharide-binding protein in rabbit hepatocyies. Pathobiology 1990;58:89-94
    • (1990) Pathobiology , vol.58 , pp. 89-94
    • Ramadori, G.1    Meyer Zum Büschenfelde, K.H.2    Tobias, P.S.3
  • 57
    • 0025759220 scopus 로고
    • Major component of RA-reactive factor, a complement activating bactericidal protein in mouse serum
    • Ihara S, Takahashi A, Hatsuse H, et al. Major component of RA-reactive factor, a complement activating bactericidal protein in mouse serum. J Immunol 1991;146:1874-1879
    • (1991) J Immunol , vol.146 , pp. 1874-1879
    • Ihara, S.1    Takahashi, A.2    Hatsuse, H.3
  • 58
    • 0030794868 scopus 로고    scopus 로고
    • The complement-activating protease P100 is expressed by hepatocytes and is induced by IL-6 in vitro and during the acute phase reaction in vivo
    • Knittel Th, Fellmer P, Neubauer K, et al. The complement-activating protease P100 is expressed by hepatocytes and is induced by IL-6 in vitro and during the acute phase reaction in vivo. Lab Invest 1997;77:221-230
    • (1997) Lab Invest , vol.77 , pp. 221-230
    • Knittel, Th.1    Fellmer, P.2    Neubauer, K.3
  • 59
    • 0024554679 scopus 로고
    • Regulation of plasma acute-phase protein and albumin levels in the liver of scalded rats
    • Sevaljevic L, Ivanovic MS, Petrovic M, et al. Regulation of plasma acute-phase protein and albumin levels in the liver of scalded rats. Biochem J 1989;258:663-668
    • (1989) Biochem J , vol.258 , pp. 663-668
    • Sevaljevic, L.1    Ivanovic, M.S.2    Petrovic, M.3
  • 60
    • 0024992594 scopus 로고
    • Gene expression in regenerating and acute-phase rat liver
    • Milland J, Tsykin A, Thomas T, et al. Gene expression in regenerating and acute-phase rat liver. Am J Physiol 1990;259: G340-G347
    • (1990) Am J Physiol , vol.259
    • Milland, J.1    Tsykin, A.2    Thomas, T.3
  • 61
    • 0030761483 scopus 로고    scopus 로고
    • Interleukin-6 downregulates factor XII production by human hepatoma cell line (HepG2)
    • Citarella F, Felici A, Brouwer M, et al. Interleukin-6 downregulates factor XII production by human hepatoma cell line (HepG2). Blood 1997;90:1501-1507
    • (1997) Blood , vol.90 , pp. 1501-1507
    • Citarella, F.1    Felici, A.2    Brouwer, M.3
  • 62
    • 0024801396 scopus 로고
    • Post-transcriptional control of negative acute phase genes by transforming growth factor beta
    • Morrone G, Cortese R, Sorrentino V. Post-transcriptional control of negative acute phase genes by transforming growth factor beta. EMBO J 1989;8:3767-3771
    • (1989) EMBO J , vol.8 , pp. 3767-3771
    • Morrone, G.1    Cortese, R.2    Sorrentino, V.3
  • 63
    • 0029113729 scopus 로고
    • Discordant regulation of proteins of cholesterol metabolism during the acute phase response
    • Feingold KR, Pollock AS, Moser AH, et al. Discordant regulation of proteins of cholesterol metabolism during the acute phase response. J Lipid Res 1995;36:1474-1482
    • (1995) J Lipid Res , vol.36 , pp. 1474-1482
    • Feingold, K.R.1    Pollock, A.S.2    Moser, A.H.3
  • 64
    • 0029988591 scopus 로고    scopus 로고
    • Endotoxemia in rats is associated with induction of the P4504A subfamily and suppression of several other forms of cytochrome P450
    • Sewer MB, Koop DR, Morgan ET. Endotoxemia in rats is associated with induction of the P4504A subfamily and suppression of several other forms of cytochrome P450. Drug Metab Dispos 1996;24:401-407
    • (1996) Drug Metab Dispos , vol.24 , pp. 401-407
    • Sewer, M.B.1    Koop, D.R.2    Morgan, E.T.3
  • 65
    • 0028135570 scopus 로고
    • Selective suppression of cytochrome P-450 gene expression by interleukins 1 and 6 in rat liver
    • Morgan ET, Thomas KB, Swanson R, et al. Selective suppression of cytochrome P-450 gene expression by interleukins 1 and 6 in rat liver. Biochim Biophys Acta 1994;1219:475-483
    • (1994) Biochim Biophys Acta , vol.1219 , pp. 475-483
    • Morgan, E.T.1    Thomas, K.B.2    Swanson, R.3
  • 66
    • 0030974473 scopus 로고    scopus 로고
    • Modulation of glutathione S-transferase subunits A2, M1, and P1 expression by interleukin-1beta in rat hepatocytes in primary culture
    • Maheo K, Antras-Ferry J, Morel F, et al. Modulation of glutathione S-transferase subunits A2, M1, and P1 expression by interleukin-1beta in rat hepatocytes in primary culture. J Biol Chem 1997;272:16125-16132
    • (1997) J Biol Chem , vol.272 , pp. 16125-16132
    • Maheo, K.1    Antras-Ferry, J.2    Morel, F.3
  • 67
    • 0025934803 scopus 로고
    • Altered transcriptional regulation of phosphoenolpyruvate carboxykinase in rats following endotoxin treatment
    • Hill M, McCallum R. Altered transcriptional regulation of phosphoenolpyruvate carboxykinase in rats following endotoxin treatment. J Clin Invest 1991;88:811-816
    • (1991) J Clin Invest , vol.88 , pp. 811-816
    • Hill, M.1    McCallum, R.2
  • 68
    • 0026768040 scopus 로고
    • Identification of tumor necrosis factor as a transcriptional regulator of the phosphoenolpyruvate carboxykinase gene following endotoxin treatment of mice
    • Hill MR, McCallum RE. Identification of tumor necrosis factor as a transcriptional regulator of the phosphoenolpyruvate carboxykinase gene following endotoxin treatment of mice. Infect Immun 1992;60:4040-4050
    • (1992) Infect Immun , vol.60 , pp. 4040-4050
    • Hill, M.R.1    McCallum, R.E.2
  • 69
    • 0028152932 scopus 로고
    • Inhibition by recombinant human interleukin-6 of the glucagon-dependent induction of phosphoenolpyruvate carboxykinase and of the insulin-dependent induction of glucokinase gene expression in cultured rat hepatocytes: Regulation of gene transcription and messenger RNA degradation
    • Christ B, Nath A, Heinrich PC, Jungermann K. Inhibition by recombinant human interleukin-6 of the glucagon-dependent induction of phosphoenolpyruvate carboxykinase and of the insulin-dependent induction of glucokinase gene expression in cultured rat hepatocytes: Regulation of gene transcription and messenger RNA degradation. Hepatology 1994;20:1577-1583
    • (1994) Hepatology , vol.20 , pp. 1577-1583
    • Christ, B.1    Nath, A.2    Heinrich, P.C.3    Jungermann, K.4
  • 70
    • 0030981553 scopus 로고    scopus 로고
    • Mechanism of the impairment of the glucagon-stimulated phosphoenolpyruvate carboxykinase gene expression by interleukin-6 in cultured rat hepatocytes: Inhibition of the increase in cyclic 3′,5′ adenosine monophosphate and the downstream cyclic 3′,5′ adenosine monophosphate action
    • Christ B, Nath A, Jungermann K. Mechanism of the impairment of the glucagon-stimulated phosphoenolpyruvate carboxykinase gene expression by interleukin-6 in cultured rat hepatocytes: Inhibition of the increase in cyclic 3′,5′ adenosine monophosphate and the downstream cyclic 3′,5′ adenosine monophosphate action. Hepatology 1997;26:73-80
    • (1997) Hepatology , vol.26 , pp. 73-80
    • Christ, B.1    Nath, A.2    Jungermann, K.3
  • 71
    • 0029826073 scopus 로고    scopus 로고
    • Impairment by interleukin 1 beta and tumour necrosis factor alpha of the glucagon-induced increase in phosphoenolpyruvate carboxykinase gene expression and gluconeogenesis in cultured rat hepatocytes
    • published erratum appears in Biochem J 1997;321:903
    • Christ B, Nath A. Impairment by interleukin 1 beta and tumour necrosis factor alpha of the glucagon-induced increase in phosphoenolpyruvate carboxykinase gene expression and gluconeogenesis in cultured rat hepatocytes [published erratum appears in Biochem J 1997;321:903]. Biochem J 1996;320:161-166
    • (1996) Biochem J , vol.320 , pp. 161-166
    • Christ, B.1    Nath, A.2
  • 72
    • 0024213958 scopus 로고
    • Nutritional aspects of leukocytic cytokines
    • Klasing KC. Nutritional aspects of leukocytic cytokines. J Nutr 1988;118:1436-1446
    • (1988) J Nutr , vol.118 , pp. 1436-1446
    • Klasing, K.C.1
  • 73
    • 0026021473 scopus 로고
    • Effects of cytokines on the liver
    • Andus T, Bauer G, Gerok W. Effects of cytokines on the liver. Hepatology 1991;13:364-375
    • (1991) Hepatology , vol.13 , pp. 364-375
    • Andus, T.1    Bauer, G.2    Gerok, W.3
  • 75
    • 0000845334 scopus 로고
    • Synthesis, processing and secretion of plasma proteins by the liver and other organs and their regulation
    • Putnam FW, ed. Vol. 5. San Diego: Academic Press
    • Schreiber G. Synthesis, processing and secretion of plasma proteins by the liver and other organs and their regulation. In: The Plasma Proteins. Putnam FW, ed. Vol. 5. San Diego: Academic Press, 1987;5:293-363
    • (1987) The Plasma Proteins , vol.5 , pp. 293-363
    • Schreiber, G.1
  • 76
    • 0021933552 scopus 로고
    • Monokines and the metabolic pathophysiology of septic shock
    • Filkins JP. Monokines and the metabolic pathophysiology of septic shock. Fed Proc 1985;44:300-304
    • (1985) Fed Proc , vol.44 , pp. 300-304
    • Filkins, J.P.1
  • 78
    • 0028878281 scopus 로고
    • Alterations in carbohydrate metabolism during stress: A review of the literature
    • Mizock BA. Alterations in carbohydrate metabolism during stress: A review of the literature. Am J Med 1995;98:75-84
    • (1995) Am J Med , vol.98 , pp. 75-84
    • Mizock, B.A.1
  • 79
    • 0030013088 scopus 로고    scopus 로고
    • The inflammatory response in interleukin-1 beta-deficient mice: Comparison with other cytokine-related knock-out mice
    • Fantuzzi G, Dinarello CA. The inflammatory response in interleukin-1 beta-deficient mice: Comparison with other cytokine-related knock-out mice. J Leukoc Biol 1996;59:489-493
    • (1996) J Leukoc Biol , vol.59 , pp. 489-493
    • Fantuzzi, G.1    Dinarello, C.A.2
  • 80
    • 0028328436 scopus 로고
    • Impaired immune and acute-phase responses in interleukin-6-deficient mice
    • Kopf M, Baumann H, Freer G, et al. Impaired immune and acute-phase responses in interleukin-6-deficient mice. Nature 1994;368:339-342
    • (1994) Nature , vol.368 , pp. 339-342
    • Kopf, M.1    Baumann, H.2    Freer, G.3
  • 81
    • 0028169379 scopus 로고
    • Response of interleukin-6-deficient mice to tumor necrosis factor-induced metabolic changes and lethality
    • Libert C, Takahashi N, Cauwels A, et al. Response of interleukin-6-deficient mice to tumor necrosis factor-induced metabolic changes and lethality. Eur J Immunol 1994;24:2237-2242
    • (1994) Eur J Immunol , vol.24 , pp. 2237-2242
    • Libert, C.1    Takahashi, N.2    Cauwels, A.3
  • 82
    • 0027984754 scopus 로고
    • Defective inflammatory response in interleukin 6-deficient mice
    • Fattori E, Cappelletti M, Costa P, et al. Defective inflammatory response in interleukin 6-deficient mice. J Exp Med 1994;180: 1243-1250
    • (1994) J Exp Med , vol.180 , pp. 1243-1250
    • Fattori, E.1    Cappelletti, M.2    Costa, P.3
  • 83
    • 0031445985 scopus 로고    scopus 로고
    • Failure of germinal center formation and impairment of response to endotoxin in tumor necrosis factor alpha-deficient mice
    • Taniguchi T, Takata M, Ikeda A, et al. Failure of germinal center formation and impairment of response to endotoxin in tumor necrosis factor alpha-deficient mice. Lab Invest 1997;77:647-658
    • (1997) Lab Invest , vol.77 , pp. 647-658
    • Taniguchi, T.1    Takata, M.2    Ikeda, A.3
  • 84
    • 0031568401 scopus 로고    scopus 로고
    • Response to local inflammation of IL-1β-converting enzyme-deficient mice
    • Fantuzzi Giamilia GKu, Harding MW, Livingston DJ, et al. Response to local inflammation of IL-1β-converting enzyme-deficient mice. J Immunol 1997;158:1818-1824
    • (1997) J Immunol , vol.158 , pp. 1818-1824
    • Fantuzzi Giamilia, G.Ku.1    Harding, M.W.2    Livingston, D.J.3
  • 85
    • 0028984948 scopus 로고
    • Mice devident in IL-1β-converting enzyme are defective in production of mature IL-1β and resistant to endotoxic shock
    • Lip AH, Banerjee S, Franklin S, et al. Mice devident in IL-1β-converting enzyme are defective in production of mature IL-1β and resistant to endotoxic shock. Cell 1995;80:401
    • (1995) Cell , vol.80 , pp. 401
    • Lip, A.H.1    Banerjee, S.2    Franklin, S.3
  • 86
    • 0031252311 scopus 로고    scopus 로고
    • Phenotypic and functional characterization of mice that lack the type I receptor for IL-1
    • Glaccum MB, Stocking KL, Charrier K, et al. Phenotypic and functional characterization of mice that lack the type I receptor for IL-1. J Immunol 1997;159:3364-3371
    • (1997) J Immunol , vol.159 , pp. 3364-3371
    • Glaccum, M.B.1    Stocking, K.L.2    Charrier, K.3
  • 87
    • 0031985413 scopus 로고    scopus 로고
    • TNF receptor-deficient mice reveal divergent roles for p55 and p75 in several models of inflammation
    • Peschon JJ, Torrance DS, Stocking KL, et al. TNF receptor-deficient mice reveal divergent roles for p55 and p75 in several models of inflammation. J Immunol 1998;160:943-952
    • (1998) J Immunol , vol.160 , pp. 943-952
    • Peschon, J.J.1    Torrance, D.S.2    Stocking, K.L.3
  • 88
    • 0031227868 scopus 로고    scopus 로고
    • Absence of IL-1 signaling and reduced inflammatory response in IL-1 type I receptor-deficient mice
    • Labow M, Shuster D, Zetterstrom M, et al. Absence of IL-1 signaling and reduced inflammatory response in IL-1 type I receptor-deficient mice. J Immunol 1997;159:2452-2461
    • (1997) J Immunol , vol.159 , pp. 2452-2461
    • Labow, M.1    Shuster, D.2    Zetterstrom, M.3
  • 89
    • 0030893635 scopus 로고    scopus 로고
    • Exacerbated febrile responses to LPS, but not turpentine, in TNF double receptor-knockout mice
    • Leon LR, Kozak W, Peschon J, Kluger MJ. Exacerbated febrile responses to LPS, but not turpentine, in TNF double receptor-knockout mice. Am J Physiol 1997;272:R563-R569
    • (1997) Am J Physiol , vol.272
    • Leon, L.R.1    Kozak, W.2    Peschon, J.3    Kluger, M.J.4
  • 90
    • 0029414792 scopus 로고
    • Targeted disruption of the IL6 related genes: Gp130 and NF-IL6
    • Akira S, Yoshida K, Tanaka T, et al. Targeted disruption of the IL6 related genes: gp130 and NF-IL6. Immunol Rev 1995; 148:221-235
    • (1995) Immunol Rev , vol.148 , pp. 221-235
    • Akira, S.1    Yoshida, K.2    Tanaka, T.3
  • 91
    • 9044222888 scopus 로고    scopus 로고
    • Targeted disruption of gp130, a common signal transducer for the IL6 family of cytokines, leads to myocardial and hematological disorders
    • Yoshida K, Taga T, Saito M, et al. Targeted disruption of gp130, a common signal transducer for the IL6 family of cytokines, leads to myocardial and hematological disorders. Proc Natl Acad Sci USA 1996;93:407-411
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 407-411
    • Yoshida, K.1    Taga, T.2    Saito, M.3
  • 92
    • 0028226196 scopus 로고
    • Soluble receptors for cytokines and growth factors: Generation and biological function
    • Rose-John S, Heinrich PC. Soluble receptors for cytokines and growth factors: Generation and biological function. Biochem J 1994;300:281-290
    • (1994) Biochem J , vol.300 , pp. 281-290
    • Rose-John, S.1    Heinrich, P.C.2
  • 93
    • 0029863504 scopus 로고    scopus 로고
    • The function of the soluble interleukin 6 ( IL-6) receptor in vivo: Sensitization of human soluble IL-6 receptor transgenic mice towards IL-6 and prolongation of the plasma half-life of IL-6
    • Peters M, Jacobs S, Ehlers M, et al. The function of the soluble interleukin 6 ( IL-6) receptor in vivo: Sensitization of human soluble IL-6 receptor transgenic mice towards IL-6 and prolongation of the plasma half-life of IL-6. J Exp Med 1996;183: 1399-1406
    • (1996) J Exp Med , vol.183 , pp. 1399-1406
    • Peters, M.1    Jacobs, S.2    Ehlers, M.3
  • 94
    • 18244419398 scopus 로고    scopus 로고
    • Extramedullary expansion of hematopoietic progenitor cells in interleukin (IL)-6-sIL-6R double transgenic mice
    • Peters M, Schirmacher P, Goldschmitt J, et al. Extramedullary expansion of hematopoietic progenitor cells in interleukin (IL)-6-sIL-6R double transgenic mice. J Exp Med 1997;185:755-766
    • (1997) J Exp Med , vol.185 , pp. 755-766
    • Peters, M.1    Schirmacher, P.2    Goldschmitt, J.3
  • 96
    • 0025166114 scopus 로고
    • CD14, a receptor for complexes of lipopolysaccharide (LPS) and LPS binding protein
    • Wright SD, Ramos RA, Tobias PS, et al. CD14, a receptor for complexes of lipopolysaccharide (LPS) and LPS binding protein [see comments]. Science 1990;249:1431-1433
    • (1990) Science , vol.249 , pp. 1431-1433
    • Wright, S.D.1    Ramos, R.A.2    Tobias, P.S.3
  • 97
    • 0029522992 scopus 로고
    • Lipopolysaccharide binding protein participation in cellular activation by LPS
    • Su GL, Simmons RL, Wang SC. Lipopolysaccharide binding protein participation in cellular activation by LPS. Crit Rev Immunol 1995;15:201-214
    • (1995) Crit Rev Immunol , vol.15 , pp. 201-214
    • Su, G.L.1    Simmons, R.L.2    Wang, S.C.3
  • 98
    • 0031440937 scopus 로고    scopus 로고
    • Targeted deletion of the lipopolysaccharide (LPS)-binding protein gene leads to profound suppression of LPS responses ex vivo, whereas in vivo responses remain intact
    • Wurfel MM, Monks BG, Ingalls RR, et al. Targeted deletion of the lipopolysaccharide (LPS)-binding protein gene leads to profound suppression of LPS responses ex vivo, whereas in vivo responses remain intact. J Exp Med 1997;186:2051-2056
    • (1997) J Exp Med , vol.186 , pp. 2051-2056
    • Wurfel, M.M.1    Monks, B.G.2    Ingalls, R.R.3
  • 99
    • 0030685133 scopus 로고    scopus 로고
    • Lipopolysaccharide-binding protein is required to combat a murine gram-negative bacterial infection
    • Jack RS, Fan X, Bernheiden M, et al. Lipopolysaccharide-binding protein is required to combat a murine gram-negative bacterial infection. Nature 1997;389:742-745
    • (1997) Nature , vol.389 , pp. 742-745
    • Jack, R.S.1    Fan, X.2    Bernheiden, M.3
  • 100
    • 0031137733 scopus 로고    scopus 로고
    • CD14-dependent and CD14-independent signaling pathways in murine macrophages from normal and CD14 knockout mice stimulated with lipopolysaccharide or taxol
    • Perera PY, Vogel SN, Detore GR, et al. CD14-dependent and CD14-independent signaling pathways in murine macrophages from normal and CD14 knockout mice stimulated with lipopolysaccharide or taxol. J Immunol 1997;158:4422-4429
    • (1997) J Immunol , vol.158 , pp. 4422-4429
    • Perera, P.Y.1    Vogel, S.N.2    Detore, G.R.3
  • 101
    • 0032521268 scopus 로고    scopus 로고
    • The induction of acute phase proteins by lipopolysaccharide uses a novel pathway that is CD14-independent
    • Haziot A, Lin XY, Zhang F, Goyert SM. The induction of acute phase proteins by lipopolysaccharide uses a novel pathway that is CD14-independent. J Immunol 1998;160:2570-2572
    • (1998) J Immunol , vol.160 , pp. 2570-2572
    • Haziot, A.1    Lin, X.Y.2    Zhang, F.3    Goyert, S.M.4
  • 102
    • 0023685762 scopus 로고
    • Cloning and expression of the human interleukin-6 (BSF-2/IFN beta 2) receptor
    • Yamasaki K, Taga T, Hirata Y, et al. Cloning and expression of the human interleukin-6 (BSF-2/IFN beta 2) receptor. Science 1988;241:825-828
    • (1988) Science , vol.241 , pp. 825-828
    • Yamasaki, K.1    Taga, T.2    Hirata, Y.3
  • 103
    • 0025783668 scopus 로고
    • The receptor for ciliary neurotrophic factor
    • Davis S, Aldrich TH, Valenzuela DM, et al. The receptor for ciliary neurotrophic factor. Science 1991;253:59-63
    • (1991) Science , vol.253 , pp. 59-63
    • Davis, S.1    Aldrich, T.H.2    Valenzuela, D.M.3
  • 104
    • 0028075945 scopus 로고
    • Cloning of a murine IL-11 receptor alpha-chain; requirement for gp130 for high affinity binding and signal transduction
    • Hilton DJ, Hilton AA, Raicevic A, et al. Cloning of a murine IL-11 receptor alpha-chain; requirement for gp130 for high affinity binding and signal transduction. EMBO J 1994;13: 4765-4775
    • (1994) EMBO J , vol.13 , pp. 4765-4775
    • Hilton, D.J.1    Hilton, A.A.2    Raicevic, A.3
  • 105
    • 0030868491 scopus 로고    scopus 로고
    • Molecular cloning of rat leukemia inhibitory factor receptor alpha-chain gene and its expression during pregnancy
    • Aikawa J, Ikeda-Naiki S, Ohgane J, Min KS, et al. Molecular cloning of rat leukemia inhibitory factor receptor alpha-chain gene and its expression during pregnancy. Biochim Biophys Acta 1997;1353:266-276
    • (1997) Biochim Biophys Acta , vol.1353 , pp. 266-276
    • Aikawa, J.1    Ikeda-Naiki, S.2    Ohgane, J.3    Min, K.S.4
  • 106
    • 0026506566 scopus 로고
    • The IL-6 signal transducer, gp130: An oncostatin M receptor and affinity converter for the LIF receptor
    • Gearing DP, Comeau MR, Friend DJ, et al. The IL-6 signal transducer, gp130: An oncostatin M receptor and affinity converter for the LIF receptor. Science 1992;255:1434-1437
    • (1992) Science , vol.255 , pp. 1434-1437
    • Gearing, D.P.1    Comeau, M.R.2    Friend, D.J.3
  • 107
    • 12644294970 scopus 로고    scopus 로고
    • Dual oncostatin M (OSM) receptors. Cloning and characterization of an alternative signaling subunit conferring OSM-specific receptor activation
    • Mosley B, De Imus C, Friend D, et al. Dual oncostatin M (OSM) receptors. Cloning and characterization of an alternative signaling subunit conferring OSM-specific receptor activation. J Biol Chem 1996;271:32635-32643
    • (1996) J Biol Chem , vol.271 , pp. 32635-32643
    • Mosley, B.1    De Imus, C.2    Friend, D.3
  • 108
    • 0028301594 scopus 로고
    • Delmastro P, Ciliberto G, Toniatti C, Oncostatin M binds directly to gp130 and behaves as interleukin-6 antagonist on a cell line expressing gp130 but lacking functional oncostatin M receptors
    • Sporeno E, Paonessa G, Salvati AL, et al. Delmastro P, Ciliberto G, Toniatti C, Oncostatin M binds directly to gp130 and behaves as interleukin-6 antagonist on a cell line expressing gp130 but lacking functional oncostatin M receptors. J Biol Chem 1994;269:10991-10995
    • (1994) J Biol Chem , vol.269 , pp. 10991-10995
    • Sporeno, E.1    Paonessa, G.2    Salvati, A.L.3
  • 109
    • 0028241548 scopus 로고
    • Signaling by the cytokine receptor superfamily: JAKs and STATs
    • Ihle JN, Witthuhn BA, Quelle FW, et al. Signaling by the cytokine receptor superfamily: JAKs and STATs. Trends Biochem Sci 1994;19:222-227
    • (1994) Trends Biochem Sci , vol.19 , pp. 222-227
    • Ihle, J.N.1    Witthuhn, B.A.2    Quelle, F.W.3
  • 110
    • 0028946686 scopus 로고
    • Signaling mechanisms through cytokinc receptors that share signal transducing receptor components
    • Taga T, Kishimoto T. Signaling mechanisms through cytokinc receptors that share signal transducing receptor components. Curr Opin Immunol 1995;7:17-23
    • (1995) Curr Opin Immunol , vol.7 , pp. 17-23
    • Taga, T.1    Kishimoto, T.2
  • 111
    • 0030045122 scopus 로고    scopus 로고
    • IL-6 cytokine family and signal transduction: A model for the cytokine system
    • Hibi M, Nakajima K, Hirano T. IL-6 cytokine family and signal transduction: A model for the cytokine system. J Mol Med 1996;74:1-12
    • (1996) J Mol Med , vol.74 , pp. 1-12
    • Hibi, M.1    Nakajima, K.2    Hirano, T.3
  • 112
    • 0028946158 scopus 로고
    • Contribution of STAT SH2 groups to specific interferon signaling by the Jak-STAT pathway
    • Heim MH, Kerr IM, Stark GR, Darnell JE Jr. Contribution of STAT SH2 groups to specific interferon signaling by the Jak-STAT pathway. Science 1995;267:1347-1349
    • (1995) Science , vol.267 , pp. 1347-1349
    • Heim, M.H.1    Kerr, I.M.2    Stark, G.R.3    Darnell J.E., Jr.4
  • 113
    • 0032518375 scopus 로고    scopus 로고
    • Induction of epithelial tubules by growth factor HGF depends on the STAT pathway
    • Boccaccio C, Ando M, Tamagnone L, et al. Induction of epithelial tubules by growth factor HGF depends on the STAT pathway. Nature 1998;391:285-288
    • (1998) Nature , vol.391 , pp. 285-288
    • Boccaccio, C.1    Ando, M.2    Tamagnone, L.3
  • 114
    • 0028848026 scopus 로고
    • In vivo growth hormone treatment rapidly stimulates the tyrosine phosphorylation and activation of Stat3
    • Gronowski AM, Zhong Z, Wen Z, et al. In vivo growth hormone treatment rapidly stimulates the tyrosine phosphorylation and activation of Stat3. Mol Endocrinol 1995;9:171-177
    • (1995) Mol Endocrinol , vol.9 , pp. 171-177
    • Gronowski, A.M.1    Zhong, Z.2    Wen, Z.3
  • 115
    • 0028952414 scopus 로고
    • Activation of acute phase-response factor (APRF)/Stat3 transcription factor by growth hormone
    • Campbell GS, Meyer DJ, Raz R, et al. Activation of acute phase-response factor (APRF)/Stat3 transcription factor by growth hormone. J Biol Chem 1995;270:3974-3979
    • (1995) J Biol Chem , vol.270 , pp. 3974-3979
    • Campbell, G.S.1    Meyer, D.J.2    Raz, R.3
  • 116
    • 0029113153 scopus 로고
    • Receptors for interleukin-3 (IL-3) and growth hormone mediate an IL-6-type transcriptional induction in the presence of JAK2 or STAT3
    • Wang Y, Morella KK, Ripperger J, et al. Receptors for interleukin-3 (IL-3) and growth hormone mediate an IL-6-type transcriptional induction in the presence of JAK2 or STAT3. Blood 1995;86:1671-1679
    • (1995) Blood , vol.86 , pp. 1671-1679
    • Wang, Y.1    Morella, K.K.2    Ripperger, J.3
  • 117
    • 0031436148 scopus 로고    scopus 로고
    • Divergent signaling capacities of the long and short isoforms of the leptin receptor
    • Bjorbaek C, Uotani S, da Silva B, Flier JS. Divergent signaling capacities of the long and short isoforms of the leptin receptor. J Biol Chem 1997;272:32686-32695
    • (1997) J Biol Chem , vol.272 , pp. 32686-32695
    • Bjorbaek, C.1    Uotani, S.2    Da Silva, B.3    Flier, J.S.4
  • 118
    • 0031467631 scopus 로고    scopus 로고
    • Direct effects of leptin on brown and white adipose tissue
    • Siegrist-Kaiser CA, Pauli V, Juge-Aubry CE, et al. Direct effects of leptin on brown and white adipose tissue. J Clin Invest 1997;100:2858-2864
    • (1997) J Clin Invest , vol.100 , pp. 2858-2864
    • Siegrist-Kaiser, C.A.1    Pauli, V.2    Juge-Aubry, C.E.3
  • 119
    • 0028986193 scopus 로고
    • NF-κB: A lesson in family values
    • Thanos T, Maniatis T. NF-κB: A lesson in family values. Cell 1995;80:529-532
    • (1995) Cell , vol.80 , pp. 529-532
    • Thanos, T.1    Maniatis, T.2
  • 120
    • 0028297068 scopus 로고
    • The sphingomyelin pathway in tumor necrosis factor and interleukin-1 signaling
    • Kolesnick R, Golde DW. The sphingomyelin pathway in tumor necrosis factor and interleukin-1 signaling. Cell 1994;77: 325-328
    • (1994) Cell , vol.77 , pp. 325-328
    • Kolesnick, R.1    Golde, D.W.2
  • 121
    • 0028076002 scopus 로고
    • The role of diacylglycerol and ceramide in tumor necrosis factor and interleukin-1 signal transduction
    • Schülze S, Machleidt T, Krönke M. The role of diacylglycerol and ceramide in tumor necrosis factor and interleukin-1 signal transduction. J Leukoc Biol 1994;56:533-541
    • (1994) J Leukoc Biol , vol.56 , pp. 533-541
    • Schülze, S.1    Machleidt, T.2    Krönke, M.3
  • 122
    • 0029900295 scopus 로고    scopus 로고
    • The tumor necrosis factor ligand and receptor families
    • Bazzoni F, Beutler B. The tumor necrosis factor ligand and receptor families. N Engl J Med 1996;334:1717-1725
    • (1996) N Engl J Med , vol.334 , pp. 1717-1725
    • Bazzoni, F.1    Beutler, B.2
  • 123
    • 0030033193 scopus 로고    scopus 로고
    • Transducers of life and death: TNF receptor superfamily and associated proteins
    • Baker SJ, Premkumar Reddy E. Transducers of life and death: TNF receptor superfamily and associated proteins. Oncogene 1996;12:1-9
    • (1996) Oncogene , vol.12 , pp. 1-9
    • Baker, S.J.1    Premkumar Reddy, E.2
  • 124
    • 0030032106 scopus 로고    scopus 로고
    • TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways
    • Hsu H, Shu HB, Pan MG, Goeddel DV. TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways. Cell 1996;84:299-308
    • (1996) Cell , vol.84 , pp. 299-308
    • Hsu, H.1    Shu, H.B.2    Pan, M.G.3    Goeddel, D.V.4
  • 126
    • 0019992469 scopus 로고
    • Mechanisms of insulin resistance following injury
    • Black PR, Brooks DC, Bessey PQ, et al. Mechanisms of insulin resistance following injury. Ann Surg 1982;196:420-435
    • (1982) Ann Surg , vol.196 , pp. 420-435
    • Black, P.R.1    Brooks, D.C.2    Bessey, P.Q.3
  • 127
    • 0029873406 scopus 로고    scopus 로고
    • Postoperative insulin resistance and circulating concentrations of stress hormones and cytokines
    • Thorell A, Loftenius A, Andersson B, Ljungqvist O. Postoperative insulin resistance and circulating concentrations of stress hormones and cytokines. Clin Nutr 1996;15:75-79
    • (1996) Clin Nutr , vol.15 , pp. 75-79
    • Thorell, A.1    Loftenius, A.2    Andersson, B.3    Ljungqvist, O.4
  • 128
    • 0024451525 scopus 로고
    • Increased plasma IL-6 levels in sepsis
    • Hack CE, DeGroot ER, Felt-Bersma-RJ, et al. Increased plasma IL-6 levels in sepsis. Blood 1989;74:1704-1710
    • (1989) Blood , vol.74 , pp. 1704-1710
    • Hack, C.E.1    DeGroot, E.R.2
  • 129
    • 0025912547 scopus 로고
    • Elevation of serum interleukin-6 concentration precedes acute phase response and reflects severity in acute pancrealitis
    • Leser HG, Gross V, Scheibenhogen C, et al. Elevation of serum interleukin-6 concentration precedes acute phase response and reflects severity in acute pancrealitis. Gastroenterology 1991; 101:782-785
    • (1991) Gastroenterology , vol.101 , pp. 782-785
    • Leser, H.G.1    Gross, V.2    Scheibenhogen, C.3
  • 130
    • 0031871503 scopus 로고    scopus 로고
    • The importance of nitric oxide in the cytokine-induced inhibition of glucose formation by cultured rat hepatocytes incubated with insulin, dexamethasone, and glucagon
    • Ceppi ED, Tithergrade MA. The importance of nitric oxide in the cytokine-induced inhibition of glucose formation by cultured rat hepatocytes incubated with insulin, dexamethasone, and glucagon. Arch Biochem Biophys 1998;349:167-174
    • (1998) Arch Biochem Biophys , vol.349 , pp. 167-174
    • Ceppi, E.D.1    Tithergrade, M.A.2
  • 131
    • 0026634322 scopus 로고
    • Sepsis-induced cascade of cytokine mRNA expression: Correlation with metabolic changes
    • Bycrley LO, Alcock NW, Starnes HFJ. Sepsis-induced cascade of cytokine mRNA expression: Correlation with metabolic changes. Am J Physiol 1992;262:E728-E735
    • (1992) Am J Physiol , vol.262
    • Bycrley, L.O.1    Alcock, N.W.2    Starnes, H.F.J.3
  • 132
    • 0028063370 scopus 로고
    • The paradoxical regulation of protein phosphorylation in insulin action
    • Saltiel AR. The paradoxical regulation of protein phosphorylation in insulin action. FASEB J 1994;8:1034-1040
    • (1994) FASEB J , vol.8 , pp. 1034-1040
    • Saltiel, A.R.1
  • 133
    • 0028085078 scopus 로고
    • The insulin signaling system
    • White MF, Kahn R. The insulin signaling system. J Biol Chem 1994;269:1-4
    • (1994) J Biol Chem , vol.269 , pp. 1-4
    • White, M.F.1    Kahn, R.2
  • 135
    • 0028982917 scopus 로고
    • Interferon-α engages the insulin receptor substrate-1 to associate with the phosphatidylinositol 3'-kinase
    • Uddiri S, Yenush L, Sun XJ, et al. Interferon-α engages the insulin receptor substrate-1 to associate with the phosphatidylinositol 3'-kinase. J Biol Chem 1995;270:15938-15941
    • (1995) J Biol Chem , vol.270 , pp. 15938-15941
    • Uddiri, S.1    Yenush, L.2    Sun, X.J.3
  • 136
    • 0031171216 scopus 로고    scopus 로고
    • The IRS-signalling system during insulin and cytokine action
    • Yenush L, White MF. The IRS-signalling system during insulin and cytokine action. BioEssays 1997;19:491-500
    • (1997) BioEssays , vol.19 , pp. 491-500
    • Yenush, L.1    White, M.F.2
  • 137
    • 0028825748 scopus 로고
    • Tumor necrosis factor α-induced phosphorylalion of insulin receptor substrate-1 (IRS-1)
    • Kanety H, Feinstein R, Papa MZ, et al. Tumor necrosis factor α-induced phosphorylalion of insulin receptor substrate-1 (IRS-1). J Biol Chem 1995;270:23780-23784
    • (1995) J Biol Chem , vol.270 , pp. 23780-23784
    • Kanety, H.1    Feinstein, R.2    Papa, M.Z.3
  • 138
    • 0028980989 scopus 로고
    • Growth hormone, interferon-gamma, and leukemia inhibitory factor promoted tyrosyl phosphorylation of insulin receptor substrate-1
    • Argetsinger LS, Hsu GW, Myers MG Jr, et al. Growth hormone, interferon-gamma, and leukemia inhibitory factor promoted tyrosyl phosphorylation of insulin receptor substrate-1. J Biol Chem 1995;270:14685-14692
    • (1995) J Biol Chem , vol.270 , pp. 14685-14692
    • Argetsinger, L.S.1    Hsu, G.W.2    Myers M.G., Jr.3
  • 139
    • 0030043596 scopus 로고    scopus 로고
    • The type I interferon receptor mediates tyrosine phosphorylation of insulin receptor substrate 2
    • Platanias LC, Uddin S, Yetter A, et al. The type I interferon receptor mediates tyrosine phosphorylation of insulin receptor substrate 2. J Biol Chem 1996;271:278-282
    • (1996) J Biol Chem , vol.271 , pp. 278-282
    • Platanias, L.C.1    Uddin, S.2    Yetter, A.3
  • 140
    • 0030060604 scopus 로고    scopus 로고
    • Tumor necrosis factor promotes phosphorylation and binding of insulin receptor substrate 1 to phosphatidylinositol 3-kinase in 3T3-L1 adipocytes
    • Guo D, Donner DB. Tumor necrosis factor promotes phosphorylation and binding of insulin receptor substrate 1 to phosphatidylinositol 3-kinase in 3T3-L1 adipocytes. J Biol Chem 1996;271:615-618
    • (1996) J Biol Chem , vol.271 , pp. 615-618
    • Guo, D.1    Donner, D.B.2
  • 141
    • 0029933665 scopus 로고    scopus 로고
    • Tumor necrosis factor (TNF)-alpha inhibits insulin signaling through stimulation of the p55 TNF receptor and activation of sphingomyelinase
    • Peraldi P, Hotamisligil GS, Buurman WA, et al. Tumor necrosis factor (TNF)-alpha inhibits insulin signaling through stimulation of the p55 TNF receptor and activation of sphingomyelinase. J Biol Chem 1996;271:13018-13022
    • (1996) J Biol Chem , vol.271 , pp. 13018-13022
    • Peraldi, P.1    Hotamisligil, G.S.2    Buurman, W.A.3
  • 142
    • 0028815235 scopus 로고
    • Insulin and counterregulatory hormones influence acute-phase protein production in human hepatocytes
    • OÔRiordain MG, Ross JA, Fearon KCH, et al. Insulin and counterregulatory hormones influence acute-phase protein production in human hepatocytes. Am J Physiol 1995;269:E323-E330
    • (1995) Am J Physiol , vol.269
    • Oôriordain, M.G.1    Ross, J.A.2    Fearon, K.C.H.3
  • 143
    • 0026520358 scopus 로고
    • Insulin is a prominent modulator of the cytokine-stimulated expression of acute-phase plasma protein genes
    • Campos SP, Baumann H. Insulin is a prominent modulator of the cytokine-stimulated expression of acute-phase plasma protein genes. Mol Cell Biol 1992;12:1789-1797
    • (1992) Mol Cell Biol , vol.12 , pp. 1789-1797
    • Campos, S.P.1    Baumann, H.2
  • 144
    • 0030049565 scopus 로고    scopus 로고
    • Interleukin-6 induces tyrosine phosphorylation of the Ras activating protein She, and its complex formation with Grb2 in the human multiple myeloma cell line LP-I
    • Neumann C, Zehentmaier G, Danhauser-Riedl S, et al. Interleukin-6 induces tyrosine phosphorylation of the Ras activating protein She, and its complex formation with Grb2 in the human multiple myeloma cell line LP-I. Eur J Immunol 1996;26:379-384
    • (1996) Eur J Immunol , vol.26 , pp. 379-384
    • Neumann, C.1    Zehentmaier, G.2    Danhauser-Riedl, S.3
  • 145
    • 0028279791 scopus 로고
    • Ciliary neurotrophic factor/leukemia inhibitory factor/interleukin 6/oncostatin M family of cytokines induce tyrosine phosphorylation of a common set of proteins overlapping those induced by other cytokines and growth factors
    • Boulton TG, Stahl N, Yancopoulos GD. Ciliary neurotrophic factor/leukemia inhibitory factor/interleukin 6/oncostatin M family of cytokines induce tyrosine phosphorylation of a common set of proteins overlapping those induced by other cytokines and growth factors. J Biol Chem 1994;269:11648-11655
    • (1994) J Biol Chem , vol.269 , pp. 11648-11655
    • Boulton, T.G.1    Stahl, N.2    Yancopoulos, G.D.3
  • 146
    • 0028810979 scopus 로고
    • Insulin activates nuclear factor KB in mammalian cells through a Raf-1 mediated pathway
    • Bertrand F, Philippe C, Antoine PJ, et al. Insulin activates nuclear factor KB in mammalian cells through a Raf-1 mediated pathway. J Biol Chem 1995;270:24435-24441
    • (1995) J Biol Chem , vol.270 , pp. 24435-24441
    • Bertrand, F.1    Philippe, C.2    Antoine, P.J.3
  • 147
    • 0028574382 scopus 로고
    • Interleukin-1, tumor necrosis factor and their specific inhibitors
    • Dayer JM, Burger D. Interleukin-1, tumor necrosis factor and their specific inhibitors. Eur Cytokine Netw 1994;5:563-571
    • (1994) Eur Cytokine Netw , vol.5 , pp. 563-571
    • Dayer, J.M.1    Burger, D.2
  • 148
    • 0025787689 scopus 로고
    • Interleukin 1 receptor antagonist. A new member of the interleukin 1 family
    • Arend WP. Interleukin 1 receptor antagonist. A new member of the interleukin 1 family. J Clin Invest 1991;88:1445-1451
    • (1991) J Clin Invest , vol.88 , pp. 1445-1451
    • Arend, W.P.1
  • 149
    • 0029180522 scopus 로고
    • Inhibiting the effects of cytokines in human diseases
    • Arend WP. Inhibiting the effects of cytokines in human diseases. Adv Intern Med 1995;40:365-394
    • (1995) Adv Intern Med , vol.40 , pp. 365-394
    • Arend, W.P.1
  • 150
    • 0027501020 scopus 로고
    • Interleukin-1 receptor antagonist
    • Arend WP. Interleukin-1 receptor antagonist. Adv Immunol 1993;54:167-227
    • (1993) Adv Immunol , vol.54 , pp. 167-227
    • Arend, W.P.1
  • 151
    • 0029979369 scopus 로고    scopus 로고
    • Biologic basis for interleukin-1 in disease
    • Dinarello CA. Biologic basis for interleukin-1 in disease. Blood 1996;87:2095-2147
    • (1996) Blood , vol.87 , pp. 2095-2147
    • Dinarello, C.A.1
  • 152
    • 0025954301 scopus 로고
    • Purification and characterization of a novel soluble receptor for interleukin 1
    • Symons JA, Eastgate JA, Duff GW. Purification and characterization of a novel soluble receptor for interleukin 1. J Exp Med 1991;174:1251-1254
    • (1991) J Exp Med , vol.174 , pp. 1251-1254
    • Symons, J.A.1    Eastgate, J.A.2    Duff, G.W.3
  • 153
    • 0027412007 scopus 로고
    • Urinary TNF-binding protein (TNF soluble receptor) protects mice against the lethal effect of TNF and endotoxic shock
    • Bertini R, Delgado R, Faggioni R, et al. Urinary TNF-binding protein (TNF soluble receptor) protects mice against the lethal effect of TNF and endotoxic shock. Eur Cylokine Netw 1993;4:39-42
    • (1993) Eur Cylokine Netw , vol.4 , pp. 39-42
    • Bertini, R.1    Delgado, R.2    Faggioni, R.3
  • 154
    • 0031048768 scopus 로고    scopus 로고
    • Circulating levels of tumor necrosis factor soluble receptors in systemic lupus erythematosus are significantly higher than in other rheumatic diseases and correlate with disease activity
    • Gabay C, Cakir N, Moral F, et al. Circulating levels of tumor necrosis factor soluble receptors in systemic lupus erythematosus are significantly higher than in other rheumatic diseases and correlate with disease activity. J Rheumatol 1997;24:303-308
    • (1997) J Rheumatol , vol.24 , pp. 303-308
    • Gabay, C.1    Cakir, N.2    Moral, F.3
  • 155
    • 0027270717 scopus 로고
    • Tumour necrosis factor (TNF) binding proteins (soluble TNF receptor forms) with possible roles in inflammation and malignancy
    • Olsson I, Gatanaga T, Gullberg U, et al. Tumour necrosis factor (TNF) binding proteins (soluble TNF receptor forms) with possible roles in inflammation and malignancy. Eur Cytokine Netw 1993;4:169-180
    • (1993) Eur Cytokine Netw , vol.4 , pp. 169-180
    • Olsson, I.1    Gatanaga, T.2    Gullberg, U.3
  • 156
    • 0028861236 scopus 로고
    • Inhibition of the production and effects of interleukin-1 and tumor necrosis factor alpha in rheumatoid arthritis
    • Arend WP, Dayer JM. Inhibition of the production and effects of interleukin-1 and tumor necrosis factor alpha in rheumatoid arthritis. Arthritis Rheum 1995;38:151-160
    • (1995) Arthritis Rheum , vol.38 , pp. 151-160
    • Arend, W.P.1    Dayer, J.M.2
  • 157
    • 0028031990 scopus 로고
    • Interleukin-6 (IL-6) as an anti-inflammatory cytokine: Induction of circulating IL-1 receptor antagonist and soluble tumor necrosis factor receptor p55
    • Tilg H, Trehu E, Atkins MB, et al. Interleukin-6 (IL-6) as an anti-inflammatory cytokine: Induction of circulating IL-1 receptor antagonist and soluble tumor necrosis factor receptor p55. Blood 1994;83:113-118
    • (1994) Blood , vol.83 , pp. 113-118
    • Tilg, H.1    Trehu, E.2    Atkins, M.B.3
  • 158
    • 0031081462 scopus 로고    scopus 로고
    • Relation between pro-and anti-inflammatory cytokines and the production of nitric oxide (NO) in severe sepsis
    • Groeneveld PH, Kwappenberg KM, Langermans JA, et al. Relation between pro-and anti-inflammatory cytokines and the production of nitric oxide (NO) in severe sepsis. Cytokine 1997; 9:138-142
    • (1997) Cytokine , vol.9 , pp. 138-142
    • Groeneveld, P.H.1    Kwappenberg, K.M.2    Langermans, J.A.3
  • 159
    • 0032495666 scopus 로고    scopus 로고
    • Anti-inflammatory cytokine profile and mortality in febrile patients
    • Van Dissel JT, Van Langevelde P, Westendorp RGJ, et al. Anti-inflammatory cytokine profile and mortality in febrile patients. Lancet 1998;351:950-953
    • (1998) Lancet , vol.351 , pp. 950-953
    • Van Dissel, J.T.1    Van Langevelde, P.2    Westendorp, R.G.J.3
  • 160
    • 0027146428 scopus 로고
    • Interleukin 4 inhibits the production of some acute-phase proteins by human hepatocytes in primary culture
    • Loyer P, Ilyin G, Abdel-Razzak Z, et al. Interleukin 4 inhibits the production of some acute-phase proteins by human hepatocytes in primary culture. FEBS Lett 1993;336:215-220
    • (1993) FEBS Lett , vol.336 , pp. 215-220
    • Loyer, P.1    Ilyin, G.2    Abdel-Razzak, Z.3
  • 161
    • 0032518415 scopus 로고    scopus 로고
    • IL-6 is an antiinflammatory cytokine required for controlling local or systemic acute inflammatory responses
    • Xing Z, Gauldie J, Cox O, et al. IL-6 is an antiinflammatory cytokine required for controlling local or systemic acute inflammatory responses. J Clin Invest 1998;101:311-320
    • (1998) J Clin Invest , vol.101 , pp. 311-320
    • Xing, Z.1    Gauldie, J.2    Cox, O.3
  • 162
    • 0028300351 scopus 로고
    • T cell activation-associated hepatic injury: Mediation by tumor necrosis factors and protection by interleukin 6
    • Mizuhara H, O'Neill E, Seki N, et al. T cell activation-associated hepatic injury: Mediation by tumor necrosis factors and protection by interleukin 6. J Exp Med 1994;179:1529-1537
    • (1994) J Exp Med , vol.179 , pp. 1529-1537
    • Mizuhara, H.1    O'Neill, E.2    Seki, N.3
  • 163
    • 0028931477 scopus 로고
    • Neutralization of endogenous IL-6 suppresses induction of IL-1 receptor antagonist
    • Jordan M, Otterness IG, Ng R, et al. Neutralization of endogenous IL-6 suppresses induction of IL-1 receptor antagonist. J Immunol 1995;154:4081-4090
    • (1995) J Immunol , vol.154 , pp. 4081-4090
    • Jordan, M.1    Otterness, I.G.2    Ng, R.3
  • 164
    • 0030823183 scopus 로고    scopus 로고
    • IL-6 and APPs: Anti-inflammatory and immunosuppressive mediators
    • Tilg H, Dinarello CA, Mier JW. IL-6 and APPs: Anti-inflammatory and immunosuppressive mediators. Immunol Today 1997; 18:428-432
    • (1997) Immunol Today , vol.18 , pp. 428-432
    • Tilg, H.1    Dinarello, C.A.2    Mier, J.W.3
  • 165
    • 0029164394 scopus 로고
    • Role of the hypothalamus-pituitary-adrenal axis in the regulation of TNF production in mice. Effect of stress and inhibition of endogenous glucocorticoids
    • Fantuzzi G, Di-Santo E, Sacco S, et al. Role of the hypothalamus-pituitary-adrenal axis in the regulation of TNF production in mice. Effect of stress and inhibition of endogenous glucocorticoids. J Immunol 1995;155:3552-3555
    • (1995) J Immunol , vol.155 , pp. 3552-3555
    • Fantuzzi, G.1    Di-Santo, E.2    Sacco, S.3
  • 166
    • 0029037126 scopus 로고
    • The hypothalamic-pituitary-adrenal axis and immune-mediated inflammation
    • Chrousos GP. The hypothalamic-pituitary-adrenal axis and immune-mediated inflammation [see comments]. N Engl J Med 1995;332:1351-1362
    • (1995) N Engl J Med , vol.332 , pp. 1351-1362
    • Chrousos, G.P.1
  • 167
    • 0026650341 scopus 로고
    • In vivo effects of the antiglucocorticoid RU 486 on glucocorticoid and cytokine responses to Escherichia coli endotoxin
    • Hawes AS, Rock CS, Keogh CV, et al. In vivo effects of the antiglucocorticoid RU 486 on glucocorticoid and cytokine responses to Escherichia coli endotoxin. Infect Immun 1992;60: 2641-2647
    • (1992) Infect Immun , vol.60 , pp. 2641-2647
    • Hawes, A.S.1    Rock, C.S.2    Keogh, C.V.3
  • 168
    • 0024509926 scopus 로고
    • Differential regulation of lipopolysaccharide-induced interleukin 1 and tumor necrosis factor synthesis: Effects of endogenous and exogenous glucocorticoids and the role of the pituitary-adrenal axis
    • Zuckerman SH, Shellhaas J, Butler LD. Differential regulation of lipopolysaccharide-induced interleukin 1 and tumor necrosis factor synthesis: Effects of endogenous and exogenous glucocorticoids and the role of the pituitary-adrenal axis. Eur J Immunol 1989;19:301-305
    • (1989) Eur J Immunol , vol.19 , pp. 301-305
    • Zuckerman, S.H.1    Shellhaas, J.2    Butler, L.D.3
  • 169
    • 0025914573 scopus 로고
    • Influence of endogenous glucocorticoid on endotoxin-induced production of circulating TNF-alpha
    • Parant M, Le-Contel C, Parant F, Chedid L. Influence of endogenous glucocorticoid on endotoxin-induced production of circulating TNF-alpha. Lymphokine Cytokine Res 1991;10: 265-271
    • (1991) Lymphokine Cytokine Res , vol.10 , pp. 265-271
    • Parant, M.1    Le-Contel, C.2    Parant, F.3    Chedid, L.4
  • 170
    • 0030802018 scopus 로고    scopus 로고
    • Glucocorticoids and immune function: Unknown dimensions and new frontiers
    • Wilckens Th, De Rijk R. Glucocorticoids and immune function: Unknown dimensions and new frontiers. Immunol Today 1997; 18:418-424
    • (1997) Immunol Today , vol.18 , pp. 418-424
    • Wilckens, Th.1    De Rijk, R.2
  • 171
    • 0032127397 scopus 로고    scopus 로고
    • Termination of acute phase response: A role of some cytokines and antiinflammatory drugs
    • Koj A. Termination of acute phase response: A role of some cytokines and antiinflammatory drugs. Gen Pharmacol 1998;31: 9-18
    • (1998) Gen Pharmacol , vol.31 , pp. 9-18
    • Koj, A.1
  • 172
    • 0030685133 scopus 로고    scopus 로고
    • Lipopolysaccharide binding protein is required to combat a murine gram-negative bacterial infection
    • Jack RS, Fan X, Bernheidem M, et al. Lipopolysaccharide binding protein is required to combat a murine gram-negative bacterial infection. Nature 1997;389:742-745
    • (1997) Nature , vol.389 , pp. 742-745
    • Jack, R.S.1    Fan, X.2    Bernheidem, M.3
  • 173
    • 0032523815 scopus 로고    scopus 로고
    • LPS-binding protein protects mice from septic shock caused by LPS or gram-negative bacteria
    • Lamping N, Dettmer R, Schröder NWJ, et al. LPS-binding protein protects mice from septic shock caused by LPS or gram-negative bacteria. J Clin Invest 1998;101:2065-2071
    • (1998) J Clin Invest , vol.101 , pp. 2065-2071
    • Lamping, N.1    Dettmer, R.2    Schröder, N.W.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.