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Volumn 63, Issue 3, 1998, Pages 395-404

Effect of proteasome inhibitors on monocytic IκB-α and -β depletion, NF-κB activation, and cytokine production

Author keywords

Interleukin 1 ; Interleukin 8; Lipopolysaccharide; Transcription factors; Tumor necrosis factor

Indexed keywords

CALPASTATIN; CYTOKINE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INHIBITOR PROTEIN; INTERLEUKIN 1BETA; INTERLEUKIN 8; LIPOPOLYSACCHARIDE; PROTEINASE INHIBITOR; TUMOR NECROSIS FACTOR;

EID: 0031931132     PISSN: 07415400     EISSN: None     Source Type: Journal    
DOI: 10.1002/jlb.63.3.395     Document Type: Article
Times cited : (63)

References (65)
  • 2
    • 0027264083 scopus 로고
    • Nuclear factor kappa B, a mediator of lipopolysaccharicle effects
    • Müller, J. M., Ziegler-Heitbrock, H. W. L., Baeuerle, P. A. (1993) Nuclear factor kappa B, a mediator of lipopolysaccharicle effects. Immunobiol. 187, 233-256.
    • (1993) Immunobiol. , vol.187 , pp. 233-256
    • Müller, J.M.1    Ziegler-Heitbrock, H.W.L.2    Baeuerle, P.A.3
  • 3
    • 0029900295 scopus 로고    scopus 로고
    • The tumor necrosis factor ligand and receptor families
    • Bazzoni, F., Beutler, B. (1996) The tumor necrosis factor ligand and receptor families. N. Engl. J. Med. 334, 1717-1725.
    • (1996) N. Engl. J. Med. , vol.334 , pp. 1717-1725
    • Bazzoni, F.1    Beutler, B.2
  • 4
    • 0028174061 scopus 로고
    • Function and activation of NF-κB in the immune system
    • Baeuerle, P. A., Henkel, T. (1994) Function and activation of NF-κB in the immune system. Annu. Rev. Immunol. 12, 141-179.
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 141-179
    • Baeuerle, P.A.1    Henkel, T.2
  • 6
    • 0025607864 scopus 로고
    • Human tumor necrosis factor α gene regulation by virus and lipopolysaccharide
    • Goldfeld, A. E., Doyle, C., Maniatis, T. (1990) Human tumor necrosis factor α gene regulation by virus and lipopolysaccharide. Proc. Natl. Acad. Sci. USA 87, 9769-9773.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9769-9773
    • Goldfeld, A.E.1    Doyle, C.2    Maniatis, T.3
  • 8
    • 0029068239 scopus 로고
    • Transcriptional activation of the human TNF-α promoter by superantigen in human monocytic cells: Role of NF-κB
    • Trede, N. S., Tsytsykova, A. L. Chatila, T., Goldfeld, A., Geha, R. S. (1995) Transcriptional activation of the human TNF-α promoter by superantigen in human monocytic cells: Role of NF-κB. J. Immunol. 155, 902-908.
    • (1995) J. Immunol. , vol.155 , pp. 902-908
    • Trede, N.S.1    Tsytsykova, A.L.2    Chatila, T.3    Goldfeld, A.4    Geha, R.S.5
  • 9
    • 0025776417 scopus 로고
    • Tissue factor mRNA in THP-1 monocytic cells is regulated at both transcriptional and posttranscriptional levels in response to lipopolysaccharide
    • Brand, K., Fowler, T. S., Mackman, N. (1991) Tissue factor mRNA in THP-1 monocytic cells is regulated at both transcriptional and posttranscriptional levels in response to lipopolysaccharide. Mol. Cell. Biol. 11, 4732-4738.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4732-4738
    • Brand, K.1    Fowler, T.S.2    Mackman, N.3
  • 10
    • 0025720571 scopus 로고
    • Lipopolysaccharide-mediated transcriptional activation of the human tissue factor gene in THP-1 monocytic cells requires both activator protein 1 and nuclear factor κB binding sites
    • Mackman, N., Brand, K., Edgington, T. S. (1991) Lipopolysaccharide-mediated transcriptional activation of the human tissue factor gene in THP-1 monocytic cells requires both activator protein 1 and nuclear factor κB binding sites. J. Exp. Med. 174, 1517-1526.
    • (1991) J. Exp. Med. , vol.174 , pp. 1517-1526
    • Mackman, N.1    Brand, K.2    Edgington, T.S.3
  • 11
    • 0027379055 scopus 로고
    • Distinct mechanisms for regulation of the interleukin-8 gene involve synergism and cooperativity between C/EBP and NF-κB
    • Stein, B., Baldwin, A. S. (1993) Distinct mechanisms for regulation of the interleukin-8 gene involve synergism and cooperativity between C/EBP and NF-κB. Mol. Cell. Biol. 13, 7191-7198.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7191-7198
    • Stein, B.1    Baldwin, A.S.2
  • 12
    • 0027384590 scopus 로고
    • NF-κB subunit-specific regulation of the interleukin-8 promoter
    • Kunsch, C., Rosen, C. A. (1993). NF-κB subunit-specific regulation of the interleukin-8 promoter. Mol. Cell. Biol. 13, 6146-6173.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6146-6173
    • Kunsch, C.1    Rosen, C.A.2
  • 13
    • 0027453552 scopus 로고
    • Transcription factors NF-IL6 and NF-κB synergistically activate transcription of the inflammatory cytokines, interleukin 6 and interleukin 8
    • Matsusaka, T., Fujikawa, K., Nishio, Y., Mukaida, N., Matsushima, K., Kishimoto, T., Akira, S. (1993) Transcription factors NF-IL6 and NF-κB synergistically activate transcription of the inflammatory cytokines, interleukin 6 and interleukin 8. Proc. Natl. Acad. Sci. USA 90, 10193-10197.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10193-10197
    • Matsusaka, T.1    Fujikawa, K.2    Nishio, Y.3    Mukaida, N.4    Matsushima, K.5    Kishimoto, T.6    Akira, S.7
  • 14
    • 0028176449 scopus 로고
    • The interleukin-8, AP-1, and κB-like sites are genetic end targets of FK506-sensitive pathway accompanied by calcium mobilization
    • Okamoto, S., Mukaida, N., Yasumoto, K., Rice, N., Ishikawa, Y., Horiguchi, H., Murakami, S., Matsushima, K. (1994) The interleukin-8, AP-1, and κB-like sites are genetic end targets of FK506-sensitive pathway accompanied by calcium mobilization. J. Biol. Chem. 269, 8582-8589.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8582-8589
    • Okamoto, S.1    Mukaida, N.2    Yasumoto, K.3    Rice, N.4    Ishikawa, Y.5    Horiguchi, H.6    Murakami, S.7    Matsushima, K.8
  • 15
    • 0027454228 scopus 로고
    • Association between protooncoproteins rel and TATA-binding protein mediates transcriptional activation by NF-κB
    • Kerr, L. D., Ransone, L. J., Wamsley, P., Schmitt, M. J., Boyer, T. G., Zhou, Q., Berk, A. J., Verma, I. M. (1993) Association between protooncoproteins rel and TATA-binding protein mediates transcriptional activation by NF-κB. Nature 365, 412-419.
    • (1993) Nature , vol.365 , pp. 412-419
    • Kerr, L.D.1    Ransone, L.J.2    Wamsley, P.3    Schmitt, M.J.4    Boyer, T.G.5    Zhou, Q.6    Berk, A.J.7    Verma, I.M.8
  • 16
    • 0026499517 scopus 로고
    • The regulation of the human tumor necrosis factor a promoter region in macrophage, T cell, and B cell lines
    • Rhoades, K., Golub, S. H., Economou, J. S. (1992) The regulation of the human tumor necrosis factor a promoter region in macrophage, T cell, and B cell lines. J. Biol. Chem. 267, 22102-22107.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22102-22107
    • Rhoades, K.1    Golub, S.H.2    Economou, J.S.3
  • 17
    • 0026608675 scopus 로고
    • The core promoter region of the tumor necrosis factor a gene confers phorbol ester responsiveness to upstream transcriptional activators
    • Leitman, D. C., Mackow, E. R., Williams, T., Baxter, J. D., West, B. L. (1992) The core promoter region of the tumor necrosis factor a gene confers phorbol ester responsiveness to upstream transcriptional activators. Mol. Cell Biol. 12, 1352-1356.
    • (1992) Mol. Cell Biol. , vol.12 , pp. 1352-1356
    • Leitman, D.C.1    Mackow, E.R.2    Williams, T.3    Baxter, J.D.4    West, B.L.5
  • 18
    • 0027326457 scopus 로고
    • Identification of a novel cyclosporin-sensitive element in the human tumor necrosis α gene promoter
    • Goldfeld, A. E., McCaffrey, P. G., Strominger, J. L., Rao, A. (1993) Identification of a novel cyclosporin-sensitive element in the human tumor necrosis α gene promoter. J. Exp. Med. 178, 1365-1379.
    • (1993) J. Exp. Med. , vol.178 , pp. 1365-1379
    • Goldfeld, A.E.1    McCaffrey, P.G.2    Strominger, J.L.3    Rao, A.4
  • 19
    • 0029610889 scopus 로고
    • Interleukin-1 and interleukin-6 gene expression in human monocytes stimulated with Salmonella typhimurium porins
    • Galdiero, M., Cippolaro-de-L'ero, G., Donnarumma, G., Marcatili, A., Galdiero, F. (1995) Interleukin-1 and interleukin-6 gene expression in human monocytes stimulated with Salmonella typhimurium porins. Immunol. 86, 612-619.
    • (1995) Immunol. , vol.86 , pp. 612-619
    • Galdiero, M.1    Cippolaro-de-L'ero, G.2    Donnarumma, G.3    Marcatili, A.4    Galdiero, F.5
  • 20
    • 0028931318 scopus 로고
    • Regulation of the human TNF promoter by the transcription factor Ets
    • Kramer, B., Wiegmann, K., Krönke, M. (1995) Regulation of the human TNF promoter by the transcription factor Ets. J. Biol. Chem. 270, 6577-6583.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6577-6583
    • Kramer, B.1    Wiegmann, K.2    Krönke, M.3
  • 21
    • 0028880833 scopus 로고
    • Superantigen-induced transcriptional activation of the human TNF gene promoter in T cells
    • Kramer, B., Machleidt, T., Wiegmann, K., Krönke, M. (1995) Superantigen-induced transcriptional activation of the human TNF gene promoter in T cells. J. Inflamm. 45, 183-192.
    • (1995) J. Inflamm. , vol.45 , pp. 183-192
    • Kramer, B.1    Machleidt, T.2    Wiegmann, K.3    Krönke, M.4
  • 22
    • 0029940394 scopus 로고    scopus 로고
    • Recombinant NFATl (NFATp) is regulated by calcineurin in T cells and mediates transcription of several cytokine genes
    • Luo, C., Burgeon, E., Carew, J. A., McCaffrey, P. G., Badalian, T. M., Lane, W. S., Hogan, P. G., Rao, A. (1996) Recombinant NFATl (NFATp) is regulated by calcineurin in T cells and mediates transcription of several cytokine genes. Mol. Cell. Biol. 16, 3955-3966.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3955-3966
    • Luo, C.1    Burgeon, E.2    Carew, J.A.3    McCaffrey, P.G.4    Badalian, T.M.5    Lane, W.S.6    Hogan, P.G.7    Rao, A.8
  • 23
    • 0024475227 scopus 로고
    • NF-κB: A pleiotropic mediator of inducible and tissue-specific gene control
    • Lenardo, M. J., Baltimore, D. (1989) NF-κB: a pleiotropic mediator of inducible and tissue-specific gene control. Cell 58, 227-229.
    • (1989) Cell , vol.58 , pp. 227-229
    • Lenardo, M.J.1    Baltimore, D.2
  • 24
    • 0027232067 scopus 로고
    • NF-κB and Rel: Participants in a multiform transcriptional regulatory system
    • Grilli, M., Chiu, J. J.-S., Lenardo, M. J. (1993) NF-κB and Rel: participants in a multiform transcriptional regulatory system. Int. Rev. Cytol. 143, 1-62.
    • (1993) Int. Rev. Cytol. , vol.143 , pp. 1-62
    • Grilli, M.1    Chiu, J.J.-S.2    Lenardo, M.J.3
  • 25
    • 0029874138 scopus 로고    scopus 로고
    • The NF-κB and IκB proteins: New discoveries and insights
    • Baldwin, A. S. (1996) The NF-κB and IκB proteins: New discoveries and insights. Annu. Rev. Immunol. 14, 649-681.
    • (1996) Annu. Rev. Immunol. , vol.14 , pp. 649-681
    • Baldwin, A.S.1
  • 26
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB
    • Palombella, V. J., Rando, O. J., Goldberg, A. L., Maniatis, T. (1994) The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB. Cell 78, 773-785.
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 27
    • 0028986193 scopus 로고
    • NF-κB: A lesson in family values
    • Thanos, D., Maniatis, T. (1995) NF-κB: a lesson in family values. Cell 80, 529-532.
    • (1995) Cell , vol.80 , pp. 529-532
    • Thanos, D.1    Maniatis, T.2
  • 28
    • 0028986194 scopus 로고
    • IκB-β regulates the persistent response in a biphasic activation of NF-κB
    • Thompson, J. E., Phillips, R. J., Erdjument-Bromage, H., Tempst, P., Ghosh, S. (1995) IκB-β regulates the persistent response in a biphasic activation of NF-κB. Cell 80, 573-582.
    • (1995) Cell , vol.80 , pp. 573-582
    • Thompson, J.E.1    Phillips, R.J.2    Erdjument-Bromage, H.3    Tempst, P.4    Ghosh, S.5
  • 29
    • 0030899121 scopus 로고    scopus 로고
    • I kappa B epsilon, a novel member of the IκB family, controls RelA and cRel NF-κB activity
    • Whiteside, S. T., Epinat, J.-C., Rice, N. R., Israel, A. (1997) I kappa B epsilon, a novel member of the IκB family, controls RelA and cRel NF-κB activity. EMBO J. 16, 1413-1426.
    • (1997) EMBO J. , vol.16 , pp. 1413-1426
    • Whiteside, S.T.1    Epinat, J.-C.2    Rice, N.R.3    Israel, A.4
  • 30
    • 0028965644 scopus 로고
    • Receptor-dependent mechanisms of cell stimulation by bacterial endotoxin
    • Ulevitch, R. J., Tobias, P. S. (1995) Receptor-dependent mechanisms of cell stimulation by bacterial endotoxin. Annu. Rev. Immunol. 13, 437-457.
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 437-457
    • Ulevitch, R.J.1    Tobias, P.S.2
  • 31
    • 0027176524 scopus 로고
    • Rapid proteolysis of IκB-α is necessary for activation of transcription factor NF-κB
    • Henkel, T., Machleidt, T., Alkalay, I., Krönke, M., Ben-Neriah, Y., Baeuerle, P. A. (1993) Rapid proteolysis of IκB-α is necessary for activation of transcription factor NF-κB. Nature 365, 182-185.
    • (1993) Nature , vol.365 , pp. 182-185
    • Henkel, T.1    Machleidt, T.2    Alkalay, I.3    Krönke, M.4    Ben-Neriah, Y.5    Baeuerle, P.A.6
  • 32
    • 0028148227 scopus 로고
    • A proteasome inhibitor prevents activation of NF-κB and stabilizes a newly phosphorylated form of IκB-α that is still bound to NF-κB
    • Traenckner, E. B.-M., Wilk, S., Baeuerle, P. A. (1994) A proteasome inhibitor prevents activation of NF-κB and stabilizes a newly phosphorylated form of IκB-α that is still bound to NF-κB. EMBO J. 13, 5433-5441.
    • (1994) EMBO J. , vol.13 , pp. 5433-5441
    • Traenckner, E.B.-M.1    Wilk, S.2    Baeuerle, P.A.3
  • 33
    • 0028970734 scopus 로고
    • Stimulation-dependent IκB-α phosphorylation marks the NF-κB inhibitor for degradation via the ubiquitin-proteasome pathway
    • Alkalay, I., Yaron, A., Hatzubai, A., Orian, A., Ciechanover, A., Ben-Neriah, Y. (1995) Stimulation-dependent IκB-α phosphorylation marks the NF-κB inhibitor for degradation via the ubiquitin-proteasome pathway. Proc. Natl. Acad. Sci. USA 92, 10599-10603.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10599-10603
    • Alkalay, I.1    Yaron, A.2    Hatzubai, A.3    Orian, A.4    Ciechanover, A.5    Ben-Neriah, Y.6
  • 34
    • 0028981050 scopus 로고
    • Activation of NF-κB requires proteolysis of the inhibitor IκB-α: Signal-induced phosphorylation of IκB-α alone does not release active NF-κB
    • Lin, Y., Brown, K., Siebenlist, U. (1995) Activation of NF-κB requires proteolysis of the inhibitor IκB-α: signal-induced phosphorylation of IκB-α alone does not release active NF-κB. Proc. Natl. Acad. Sci. USA 92, 552-556.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 552-556
    • Lin, Y.1    Brown, K.2    Siebenlist, U.3
  • 37
    • 0030271387 scopus 로고    scopus 로고
    • NF-κB: Ten years after
    • Baeuerle, P. A., Baltimore, D. (1996) NF-κB: Ten years after. Cell 87, 13-20.
    • (1996) Cell , vol.87 , pp. 13-20
    • Baeuerle, P.A.1    Baltimore, D.2
  • 38
    • 0029664304 scopus 로고    scopus 로고
    • Proteasome inhibitors block VCAM-1 and ICAM-1 gene expression in endothelial cells without affecting nuclear translocation of nuclear factor-κB
    • Cobb, R. R., Felts, K. A., Parry, G. C. N., Mackman, N. (1996) Proteasome inhibitors block VCAM-1 and ICAM-1 gene expression in endothelial cells without affecting nuclear translocation of nuclear factor-κB. Eur. J. Immunol. 26, 839-845.
    • (1996) Eur. J. Immunol. , vol.26 , pp. 839-845
    • Cobb, R.R.1    Felts, K.A.2    Parry, G.C.N.3    Mackman, N.4
  • 39
    • 0028985248 scopus 로고
    • Proteolytic processing of NF-κB/IκB in human monocytes
    • Donald, R., Ballard, D. W., Hawiger, J. (1995) Proteolytic processing of NF-κB/IκB in human monocytes. J. Biol. Chem. 270, 9-12.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9-12
    • Donald, R.1    Ballard, D.W.2    Hawiger, J.3
  • 40
    • 0031081019 scopus 로고    scopus 로고
    • N-Acetyl-leucinyl-leucinyl-norleucinal inhibits lipopolysaccharide-induced NF-κB activation and prevents TNF and IL-6 synthesis in vivo
    • Schow, S. R., Joly, A. (1997) N-Acetyl-leucinyl-leucinyl-norleucinal inhibits lipopolysaccharide-induced NF-κB activation and prevents TNF and IL-6 synthesis in vivo. Cell Immunol. 175, 199-202.
    • (1997) Cell Immunol. , vol.175 , pp. 199-202
    • Schow, S.R.1    Joly, A.2
  • 41
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock, K. L., Gramm, C., Rothstein, L., Clark, K., Stein, R., Dick, L., Hwang, D., Goldberg, D. (1994) Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78, 761-771.
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, D.8
  • 42
    • 0025820405 scopus 로고
    • Evidence that agonist-induced activation of calpain causes the shedding of procoagulant-containing microvesicles from the membrane of aggregating platelets
    • Fox, J. E. B., Austin, C. D., Reynolds, C. C., Steffen, P. K. (1991) Evidence that agonist-induced activation of calpain causes the shedding of procoagulant-containing microvesicles from the membrane of aggregating platelets. J. Biol. Chem. 20, 13289-13295.
    • (1991) J. Biol. Chem. , vol.20 , pp. 13289-13295
    • Fox, J.E.B.1    Austin, C.D.2    Reynolds, C.C.3    Steffen, P.K.4
  • 43
    • 0024593798 scopus 로고
    • Inhibition of calpain in intact platelets by the thiol protease inhibitor E-64d
    • McGowan, E. B., Becker, E., Detweiler, T. C. (1989) Inhibition of calpain in intact platelets by the thiol protease inhibitor E-64d. Biochem. Biophys. Res. Commun. 158, 432-435.
    • (1989) Biochem. Biophys. Res. Commun. , vol.158 , pp. 432-435
    • McGowan, E.B.1    Becker, E.2    Detweiler, T.C.3
  • 44
    • 0026742378 scopus 로고
    • Inhibition of cysteine proteinases in lysosomes and whole cells
    • Wilcox, D., Mason, R. W. (1992) Inhibition of cysteine proteinases in lysosomes and whole cells. Biochem. J. 285, 495-502.
    • (1992) Biochem. J. , vol.285 , pp. 495-502
    • Wilcox, D.1    Mason, R.W.2
  • 46
    • 0028293250 scopus 로고
    • Comparison of the effect of calpain inhibitors on two extralysosomal proteinases: The multicatalytic proteinase complex and m-calpain
    • Figueiredo-Pereira, M. E., Banik, N., Wilk, S. (1994) Comparison of the effect of calpain inhibitors on two extralysosomal proteinases: the multicatalytic proteinase complex and m-calpain. J. Neurochem. 62, 1989-1994.
    • (1994) J. Neurochem. , vol.62 , pp. 1989-1994
    • Figueiredo-Pereira, M.E.1    Banik, N.2    Wilk, S.3
  • 47
    • 0027233082 scopus 로고
    • Interferon-γ inhibits macrophage apolipoprotein E production by posttranslational mechanisms
    • Brand, K., Mackman, N., Curtiss, L. K. (1993) Interferon-γ inhibits macrophage apolipoprotein E production by posttranslational mechanisms. J. Clin. Invest. 91, 2031-2039.
    • (1993) J. Clin. Invest. , vol.91 , pp. 2031-2039
    • Brand, K.1    Mackman, N.2    Curtiss, L.K.3
  • 48
    • 0028214529 scopus 로고
    • Oxidized low density lipoprotein enhances lipopolysaccharide-induced tissue factor expression in human adherent monocytes
    • Brand, K., Banca, C. L., Mackman, N., Terkeltaub, R. A., Fan, S. T., Curtiss, L. K. (1994) Oxidized low density lipoprotein enhances lipopolysaccharide-induced tissue factor expression in human adherent monocytes. Arterioscler. Thromb. 14, 790-797.
    • (1994) Arterioscler. Thromb. , vol.14 , pp. 790-797
    • Brand, K.1    Banca, C.L.2    Mackman, N.3    Terkeltaub, R.A.4    Fan, S.T.5    Curtiss, L.K.6
  • 49
    • 0029688891 scopus 로고    scopus 로고
    • Analysis of promoter activity by polymerase chain reaction amplification of reporter gene mRNA
    • Kastenbauer, S., Wedel, A., Frankenberger, M., Wirth, T., Ziegler-Heitbrock, H. W. L. (1996) Analysis of promoter activity by polymerase chain reaction amplification of reporter gene mRNA. Anal. Biochem. 233, 137-139.
    • (1996) Anal. Biochem. , vol.233 , pp. 137-139
    • Kastenbauer, S.1    Wedel, A.2    Frankenberger, M.3    Wirth, T.4    Ziegler-Heitbrock, H.W.L.5
  • 50
    • 0028945987 scopus 로고
    • Isolation of the human interleukin 10 promoter, characterization of the promoter activity in Burkitt's lymphoma cell lines
    • Kube, D., Platzer, C., Von Knethen, A., Straub, H., Bohlen, H., Hafner, M., Tesch, H. (1995) Isolation of the human interleukin 10 promoter, characterization of the promoter activity in Burkitt's lymphoma cell lines. Cytokine 7, 1-7.
    • (1995) Cytokine , vol.7 , pp. 1-7
    • Kube, D.1    Platzer, C.2    Von Knethen, A.3    Straub, H.4    Bohlen, H.5    Hafner, M.6    Tesch, H.7
  • 51
    • 0025186678 scopus 로고
    • κB-type enhancers are involved in lipopolysaccharidemediated transcriptional activation of the tumor necrosis factor α gene in primary macrophages
    • Shakhov, A. N., Collart, M. A., Vassalli, P., Nedospasov, S. A., Jongeneel, C. V. (1990) κB-type enhancers are involved in lipopolysaccharidemediated transcriptional activation of the tumor necrosis factor α gene in primary macrophages. J. Exp. Med. 171, 35-47.
    • (1990) J. Exp. Med. , vol.171 , pp. 35-47
    • Shakhov, A.N.1    Collart, M.A.2    Vassalli, P.3    Nedospasov, S.A.4    Jongeneel, C.V.5
  • 53
    • 0030894683 scopus 로고    scopus 로고
    • Activation of the transcription factor MEF2C by the MAP kinase p38 in inflammation
    • Han, J., Jiang, Y., Li, Z., Kravchenko, V. V., Ulevitch, R. J. (1997) Activation of the transcription factor MEF2C by the MAP kinase p38 in inflammation. Nature 386, 296-299.
    • (1997) Nature , vol.386 , pp. 296-299
    • Han, J.1    Jiang, Y.2    Li, Z.3    Kravchenko, V.V.4    Ulevitch, R.J.5
  • 54
    • 0029010658 scopus 로고
    • The proteasome pathway is required for cytokine-induced endothelial leukocyte adhesion molecule expression
    • Read, M. A., Neish, A. S., Luscinskas, F. W., Palombella, V. J., Maniatis, T., Collins, T. (1995) The proteasome pathway is required for cytokine-induced endothelial leukocyte adhesion molecule expression. Immunity 2, 493-506.
    • (1995) Immunity , vol.2 , pp. 493-506
    • Read, M.A.1    Neish, A.S.2    Luscinskas, F.W.3    Palombella, V.J.4    Maniatis, T.5    Collins, T.6
  • 55
    • 0029132707 scopus 로고
    • Identification and initial characterization of a specific proteasome (prosome) associated RNase activity
    • Pouch, M.-N., Petit, F., Buri, J., Briand, Y., Schmid, H.-P. (1995) Identification and initial characterization of a specific proteasome (prosome) associated RNase activity. J. Biol. Chem. 270, 22023-22028.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22023-22028
    • Pouch, M.-N.1    Petit, F.2    Buri, J.3    Briand, Y.4    Schmid, H.-P.5
  • 56
    • 0029666281 scopus 로고    scopus 로고
    • A sustained reduction in IκB-β may contribute to persistent NF-κB activation in human endothelial cells
    • Johnson, D. R., Douglas, I., Jahnke, A., Ghosh, S., Pober, J. S. (1996) A sustained reduction in IκB-β may contribute to persistent NF-κB activation in human endothelial cells. J. Biol. Chem. 271, 16317-16322.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16317-16322
    • Johnson, D.R.1    Douglas, I.2    Jahnke, A.3    Ghosh, S.4    Pober, J.S.5
  • 57
    • 0026503828 scopus 로고
    • The mechanism and functions of ATP-dependent proteases in bacterial and animal cells
    • Goldberg, A. L. (1992) The mechanism and functions of ATP-dependent proteases in bacterial and animal cells. Eur. J. Biochem. 203, 9-23.
    • (1992) Eur. J. Biochem. , vol.203 , pp. 9-23
    • Goldberg, A.L.1
  • 58
    • 0027516156 scopus 로고
    • Proteasomes: Multicatalytic proteinase complexes
    • Rivett, A. J. (1993) Proteasomes: multicatalytic proteinase complexes. Biochem. J. 291, 1-10.
    • (1993) Biochem. J. , vol.291 , pp. 1-10
    • Rivett, A.J.1
  • 59
    • 0029867623 scopus 로고    scopus 로고
    • Proteasomes: Destruction as a programme
    • Hilt, W., Wolf, D. H. (1996) Proteasomes: destruction as a programme. Trends Biol. Sci. 21, 96-102.
    • (1996) Trends Biol. Sci. , vol.21 , pp. 96-102
    • Hilt, W.1    Wolf, D.H.2
  • 60
    • 0028817874 scopus 로고
    • The cleavage preference of the proteasome governs the yield of antigenic peptides
    • Eggers, M., Boes-Fabian, B., Ruppert, T., Kloetzel, P.-M, Koszinowski, U. H. (1995) The cleavage preference of the proteasome governs the yield of antigenic peptides. J. Exp. Med. 182, 1865-1870.
    • (1995) J. Exp. Med. , vol.182 , pp. 1865-1870
    • Eggers, M.1    Boes-Fabian, B.2    Ruppert, T.3    Kloetzel, P.-M.4    Koszinowski, U.H.5
  • 61
    • 0029162601 scopus 로고
    • Incorporation of major histocompatibility complex-encoded subunits LMP2 and LMP7 changes the quality of the 20S proteasome polypeptide processing products independent of interferon-γ
    • Kuckelkorn, U., Frentzel, S., Kraft, R., Kostka, S., Groettrup, M., Kloetzel, P.-M. (1995) Incorporation of major histocompatibility complex-encoded subunits LMP2 and LMP7 changes the quality of the 20S proteasome polypeptide processing products independent of interferon-γ. Eur. J. Immunol. 25, 2605-2611.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 2605-2611
    • Kuckelkorn, U.1    Frentzel, S.2    Kraft, R.3    Kostka, S.4    Groettrup, M.5    Kloetzel, P.-M.6
  • 62
    • 0029912242 scopus 로고    scopus 로고
    • Inhibitors of the proteasome pathway interfere with the induction of nitric oxide synthase in macrophages by blocking activation of transcription factor NF-κB
    • Griscavage, J. M., Wilk, S., Ignarro, L. J. (1996) Inhibitors of the proteasome pathway interfere with the induction of nitric oxide synthase in macrophages by blocking activation of transcription factor NF-κB. Proc. Natl. Acad. Sci. USA 93, 3308-3312.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3308-3312
    • Griscavage, J.M.1    Wilk, S.2    Ignarro, L.J.3
  • 65
    • 0030183959 scopus 로고    scopus 로고
    • Endotoxin-related intracellular pathways: Implications for therapeutic intervention
    • Ulevitch, R. J., Dunn, D. L., Fink, M. P., Taylor, C. E. (1996) Endotoxin-related intracellular pathways: implications for therapeutic intervention. Shock 6, 1-2.
    • (1996) Shock , vol.6 , pp. 1-2
    • Ulevitch, R.J.1    Dunn, D.L.2    Fink, M.P.3    Taylor, C.E.4


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