메뉴 건너뛰기




Volumn 174, Issue 5, 2005, Pages 2974-2980

The production of IL-1 receptor antagonist in IFN-β-stimulated human monocytes depends on the activation of phosphatidylinositol 3-kinase but not of STAT1

Author keywords

[No Author keywords available]

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; 2 MORPHOLINO 8 PHENYLCHROMONE; BETA INTERFERON; CYCLOHEXIMIDE; DACTINOMYCIN; INTERLEUKIN 1 RECEPTOR BLOCKING AGENT; INTERLEUKIN 1BETA; JANUS KINASE; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE INHIBITOR; MITOGEN ACTIVATED PROTEIN KINASE KINASE 1; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3 KINASE INHIBITOR; SERINE; SMALL INTERFERING RNA; STAT PROTEIN; STAT1 PROTEIN;

EID: 14044273004     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.174.5.2974     Document Type: Article
Times cited : (28)

References (53)
  • 1
    • 0000084250 scopus 로고    scopus 로고
    • IL-1Ra
    • J. J. Oppenheim and M. Feldmann, eds. Academic Press, London
    • Burger, D., and J. M. Dayer. 2000. IL-1Ra. In Cytokine Reference. J. J. Oppenheim and M. Feldmann, eds. Academic Press, London, pp. 319-336.
    • (2000) Cytokine Reference , pp. 319-336
    • Burger, D.1    Dayer, J.M.2
  • 2
    • 0027761344 scopus 로고
    • Interleukin 1 receptor antagonist production in human monocytes is induced by IL-1α, IL-3, IL-4 and GM-CSF
    • Jenkins, J. K., and W. P. Arend. 1993. Interleukin 1 receptor antagonist production in human monocytes is induced by IL-1α, IL-3, IL-4 and GM-CSF. Cytokine 5:407.
    • (1993) Cytokine , vol.5 , pp. 407
    • Jenkins, J.K.1    Arend, W.P.2
  • 4
    • 0035821606 scopus 로고    scopus 로고
    • IFN-β inhibits the ability of T lymphocytes to induce TNF-α and IL-1β production in monocytes upon direct cell-cell contact
    • Jungo, F., J. M. Dayer, C. Modoux, N. Hyka, and D. Burger. 2001. IFN-β inhibits the ability of T lymphocytes to induce TNF-α and IL-1β production in monocytes upon direct cell-cell contact. Cytokine 14:272.
    • (2001) Cytokine , vol.14 , pp. 272
    • Jungo, F.1    Dayer, J.M.2    Modoux, C.3    Hyka, N.4    Burger, D.5
  • 5
    • 0034129854 scopus 로고    scopus 로고
    • Induction of IL-1 receptor antagonist by interferon β: Implication for the treatment of multiple sclerosis
    • Sciacca, F. L., N. Canal, and L. M. E. Grimaldi. 2000. Induction of IL-1 receptor antagonist by interferon β: implication for the treatment of multiple sclerosis. J. Neurovir. 6:S33.
    • (2000) J. Neurovir. , vol.6
    • Sciacca, F.L.1    Canal, N.2    Grimaldi, L.M.E.3
  • 6
    • 0026503448 scopus 로고
    • Coordinated antiinflammatory effects of interleukin 4: Interleukin 4 suppresses interleukin 1 production but up-regulates gene expression and synthesis of interleukin 1 receptor antagonist
    • Vannier, E., L. C. Miller, and C. A. Dinarello. 1992. Coordinated antiinflammatory effects of interleukin 4: interleukin 4 suppresses interleukin 1 production but up-regulates gene expression and synthesis of interleukin 1 receptor antagonist. Proc. Natl. Acad. Sci. USA 89:4076.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4076
    • Vannier, E.1    Miller, L.C.2    Dinarello, C.A.3
  • 7
    • 34247637856 scopus 로고    scopus 로고
    • The role of human T lymphocyte-monocyte contact in inflammation and tissue destruction
    • Burger, D., and J. M. Dayer. 2002. The role of human T lymphocyte-monocyte contact in inflammation and tissue destruction. Arthritis Res. 4 (Suppl 3):S169.
    • (2002) Arthritis Res. , vol.4 , Issue.SUPPL. 3
    • Burger, D.1    Dayer, J.M.2
  • 8
    • 0036308243 scopus 로고    scopus 로고
    • Cytokines, acute-phase proteins, and hormones: IL-1 and TNF-α production in contact-mediated activation of monocytes by T lymphocytes
    • Burger, D., and J. M. Dayer. 2002. Cytokines, acute-phase proteins, and hormones: IL-1 and TNF-α production in contact-mediated activation of monocytes by T lymphocytes. Ann. NY Acad Sci. 966:464.
    • (2002) Ann. NY Acad Sci. , vol.966 , pp. 464
    • Burger, D.1    Dayer, J.M.2
  • 9
    • 17544387368 scopus 로고
    • Differential aspects of cytokines in the immunopathology of multiple sclerosis
    • Lucas, K., and R. Hohlfeld. 1995. Differential aspects of cytokines in the immunopathology of multiple sclerosis. Neurology 45:54.
    • (1995) Neurology , vol.45 , pp. 54
    • Lucas, K.1    Hohlfeld, R.2
  • 10
    • 0000066854 scopus 로고    scopus 로고
    • Cytokines and growth factors
    • W. N. Kelley, E. D. Harris, Jr., S. Ruddy, and C. S. Sledge, eds. W.B. Saunders, Philadelphia
    • Dayer, J. M., and W, P. Arend. 1997. Cytokines and growth factors. In Textbook of Rheumatology. W. N. Kelley, E. D. Harris, Jr., S. Ruddy, and C. S. Sledge, eds. W.B. Saunders, Philadelphia, pp. 267-286.
    • (1997) Textbook of Rheumatology , pp. 267-286
    • Dayer, J.M.1    Arend, W.P.2
  • 11
    • 0008376732 scopus 로고    scopus 로고
    • Interferon β in the treatment of multiple sclerosis: Mechanisms of action
    • Yong, V. W., S. Chabot, O. Stuve, and G. Williams. 1998. Interferon β in the treatment of multiple sclerosis: mechanisms of action. Neurology 51:682.
    • (1998) Neurology , vol.51 , pp. 682
    • Yong, V.W.1    Chabot, S.2    Stuve, O.3    Williams, G.4
  • 13
    • 0036434695 scopus 로고    scopus 로고
    • Interferon-β for treatment of rheumatoid arthritis?
    • Van Holten, J., C. Plater-Zyberk, and P. P. Tak. 2002. Interferon-β for treatment of rheumatoid arthritis? Arthritis Res. 4:346.
    • (2002) Arthritis Res. , vol.4 , pp. 346
    • Van Holten, J.1    Plater-Zyberk, C.2    Tak, P.P.3
  • 14
    • 17644372231 scopus 로고    scopus 로고
    • Treatment with recombinant interferon-β reduces inflammation and slows cartilage destruction in the collagen-induced arthritis model of rheumatoid arthritis
    • Van Holten, J., K. Reedquist, P. Sattonet-Roche, T. J. Smeets, C. Plater-Zyberk, M. J. Vervoordeldonk, and P. P. Tak. 2004. Treatment with recombinant interferon-β reduces inflammation and slows cartilage destruction in the collagen-induced arthritis model of rheumatoid arthritis. Arthritis Res. Ther. 6:R239.
    • (2004) Arthritis Res. Ther. , vol.6
    • Van Holten, J.1    Reedquist, K.2    Sattonet-Roche, P.3    Smeets, T.J.4    Plater-Zyberk, C.5    Vervoordeldonk, M.J.6    Tak, P.P.7
  • 15
    • 0033953738 scopus 로고    scopus 로고
    • Reduction of both pro- and anti-inflammatory cytokines after 6 months of interferon β-1a treatment of multiple sclerosis
    • Khademi, M., E. Wallstrom, M. Andersson, F. Piehl, R. Di Marco, and T. Olsson. 2000. Reduction of both pro- and anti-inflammatory cytokines after 6 months of interferon β-1a treatment of multiple sclerosis. J. Neuroimmunol. 103:202.
    • (2000) J. Neuroimmunol. , vol.103 , pp. 202
    • Khademi, M.1    Wallstrom, E.2    Andersson, M.3    Piehl, F.4    Di Marco, R.5    Olsson, T.6
  • 17
    • 0034982136 scopus 로고    scopus 로고
    • Interferon-β in multiple sclerosis: Altering the balance of interleukin-12 and interleukin-10?
    • Karp, C. L., A. H. Boxel-Dezaire, A. A. Byrnes, and L. Nagelkerken. 2001. Interferon-β in multiple sclerosis: altering the balance of interleukin-12 and interleukin-10? Curr. Opin. Neurol. 14:361.
    • (2001) Curr. Opin. Neurol. , vol.14 , pp. 361
    • Karp, C.L.1    Boxel-Dezaire, A.H.2    Byrnes, A.A.3    Nagelkerken, L.4
  • 18
    • 0031463988 scopus 로고    scopus 로고
    • Interferon-β not only inhibits interleukin-1β and tumor necrosis factor-α but stimulates interleukin-1 receptor antagonist production in human peripheral blood mononuclear cells
    • Coclet-Ninin, J., J. M. Dayer, and D. Burger. 1997. Interferon-β not only inhibits interleukin-1β and tumor necrosis factor-α but stimulates interleukin-1 receptor antagonist production in human peripheral blood mononuclear cells. Eur. Cytokine Network 8:345.
    • (1997) Eur. Cytokine Network , vol.8 , pp. 345
    • Coclet-Ninin, J.1    Dayer, J.M.2    Burger, D.3
  • 19
    • 0346101877 scopus 로고    scopus 로고
    • Opposite effects of IFNβ on cytokine homeostasis in LPS- and T cell contact-activated human monocytes
    • Molnarfi, N., L. Gruaz, J. M. Dayer, and D. Burger. 2004. Opposite effects of IFNβ on cytokine homeostasis in LPS- and T cell contact-activated human monocytes. J. Neuroimmunol. 146:76.
    • (2004) J. Neuroimmunol. , vol.146 , pp. 76
    • Molnarfi, N.1    Gruaz, L.2    Dayer, J.M.3    Burger, D.4
  • 20
    • 0035344461 scopus 로고    scopus 로고
    • A weak signal for strong responses: Interferon-α/β revisited
    • Taniguchi, T., and A. Takaoka. 2001. A weak signal for strong responses: interferon-α/β revisited. Nat. Rev. Mol. Cell Biol. 2:378.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 378
    • Taniguchi, T.1    Takaoka, A.2
  • 21
    • 0037144598 scopus 로고    scopus 로고
    • STAT3 activation by type I interferons is dependent on specific tyrosines located in the cytoplasmic domain of interferon receptor chain 2c: Activation of multiple STATS proceeds through the redundant usage of two tyrosine residues
    • Velichko, S., T. C. Wagner, J. Turkson, R. Jove, and E. Croze. 2002. STAT3 activation by type I interferons is dependent on specific tyrosines located in the cytoplasmic domain of interferon receptor chain 2c: activation of multiple STATS proceeds through the redundant usage of two tyrosine residues. J. Biol. Chem. 277:35635.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35635
    • Velichko, S.1    Wagner, T.C.2    Turkson, J.3    Jove, R.4    Croze, E.5
  • 22
    • 0029069145 scopus 로고
    • Transcriptional responses to polypeptide ligands: The JAK-STAT pathway
    • Schindler, C., and S. E. Darnell, Jr. 1995. Transcriptional responses to polypeptide ligands: the JAK-STAT pathway. Annu. Rev. Biochem. 64:621.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 621
    • Schindler, C.1    Darnell Jr., S.E.2
  • 23
    • 0036467492 scopus 로고    scopus 로고
    • The interferon-α/β system in antiviral responses: A multimodal machinery of gene regulation by the IRF family of transcription factors
    • Taniguchi, T., and A. Takaoka. 2002. The interferon-α/β system in antiviral responses: a multimodal machinery of gene regulation by the IRF family of transcription factors. Curr. Opin. Immunol. 14:111.
    • (2002) Curr. Opin. Immunol. , vol.14 , pp. 111
    • Taniguchi, T.1    Takaoka, A.2
  • 25
    • 0030999696 scopus 로고    scopus 로고
    • STAT3 as an adapter to couple phosphatidylinositol 3-kinase to the IF-NAR1 chain of the type I interferon receptor
    • Pfeffer, L. M., J. E. Mullersman, S. R. Pfeffer, A. Murti, W. Shi, and C. H. Yang. 1997. STAT3 as an adapter to couple phosphatidylinositol 3-kinase to the IF-NAR1 chain of the type I interferon receptor. Science 276:1418.
    • (1997) Science , vol.276 , pp. 1418
    • Pfeffer, L.M.1    Mullersman, J.E.2    Pfeffer, S.R.3    Murti, A.4    Shi, W.5    Yang, C.H.6
  • 26
    • 0034595093 scopus 로고    scopus 로고
    • Interferon-dependent activation of the serine kinase PI 3′-kinase requires engagement of the IRS pathway but not the Stat pathway
    • Uddin, S., B. Majchrzak, P. C. Wang, S. Modi, M. K. Khan, E. N. Fish, and L. C. Platanias. 2000. Interferon-dependent activation of the serine kinase PI 3′-kinase requires engagement of the IRS pathway but not the Stat pathway. Biochem. Biophys. Res. Commun. 270:158.
    • (2000) Biochem. Biophys. Res. Commun. , vol.270 , pp. 158
    • Uddin, S.1    Majchrzak, B.2    Wang, P.C.3    Modi, S.4    Khan, M.K.5    Fish, E.N.6    Platanias, L.C.7
  • 27
    • 0033527566 scopus 로고    scopus 로고
    • Catalytically active TYK2 is essential for interferon-β-mediated phosphorylation of STAT3 and interferon-α receptor-1 (IFNAR-1) but not for activation of phosphoinositol 3-kinase
    • Rani, M. R. S., D. W. Leaman, Y. Han, S. Leung, E. Croze, E. N. Fish, A. Wolfman, and R. M. Ransohoff. 1999. Catalytically active TYK2 is essential for interferon-β-mediated phosphorylation of STAT3 and interferon-α receptor-1 (IFNAR-1) but not for activation of phosphoinositol 3-kinase. J. Biol. Chem. 274:32507.
    • (1999) J. Biol. Chem. , vol.274 , pp. 32507
    • Rani, M.R.S.1    Leaman, D.W.2    Han, Y.3    Leung, S.4    Croze, E.5    Fish, E.N.6    Wolfman, A.7    Ransohoff, R.M.8
  • 28
    • 0029133702 scopus 로고
    • Requirement for MAP kinase (ERK2) activity in interferon α- and interferon β-stimulated gene expression through STAT proteins
    • David, M., E. Petricoin III, C. Benjamin, R. Pine, M. J. Weber, and A. C. Larner. 1995. Requirement for MAP kinase (ERK2) activity in interferon α- and interferon β-stimulated gene expression through STAT proteins. Science 269:1721.
    • (1995) Science , vol.269 , pp. 1721
    • David, M.1    Petricoin III, E.2    Benjamin, C.3    Pine, R.4    Weber, M.J.5    Larner, A.C.6
  • 29
    • 0031035322 scopus 로고    scopus 로고
    • Lipopolysaccharide and Raf-1 kinase regulate secretory interleukin-1 receptor antagonist gene expression by mutually antagonistic mechanisms
    • Guthridge, C. J., D. Eidlen, W. P. Arend, A. Gutierrez-Hartmann, and M. F. Smith, Jr. 1997. Lipopolysaccharide and Raf-1 kinase regulate secretory interleukin-1 receptor antagonist gene expression by mutually antagonistic mechanisms. Mol. Cell. Biol. 17:1118.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1118
    • Guthridge, C.J.1    Eidlen, D.2    Arend, W.P.3    Gutierrez-Hartmann, A.4    Smith Jr., M.F.5
  • 30
    • 0037337667 scopus 로고    scopus 로고
    • Leptin activates the promoter of the interleukin-1 receptor antagonist through p42/44 mitogen-activated protein kinase and a composite nuclear factor κB/PU.1 binding site
    • Dreyer, M. G., C. E. Juge-Aubry, C. Gabay, U. Lang, F. Rohner-Jeanrenaud, J. M. Dayer, and C. A. Meier. 2003. Leptin activates the promoter of the interleukin-1 receptor antagonist through p42/44 mitogen-activated protein kinase and a composite nuclear factor κB/PU.1 binding site. Biochem. J. 370:591.
    • (2003) Biochem. J. , vol.370 , pp. 591
    • Dreyer, M.G.1    Juge-Aubry, C.E.2    Gabay, C.3    Lang, U.4    Rohner-Jeanrenaud, F.5    Dayer, J.M.6    Meier, C.A.7
  • 31
    • 0031193955 scopus 로고    scopus 로고
    • Direct contact with stimulated T cells induces the expression of IL-1β and IL-1 receptor antagonist in human monocytes: Involvement of serine/threonine phosphatases in differential regulation
    • Vey, E., J. M. Dayer, and D. Burger. 1997. Direct contact with stimulated T cells induces the expression of IL-1β and IL-1 receptor antagonist in human monocytes: involvement of serine/threonine phosphatases in differential regulation. Cytokine 9:480.
    • (1997) Cytokine , vol.9 , pp. 480
    • Vey, E.1    Dayer, J.M.2    Burger, D.3
  • 32
    • 0030239633 scopus 로고    scopus 로고
    • IL-4-induced expression of the IL-1 receptor antagonist gene is mediated by STAT6
    • Ohmori, Y., M. F. Smith, Jr., and T. A. Hamilton. 1996. IL-4-induced expression of the IL-1 receptor antagonist gene is mediated by STAT6. J. Immunol. 157:2058.
    • (1996) J. Immunol. , vol.157 , pp. 2058
    • Ohmori, Y.1    Smith Jr., M.F.2    Hamilton, T.A.3
  • 33
    • 0035827666 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase pathway selectively controls sIL-1RA not interleukin-1β production in the septic leukocytes
    • Learn, C. A., M. S. Boger, L. Li, and C. E. McCall. 2001. The phosphatidylinositol 3-kinase pathway selectively controls sIL-1RA not interleukin-1β production in the septic leukocytes. J. Biol. Chem. 276:20234.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20234
    • Learn, C.A.1    Boger, M.S.2    Li, L.3    McCall, C.E.4
  • 34
    • 0035871793 scopus 로고    scopus 로고
    • Apolipoprotein A-I inhibits the production of interleukin-1β and tumor necrosis factor-α by blocking contact-mediated activation of monocytes by T lymphocytes
    • Hyka, N., J. M. Dayer, C. Modoux, T. Kohno, C. K. Edwards III, P. Roux-Lombard, and D. Burger. 2001. Apolipoprotein A-I inhibits the production of interleukin-1β and tumor necrosis factor-α by blocking contact-mediated activation of monocytes by T lymphocytes. Blood 97:2381.
    • (2001) Blood , vol.97 , pp. 2381
    • Hyka, N.1    Dayer, J.M.2    Modoux, C.3    Kohno, T.4    Edwards III, C.K.5    Roux-Lombard, P.6    Burger, D.7
  • 35
    • 0034660486 scopus 로고    scopus 로고
    • 2 integrin by antibodies or soluble CD23 induces IL-1β production on primary human monocytes through mitogen-activated protein kinase-dependent pathways
    • 2 integrin by antibodies or soluble CD23 induces IL-1β production on primary human monocytes through mitogen-activated protein kinase-dependent pathways. Blood 95:3868.
    • (2000) Blood , vol.95 , pp. 3868
    • Rezzonico, R.1    Chicheportiche, R.2    Imbert, V.3    Dayer, J.M.4
  • 36
    • 0035874494 scopus 로고    scopus 로고
    • 2 integrins by antibodies or soluble CD23 induces macrophage inflammatory protein 1α (MIP-1α) and MIP-1β production in primary human monocytes through a pathway dependent on nuclear factor-κB
    • 2 integrins by antibodies or soluble CD23 induces macrophage inflammatory protein 1α (MIP-1α) and MIP-1β production in primary human monocytes through a pathway dependent on nuclear factor-κB. Blood 97:2932.
    • (2001) Blood , vol.97 , pp. 2932
    • Rezzonico, R.1    Imbert, V.2    Chicheportiche, R.3    Dayer, J.M.4
  • 37
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248.
    • (1976) Anal. Biochem. , vol.72 , pp. 248
    • Bradford, M.1
  • 38
    • 0343618515 scopus 로고    scopus 로고
    • Cooperation among Stat1, glucocorticoid receptor, and PU.1 in transcriptional activation of the high-affinity Fcγ receptor I in monocytes
    • Aittomaki, S., M. Pesu, B. Groner, O. A. Janne, J. J. Palvimo, and O. Silvennoinen. 2000. Cooperation among Stat1, glucocorticoid receptor, and PU.1 in transcriptional activation of the high-affinity Fcγ receptor I in monocytes. J. Immunol. 164:5689.
    • (2000) J. Immunol. , vol.164 , pp. 5689
    • Aittomaki, S.1    Pesu, M.2    Groner, B.3    Janne, O.A.4    Palvimo, J.J.5    Silvennoinen, O.6
  • 39
    • 1042292572 scopus 로고    scopus 로고
    • Molecular basis of Stat1 and PU.1 cooperation in cytokine-induced Fcγ receptor I promoter activation
    • Aittomaki, S., J. Yang, E. W. Scott, M. C. Simon, and O. Silvennoinen. 2004. Molecular basis of Stat1 and PU.1 cooperation in cytokine-induced Fcγ receptor I promoter activation. Int. Immunol. 16:265.
    • (2004) Int. Immunol. , vol.16 , pp. 265
    • Aittomaki, S.1    Yang, J.2    Scott, E.W.3    Simon, M.C.4    Silvennoinen, O.5
  • 40
    • 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
    • Collart, M. A., D. Belin, J. D. Vassalli, S. de Kossodo, and P. Vassalli. 1986. 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.
    • (1986) J. Exp. Med. , vol.164 , pp. 2113
    • Collart, M.A.1    Belin, D.2    Vassalli, J.D.3    De Kossodo, S.4    Vassalli, P.5
  • 42
    • 0029147738 scopus 로고
    • Protein synthesis inhibitors reveal differential regulation of mitogen-activated protein kinase and stress-activated protein kinase pathways that converge on Elk-1
    • Zinck, R., M. A. Cahill, M. Kracht, C. Sachsenmaier, R. A. Hipskind, and A. Nordheim. 1995. Protein synthesis inhibitors reveal differential regulation of mitogen-activated protein kinase and stress-activated protein kinase pathways that converge on Elk-1. Mol. Cell. Biol. 15:4930.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4930
    • Zinck, R.1    Cahill, M.A.2    Kracht, M.3    Sachsenmaier, C.4    Hipskind, R.A.5    Nordheim, A.6
  • 44
    • 0037444373 scopus 로고    scopus 로고
    • Discovery of JSI-124 (cucuibitacin I), a selective Janus kinase/signal transducer and activator of transcription 3 signaling pathway inhibitor with potent antitumor activity against human and murine cancer cells in mice
    • Blaskovich, M. A., J. Sun, A. Cantor, J. Turkson, R. Jove, and S. M. Sebti. 2003. Discovery of JSI-124 (cucuibitacin I), a selective Janus kinase/signal transducer and activator of transcription 3 signaling pathway inhibitor with potent antitumor activity against human and murine cancer cells in mice. Cancer Res. 63:1270.
    • (2003) Cancer Res. , vol.63 , pp. 1270
    • Blaskovich, M.A.1    Sun, J.2    Cantor, A.3    Turkson, J.4    Jove, R.5    Sebti, S.M.6
  • 45
    • 0028107016 scopus 로고
    • Role of interferon α/β receptor chain 1 in the structure and transmembrane signaling of the interferon α/β receptor complex
    • Constantinescu, S. N., E. Croze, C. Wang, A. Murti, L. Basu, J. E. Mullersman, and L. M. Pfeffer. 1994. Role of interferon α/β receptor chain 1 in the structure and transmembrane signaling of the interferon α/β receptor complex. Proc. Natl. Acad. Sci. USA 91:9602.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9602
    • Constantinescu, S.N.1    Croze, E.2    Wang, C.3    Murti, A.4    Basu, L.5    Mullersman, J.E.6    Pfeffer, L.M.7
  • 46
    • 0029117304 scopus 로고
    • Maximal activation of transcription by Stat1 and Stat3 requires both tyrosine and serine phosphorylation
    • Wen, Z., Z. Zhong, and J. E. Darnell, Jr. 1995. Maximal activation of transcription by Stat1 and Stat3 requires both tyrosine and serine phosphorylation. Cell 82:241.
    • (1995) Cell , vol.82 , pp. 241
    • Wen, Z.1    Zhong, Z.2    Darnell Jr., J.E.3
  • 47
    • 0034658024 scopus 로고    scopus 로고
    • Serine phosphorylation of STATs
    • Decker, T., and P. Kovarik. 2000. Serine phosphorylation of STATs. Oncogene 19:2628.
    • (2000) Oncogene , vol.19 , pp. 2628
    • Decker, T.1    Kovarik, P.2
  • 49
    • 0037645144 scopus 로고    scopus 로고
    • A PI-3 kinase-dependent, Stat1-independent signaling pathway regulates interferon-stimulated monocyte adhesion
    • Navarro, A., B. Anand-Apte, Y. Tanabe, G. Feldman, and A. C. Lamer. 2003. A PI-3 kinase-dependent, Stat1-independent signaling pathway regulates interferon-stimulated monocyte adhesion. J. Leukocyte Biol. 73:540.
    • (2003) J. Leukocyte Biol. , vol.73 , pp. 540
    • Navarro, A.1    Anand-Apte, B.2    Tanabe, Y.3    Feldman, G.4    Lamer, A.C.5
  • 50
    • 0038605053 scopus 로고    scopus 로고
    • Toll-like receptors 2 and 4 activate STAT1 serine phosphorylation by distinct mechanisms in macrophages
    • Rhee, S. H., B. W. Jones, V. Toshchakov, S. N. Vogel, and M. J. Fenton. 2003. Toll-like receptors 2 and 4 activate STAT1 serine phosphorylation by distinct mechanisms in macrophages. J. Biol. Chem. 278:22506.
    • (2003) J. Biol. Chem. , vol.278 , pp. 22506
    • Rhee, S.H.1    Jones, B.W.2    Toshchakov, V.3    Vogel, S.N.4    Fenton, M.J.5
  • 51
    • 0035930348 scopus 로고    scopus 로고
    • CD40 ligation induces macrophage IL-10 and TNF-α production: Differential use of the PI3K and p42/44 MAPK-pathways
    • Foey, A. D., M. Feldmann, and F. M. Brennan. 2001. CD40 ligation induces macrophage IL-10 and TNF-α production: differential use of the PI3K and p42/44 MAPK-pathways. Cytokine 16:131.
    • (2001) Cytokine , vol.16 , pp. 131
    • Foey, A.D.1    Feldmann, M.2    Brennan, F.M.3
  • 52
    • 0036153880 scopus 로고    scopus 로고
    • Cytokine-stimulated T cells induce macrophage IL-10 production dependent on phosphatidylinositol 3-kinase and p70S6K: Implications for rheumatoid arthritis
    • Foey, A. D., P. Green, B. Foxwell, M. Feldmann, and F. Brennan. 2002. Cytokine-stimulated T cells induce macrophage IL-10 production dependent on phosphatidylinositol 3-kinase and p70S6K: implications for rheumatoid arthritis. Arthritis Res. 4:64.
    • (2002) Arthritis Res. , vol.4 , pp. 64
    • Foey, A.D.1    Green, P.2    Foxwell, B.3    Feldmann, M.4    Brennan, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.