메뉴 건너뛰기




Volumn 163, Issue 4, 1999, Pages 2000-2007

Roles of IFN consensus sequence binding protein and PU.1 in regulating IL-18 gene expression

Author keywords

[No Author keywords available]

Indexed keywords

GENE PRODUCT; INTERFERON CONSENSUS SEQUENCE BINDING PROTEIN; INTERLEUKIN 18; PROTEIN PU.1; UNCLASSIFIED DRUG;

EID: 0033567084     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (99)

References (37)
  • 4
    • 15844367093 scopus 로고    scopus 로고
    • Cloning of the cDNA for human IFN-γ-inducing factor, expression in Escherichia coli, and studies on the biologic activity of the protein
    • Ushio, S., M. Namba, T. Okura, M. Hattori, Y. Nukada, K. Akita, F. Tanabe, K. Konoshi, M. Micallef, M. Fujii, et al. 1996. Cloning of the cDNA for human IFN-γ-inducing factor, expression in Escherichia coli, and studies on the biologic activity of the protein. J. Immunol. 156:4274.
    • (1996) J. Immunol. , vol.156 , pp. 4274
    • Ushio, S.1    Namba, M.2    Okura, T.3    Hattori, M.4    Nukada, Y.5    Akita, K.6    Tanabe, F.7    Konoshi, K.8    Micallef, M.9    Fujii, M.10
  • 6
    • 0030885123 scopus 로고    scopus 로고
    • Interleukin-12 and IL-18 synergistically induce the fungicidal activity of murine peritoneal exudate cells against Cryptococcus neoformans through production of γ interferon by natural killer cells
    • Zhang, T., K. Kawakamo, M. Qureshi, H. Okamura, M. Kurimoto, and A. Saito. 1997. Interleukin-12 and IL-18 synergistically induce the fungicidal activity of murine peritoneal exudate cells against Cryptococcus neoformans through production of γ interferon by natural killer cells. Infect. Immun. 65:3594.
    • (1997) Infect. Immun. , vol.65 , pp. 3594
    • Zhang, T.1    Kawakamo, K.2    Qureshi, M.3    Okamura, H.4    Kurimoto, M.5    Saito, A.6
  • 7
    • 0030933144 scopus 로고    scopus 로고
    • Interleukin 18 together with interleukin 12 inhibits IgE production by induction of interferon-γ production from activated B cells
    • Yoshimoto T., H. Okamura, Y.-I. Tagawa, Y. Iwakura, and K. Nakanishi. 1997. Interleukin 18 together with interleukin 12 inhibits IgE production by induction of interferon-γ production from activated B cells. Proc. Natl. Acad. Sci. USA 94:3948.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3948
    • Yoshimoto, T.1    Okamura, H.2    Tagawa, Y.-I.3    Iwakura, Y.4    Nakanishi, K.5
  • 13
    • 0031572443 scopus 로고    scopus 로고
    • IL-18 accounts for both TNF-α and Fas ligand-mediated hepatotoxic pathways in endotoxin-induced liver injury in mice
    • Tsutsui, H., K. Matsui, N. Kawada, Y. Hyodo, N. Hayashi, H. Okumura, K. Higashino, and K. Nakanishi. 1997. IL-18 accounts for both TNF-α and Fas ligand-mediated hepatotoxic pathways in endotoxin-induced liver injury in mice. J. Immunol. 159:3961.
    • (1997) J. Immunol. , vol.159 , pp. 3961
    • Tsutsui, H.1    Matsui, K.2    Kawada, N.3    Hyodo, Y.4    Hayashi, N.5    Okumura, H.6    Higashino, K.7    Nakanishi, K.8
  • 14
    • 0030293444 scopus 로고    scopus 로고
    • IFN-γ-inducing factor up-regulates Fas ligand-mediated cytotoxic activity of murine natural killer cell clones
    • Tsutsui, H., K. Nakanishi, K. Matsui, K. Higashino, H. Okamura, Y. Miyazawa, and K. Kaneda. 1996. IFN-γ-inducing factor up-regulates Fas ligand-mediated cytotoxic activity of murine natural killer cell clones. J. Immunol. 157:3967.
    • (1996) J. Immunol. , vol.157 , pp. 3967
    • Tsutsui, H.1    Nakanishi, K.2    Matsui, K.3    Higashino, K.4    Okamura, H.5    Miyazawa, Y.6    Kaneda, K.7
  • 15
    • 0030766468 scopus 로고    scopus 로고
    • Interleukin-18 induces the sequential activation of natural killer cells and cytotoxic T lymphocytes to protect syngenic mice from transplantation with Meth A sarcoma
    • Micallef, M. J., T. Tanimoto, K. Kohno, M. Ikeda, and M. Kurimoto. 1997. Interleukin-18 induces the sequential activation of natural killer cells and cytotoxic T lymphocytes to protect syngenic mice from transplantation with Meth A sarcoma. Cancer Res. 57:4557.
    • (1997) Cancer Res. , vol.57 , pp. 4557
    • Micallef, M.J.1    Tanimoto, T.2    Kohno, K.3    Ikeda, M.4    Kurimoto, M.5
  • 16
  • 18
    • 17544389276 scopus 로고    scopus 로고
    • Interleukin-18 (IFN-γ-inducing factor) is produced by osteoblasts and acts via granulocyte/macrophage colony-stimulating factor and not via interferon-γ to inhibit osteoblast formation
    • Udagawa, N., N. J. Horwood, J. Elliott, A. Mackay, J. Owen, H. Okamura, M. Kurimoto, T. J. Chambers, T. J. Martin, and M. T. Gillespie. 1997. Interleukin-18 (IFN-γ-inducing factor) is produced by osteoblasts and acts via granulocyte/macrophage colony-stimulating factor and not via interferon-γ to inhibit osteoblast formation. J. Exp. Med. 185:1005.
    • (1997) J. Exp. Med. , vol.185 , pp. 1005
    • Udagawa, N.1    Horwood, N.J.2    Elliott, J.3    Mackay, A.4    Owen, J.5    Okamura, H.6    Kurimoto, M.7    Chambers, T.J.8    Martin, T.J.9    Gillespie, M.T.10
  • 20
    • 15144344777 scopus 로고    scopus 로고
    • Induction of interferon-γ inducing factor in the adrenal cortex
    • Conti, B., J. W. Jahng, C. Tinti, J. H. Son, and T. H. Joh. 1997. Induction of interferon-γ inducing factor in the adrenal cortex. J. Biol. Chem. 272:2035.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2035
    • Conti, B.1    Jahng, J.W.2    Tinti, C.3    Son, J.H.4    Joh, T.H.5
  • 22
    • 0032170972 scopus 로고    scopus 로고
    • Neutrophils deficient in PU.1 do not terminal differentiate or become functionally competent
    • Anderson, K. L., K. A. Smith, F. Pio, B. E. Torbett, and R. A. Maki. 1998. Neutrophils deficient in PU.1 do not terminal differentiate or become functionally competent. Blood 92:1576.
    • (1998) Blood , vol.92 , pp. 1576
    • Anderson, K.L.1    Smith, K.A.2    Pio, F.3    Torbett, B.E.4    Maki, R.A.5
  • 24
    • 0020435972 scopus 로고
    • Recombinant genomes which express chloramphenicol acetyltransferase in mammalian cells
    • Gorman, C. M., L. F. Moffat, and B, H. Howard. 1982. Recombinant genomes which express chloramphenicol acetyltransferase in mammalian cells. Mol. Cell. Biol. 2:1044.
    • (1982) Mol. Cell. Biol. , vol.2 , pp. 1044
    • Gorman, C.M.1    Moffat, L.F.2    Howard, B.H.3
  • 25
    • 0021100690 scopus 로고
    • Accurate transcription initiation by polymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam, J. D., R. M. Lebovitz, and R. G. Roeder. 1983. Accurate transcription initiation by polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11:1474.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 1474
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3
  • 27
    • 0027250364 scopus 로고
    • Recognition DNA sequences of interferon regulatory factor 1 (IRF-1) and IRF-2, regulators of cell growth and the interferon system
    • Tanaka, N., T. Kawakami, and T. Taniguchi. 1993. Recognition DNA sequences of interferon regulatory factor 1 (IRF-1) and IRF-2, regulators of cell growth and the interferon system. Mol. Cell. Biol. 13:4531.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4531
    • Tanaka, N.1    Kawakami, T.2    Taniguchi, T.3
  • 28
    • 0026461132 scopus 로고
    • Human interferon consensus sequence binding protein is a negative regulator of enhancer elements common to interferon-inducible genes
    • Weisz, A., P. Marx, R. Sharf, E. Appella, P. H. Driggers, K. Ozato, and B.-Z. Levi. 1992. Human interferon consensus sequence binding protein is a negative regulator of enhancer elements common to interferon-inducible genes. J. Biol. Chem. 267:25589.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25589
    • Weisz, A.1    Marx, P.2    Sharf, R.3    Appella, E.4    Driggers, P.H.5    Ozato, K.6    Levi, B.-Z.7
  • 31
    • 0031568533 scopus 로고    scopus 로고
    • Stimulation of macrophages by lipopolysaccharide alters the phosphorylation state, conformation, and function of PU.1 via activation of casein kinase II
    • Lodie, T. A., R. Savedra, Jr., D. T. Golenbock, C. P. van Beveren, R. A. Maki, and M. J. Fenton. 1997. Stimulation of macrophages by lipopolysaccharide alters the phosphorylation state, conformation, and function of PU.1 via activation of casein kinase II. J. Immunol. 158:1848.
    • (1997) J. Immunol. , vol.158 , pp. 1848
    • Lodie, T.A.1    Savedra R., Jr.2    Golenbock, D.T.3    Van Beveren, C.P.4    Maki, R.A.5    Fenton, M.J.6
  • 32
    • 0028977911 scopus 로고
    • IFN-γ and lipopolysaccharide induce DNA binding of transcription factor PU.1 in murine tissue macrophages
    • Shackelford, R., D. O. Adams, and S. P. Johnson. 1995. IFN-γ and lipopolysaccharide induce DNA binding of transcription factor PU.1 in murine tissue macrophages. J. Immunol. 154:1374.
    • (1995) J. Immunol. , vol.154 , pp. 1374
    • Shackelford, R.1    Adams, D.O.2    Johnson, S.P.3
  • 33
    • 0033555418 scopus 로고    scopus 로고
    • Differential requirement of IFN consensus sequence binding protein for the production of IL-12 and induction of Th1-type cells in response to IFN-γ
    • Wu, C.-Y., H. Maeda, C. Contursi, K. Ozato, and R. A. Seder. 1999. Differential requirement of IFN consensus sequence binding protein for the production of IL-12 and induction of Th1-type cells in response to IFN-γ. J. Immunol. 162:807.
    • (1999) J. Immunol. , vol.162 , pp. 807
    • Wu, C.-Y.1    Maeda, H.2    Contursi, C.3    Ozato, K.4    Seder, R.A.5
  • 34
    • 0030664056 scopus 로고    scopus 로고
    • Interferon consensus sequence binding protein-deficient mice display impaired resistance to intracellular infection due to a primary defect in interleukin 12 p40 induction
    • Scharton-Kersten, T., C. Contursi, A. Masumi, A. Sher, and K. Ozato. 1997. Interferon consensus sequence binding protein-deficient mice display impaired resistance to intracellular infection due to a primary defect in interleukin 12 p40 induction. J. Exp. Med. 186:1523.
    • (1997) J. Exp. Med. , vol.186 , pp. 1523
    • Scharton-Kersten, T.1    Contursi, C.2    Masumi, A.3    Sher, A.4    Ozato, K.5
  • 35
    • 0029067356 scopus 로고
    • Functional domain analysis of interferon consensus sequence binding protein (ICSBP) and its association with interferon regulatory factors
    • Shart, R., A. Azriel, F. Lejbkowicz, S. Winograde, R. Ehrlich, and B.-Z. Levi. 1995. Functional domain analysis of interferon consensus sequence binding protein (ICSBP) and its association with interferon regulatory factors. J. Biol. Chem. 270:13063.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13063
    • Shart, R.1    Azriel, A.2    Lejbkowicz, F.3    Winograde, S.4    Ehrlich, R.5    Levi, B.-Z.6
  • 36
    • 0030899516 scopus 로고    scopus 로고
    • Phosphorylation events modulate the ability of interferon consensus sequence binding protein to interact with interferon regulatory factors and to bind DNA
    • Sharf, R., D. Merara, A. Azriel, A. M. Thornton, K. Ozato, E. F. Petricoin, A. C. Larner, F. Schaper, H. Hauser, and B.-Z. Levi. 1997. Phosphorylation events modulate the ability of interferon consensus sequence binding protein to interact with interferon regulatory factors and to bind DNA. J. Biol. Chem. 272: 9785.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9785
    • Sharf, R.1    Merara, D.2    Azriel, A.3    Thornton, A.M.4    Ozato, K.5    Petricoin, E.F.6    Larner, A.C.7    Schaper, F.8    Hauser, H.9    Levi, B.-Z.10
  • 37
    • 0029763203 scopus 로고    scopus 로고
    • Pip, a lymphoid-restricted IRF, contains a regulatory domain that is important for autoinhibition and ternary complex formation with the ets factor PU.1
    • Brass, A. L., E. Kehrli, C. F. Eisenbeis, U. Storb, and H. Singh. 1996. Pip, a lymphoid-restricted IRF, contains a regulatory domain that is important for autoinhibition and ternary complex formation with the ets factor PU.1. Genes Dev. 10:2335.
    • (1996) Genes Dev. , vol.10 , pp. 2335
    • Brass, A.L.1    Kehrli, E.2    Eisenbeis, C.F.3    Storb, U.4    Singh, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.