메뉴 건너뛰기




Volumn 243, Issue 2, 1998, Pages 425-433

Lipopolysaccharide-induced NF-κB activation in human endothelial cells involves degradation of Iκbα but not Iκb̄

Author keywords

Endothelial; Herbimycin A; I B ; Lipopolysaccharide; Tyrosine kinase

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LIPOPOLYSACCHARIDE; MESSENGER RNA;

EID: 0032531208     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.1998.4162     Document Type: Article
Times cited : (31)

References (62)
  • 1
    • 0025271844 scopus 로고
    • Tumor necrosis factor-α induction of novel gene products in human endothelial cells including a macrophage-specific chemotaxin
    • Dixit V. M., Green S., Sarma V., Holzman L. B., Wolf F. W., O'Rourke K., Ward P. A., Prochownik E. V., Marks R. M. Tumor necrosis factor-α induction of novel gene products in human endothelial cells including a macrophage-specific chemotaxin. J. Biol. Chem. 265:1990;2973-2978.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2973-2978
    • Dixit, V.M.1    Green, S.2    Sarma, V.3    Holzman, L.B.4    Wolf, F.W.5    O'Rourke, K.6    Ward, P.A.7    Prochownik, E.V.8    Marks, R.M.9
  • 2
    • 0026691240 scopus 로고
    • The A20 zinc finger protein protects cells from tumor necrosis factor cytotoxicity
    • Opipari A. W. J., Hu H. M., Yabkowitz R., Dixit V. M. The A20 zinc finger protein protects cells from tumor necrosis factor cytotoxicity. J. Biol. Chem. 267:1992;12424-12427.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12424-12427
    • Opipari, A.W.J.1    Hu, H.M.2    Yabkowitz, R.3    Dixit, V.M.4
  • 3
    • 0028850937 scopus 로고
    • Lymphoid expression and regulation of A20, an inhibitor of programmed cell death
    • Tewari M., Wolf F. W., Seldin M. F., O'Shea K. S., Dixit V. M., Turka L. A. Lymphoid expression and regulation of A20, an inhibitor of programmed cell death. J. Immunol. 154:1995;1699-1706.
    • (1995) J. Immunol. , vol.154 , pp. 1699-1706
    • Tewari, M.1    Wolf, F.W.2    Seldin, M.F.3    O'Shea, K.S.4    Dixit, V.M.5    Turka, L.A.6
  • 4
    • 0024564509 scopus 로고
    • Human endothelial cell response to lipopolysaccharide, interleukin-1, and tumor necrosis factor is regulated by protein synthesis
    • Pohlman T. H., Harlan J. M. Human endothelial cell response to lipopolysaccharide, interleukin-1, and tumor necrosis factor is regulated by protein synthesis. Cell. Immunol. 119:1989;41-52.
    • (1989) Cell. Immunol. , vol.119 , pp. 41-52
    • Pohlman, T.H.1    Harlan, J.M.2
  • 5
    • 0027971199 scopus 로고
    • Induction of endothelial cell apoptosis by TNF-α: Modulation by inhibitors of protein synthesis
    • Polunovsky V. A., Wendt C. H., Ingbar D. H., Peterson M. S., Bitterman P. B. Induction of endothelial cell apoptosis by TNF-α: Modulation by inhibitors of protein synthesis. Exp. Cell Res. 214:1994;584-594.
    • (1994) Exp. Cell Res. , vol.214 , pp. 584-594
    • Polunovsky, V.A.1    Wendt, C.H.2    Ingbar, D.H.3    Peterson, M.S.4    Bitterman, P.B.5
  • 7
    • 0029861518 scopus 로고    scopus 로고
    • Endothelial cell death induced by tumor necrosis factor-α is inhibited by the Bcl-2 family member, A1
    • Karsan A., Yee E., Harlan J. M. Endothelial cell death induced by tumor necrosis factor-α is inhibited by the Bcl-2 family member, A1. J. Biol. Chem. 271:1996;27201-27204.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27201-27204
    • Karsan, A.1    Yee, E.2    Harlan, J.M.3
  • 8
    • 0030026698 scopus 로고    scopus 로고
    • A20 zinc finger protein inhibits TNF and IL-1 signaling
    • Jaattela M., Mouritzen H., Elling F., Bastholm L. A20 zinc finger protein inhibits TNF and IL-1 signaling. J. Immunol. 156:1996;1166-1173.
    • (1996) J. Immunol. , vol.156 , pp. 1166-1173
    • Jaattela, M.1    Mouritzen, H.2    Elling, F.3    Bastholm, L.4
  • 9
    • 0000564581 scopus 로고    scopus 로고
    • The tumor necrosis factor-inducible zinc finger protein A20 interacts with TRAF1/TRAF2 and inhibits NF-κB activation
    • Song H. Y., Rothe M., Goeddel D. V. The tumor necrosis factor-inducible zinc finger protein A20 interacts with TRAF1/TRAF2 and inhibits NF-κB activation. Proc. Natl. Acad. Sci. USA. 93:1996;6721-6725.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6721-6725
    • Song, H.Y.1    Rothe, M.2    Goeddel, D.V.3
  • 10
    • 0029829237 scopus 로고    scopus 로고
    • 14-3-3 proteins associate with A20 in an isoform-specific manner and function both as chaperone and adapter molecules
    • Vincenz C., Dixit V. M. 14-3-3 proteins associate with A20 in an isoform-specific manner and function both as chaperone and adapter molecules. J. Biol. Chem. 271:1996;20029-20034.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20029-20034
    • Vincenz, C.1    Dixit, V.M.2
  • 11
    • 0029874138 scopus 로고    scopus 로고
    • The NF-κB and IκB proteins: New discoveries and insights
    • Baldwin A. S. J. The NF-κB and IκB proteins: new discoveries and insights. Annu. Rev. Immunol. 14:1996;649-683.
    • (1996) Annu. Rev. Immunol. , vol.14 , pp. 649-683
    • Baldwin, A.S.J.1
  • 12
    • 0028179224 scopus 로고
    • NF-κB and IκBα: An inducible regulatory system in endothelial activation
    • Read M. A., Whitley M. Z., Williams A. J., Collins T. NF-κB and IκBα: An inducible regulatory system in endothelial activation. J. Exp. Med. 179:1994;503-512.
    • (1994) J. Exp. Med. , vol.179 , pp. 503-512
    • Read, M.A.1    Whitley, M.Z.2    Williams, A.J.3    Collins, T.4
  • 13
    • 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. The proteasome pathway is required for cytokine-induced endothelial-leukocyte adhesion molecule expression. Immunity. 2:1995;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
  • 15
    • 0029007855 scopus 로고
    • The TNF receptor 1-associated protein TRADD signals cell death and NF-κB activation
    • Hsu H., Xiong J., Goeddel D. V. The TNF receptor 1-associated protein TRADD signals cell death and NF-κB activation. Cell. 81:1995;495-504.
    • (1995) Cell , vol.81 , pp. 495-504
    • Hsu, H.1    Xiong, J.2    Goeddel, D.V.3
  • 16
    • 0030032106 scopus 로고    scopus 로고
    • TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways
    • Hsu H., Shu H. B., Pan M. G., Goeddel D. V. TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways. Cell. 84:1996;299-308.
    • (1996) Cell , vol.84 , pp. 299-308
    • Hsu, H.1    Shu, H.B.2    Pan, M.G.3    Goeddel, D.V.4
  • 17
    • 0030298294 scopus 로고    scopus 로고
    • Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-κB activation prevents cell death
    • Liu Z. G., Hsu H., Goeddel D. V., Karin M. Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-κB activation prevents cell death. Cell. 87:1996;565-576.
    • (1996) Cell , vol.87 , pp. 565-576
    • Liu, Z.G.1    Hsu, H.2    Goeddel, D.V.3    Karin, M.4
  • 19
    • 0027194212 scopus 로고
    • Endotoxin-mediated endothelial cell injury and activation: Role of soluble CD14
    • Arditi M., Zhou J., Dorio R., Rong G. W., Goyert S. M., Kim K. S. Endotoxin-mediated endothelial cell injury and activation: Role of soluble CD14. Infect. Immun. 61:1993;3149-3156.
    • (1993) Infect. Immun. , vol.61 , pp. 3149-3156
    • Arditi, M.1    Zhou, J.2    Dorio, R.3    Rong, G.W.4    Goyert, S.M.5    Kim, K.S.6
  • 21
    • 0027249007 scopus 로고
    • Recombinant soluble CD14 mediates the activation of endothelial cells by lipopolysaccharide
    • Haziot A., Rong G. W., Silver J., Goyert S. M. Recombinant soluble CD14 mediates the activation of endothelial cells by lipopolysaccharide. J. Immunol. 151:1993;1500-1507.
    • (1993) J. Immunol. , vol.151 , pp. 1500-1507
    • Haziot, A.1    Rong, G.W.2    Silver, J.3    Goyert, S.M.4
  • 22
    • 0029164795 scopus 로고
    • Lipopolysaccharide stimulates the tyrosine phosphorylation of mitogen-activated protein kinases p44, p42, and p41 in vascular endothelial cells in a soluble CD14-dependent manner: Role of protein tyrosine phosphorylation in lipopolysaccharide-induced stimulation of endothelial cells
    • Arditi M., Zhou J., Torres M., Durden D. L., Stins M., Kim K. S. Lipopolysaccharide stimulates the tyrosine phosphorylation of mitogen-activated protein kinases p44, p42, and p41 in vascular endothelial cells in a soluble CD14-dependent manner: Role of protein tyrosine phosphorylation in lipopolysaccharide-induced stimulation of endothelial cells. J. Immunol. 155:1995;3994-4003.
    • (1995) J. Immunol. , vol.155 , pp. 3994-4003
    • Arditi, M.1    Zhou, J.2    Torres, M.3    Durden, D.L.4    Stins, M.5    Kim, K.S.6
  • 23
    • 0029881378 scopus 로고    scopus 로고
    • Lipopolysaccharide induces the rapid tyrosine phosphorylation of the mitogen-activated protein kinases erk-1 and p38 in cultured human vascular endothelial cells requiring the presence of soluble CD14
    • Schumann R. R., Pfeil D., Lamping N., Kirschning C., Scherzinger G., Schlag P., Karawajew L., Herrmann F. Lipopolysaccharide induces the rapid tyrosine phosphorylation of the mitogen-activated protein kinases erk-1 and p38 in cultured human vascular endothelial cells requiring the presence of soluble CD14. Blood. 87:1996;2805-2814.
    • (1996) Blood , vol.87 , pp. 2805-2814
    • Schumann, R.R.1    Pfeil, D.2    Lamping, N.3    Kirschning, C.4    Scherzinger, G.5    Schlag, P.6    Karawajew, L.7    Herrmann, F.8
  • 24
    • 0027961095 scopus 로고
    • Gene expression of monocyte chemoattractant protein-1 in human monocytes is regulated by cell density through protein tyrosine kinase and protein kinase C
    • Zen K., Masuda J., Sasaguri T., Kosaka C., Ogata J. Gene expression of monocyte chemoattractant protein-1 in human monocytes is regulated by cell density through protein tyrosine kinase and protein kinase C. Exp. Cell Res. 215:1994;172-179.
    • (1994) Exp. Cell Res. , vol.215 , pp. 172-179
    • Zen, K.1    Masuda, J.2    Sasaguri, T.3    Kosaka, C.4    Ogata, J.5
  • 27
    • 0026699666 scopus 로고
    • Transcriptional activation of the tumor necrosis factor α-inducible zinc finger protein, A20, is mediated by κb elements
    • Krikos A., Laherty C. D., Dixit V. M. Transcriptional activation of the tumor necrosis factor α-inducible zinc finger protein, A20, is mediated by κB elements. J. Biol. Chem. 267:1992;17971-17976.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17971-17976
    • Krikos, A.1    Laherty, C.D.2    Dixit, V.M.3
  • 29
    • 0028172554 scopus 로고
    • Murine inhibitory protein-κBα negatively regulates κb-dependent transcription in lipopolysaccharide-stimulated RAW 264.7 macrophages
    • Tebo J. M., Chaoqun W., Ohmori Y., Hamilton T. A. Murine inhibitory protein-κBα negatively regulates κB-dependent transcription in lipopolysaccharide-stimulated RAW 264.7 macrophages. J. Immunol. 153:1994;4713-4720.
    • (1994) J. Immunol. , vol.153 , pp. 4713-4720
    • Tebo, J.M.1    Chaoqun, W.2    Ohmori, Y.3    Hamilton, T.A.4
  • 30
    • 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. A sustained reduction in IκB-β may contribute to persistent NF-κB activation in human endothelial cells. J. Biol. Chem. 271:1996;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
  • 31
    • 17544374742 scopus 로고    scopus 로고
    • The role of the C-terminal domain of IκBα in protein degradation and stabilization
    • Beauparlant P., Lin R., Hiscott J. The role of the C-terminal domain of IκBα in protein degradation and stabilization. J. Biol. Chem. 271:1996;10690-10696.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10690-10696
    • Beauparlant, P.1    Lin, R.2    Hiscott, J.3
  • 32
    • 0028032360 scopus 로고
    • Hypoxic activation of nuclear factor-κB is mediated by a Ras and Raf signaling pathway and does not involve MAP kinase (ERK1 or ERK2)
    • Koong A. C., Chen E. Y., Mivechi N. F., Denko N. C., Stambrook P., Giaccia A. J. Hypoxic activation of nuclear factor-κB is mediated by a Ras and Raf signaling pathway and does not involve MAP kinase (ERK1 or ERK2). Cancer Res. 54:1994;5273-5279.
    • (1994) Cancer Res. , vol.54 , pp. 5273-5279
    • Koong, A.C.1    Chen, E.Y.2    Mivechi, N.F.3    Denko, N.C.4    Stambrook, P.5    Giaccia, A.J.6
  • 33
    • 0029890168 scopus 로고    scopus 로고
    • Endotoxin signal transduction in macrophages
    • Sweet M. J., Hume D. A. Endotoxin signal transduction in macrophages. J. Leukocyte Biol. 60:1996;8-26.
    • (1996) J. Leukocyte Biol. , vol.60 , pp. 8-26
    • Sweet, M.J.1    Hume, D.A.2
  • 34
    • 0029900009 scopus 로고    scopus 로고
    • Protein tyrosine kinase inhibitors act downstream of IL-1α and LPS stimulated MAP-kinase phosphorylation to inhibit expression of E-selectin on human umbilical vein endothelial cells
    • Adamson P., Tighe M., Pearson J. D. Protein tyrosine kinase inhibitors act downstream of IL-1α and LPS stimulated MAP-kinase phosphorylation to inhibit expression of E-selectin on human umbilical vein endothelial cells. Cell Adhes. Commun. 3:1996;511-525.
    • (1996) Cell Adhes. Commun. , vol.3 , pp. 511-525
    • Adamson, P.1    Tighe, M.2    Pearson, J.D.3
  • 35
    • 0028988138 scopus 로고
    • SB 203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin-1
    • Cuenda A., Rouse J., Doza Y. N., Meier R., Cohen P., Gallagher T. F., Young P. R., Lee J. C. SB 203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin-1. FEBS Lett. 364:1995;229-233.
    • (1995) FEBS Lett. , vol.364 , pp. 229-233
    • Cuenda, A.1    Rouse, J.2    Doza, Y.N.3    Meier, R.4    Cohen, P.5    Gallagher, T.F.6    Young, P.R.7    Lee, J.C.8
  • 38
    • 0029851622 scopus 로고    scopus 로고
    • IκBγ inhibits DNA binding of NF-κB p50 homodimers by interacting with residues that contact DNA
    • Bell S., Matthews J. R., Jaffray E., Hay R. T. IκBγ inhibits DNA binding of NF-κB p50 homodimers by interacting with residues that contact DNA. Mol. Cell Biol. 16:1996;6477-6485.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 6477-6485
    • Bell, S.1    Matthews, J.R.2    Jaffray, E.3    Hay, R.T.4
  • 39
    • 0028986194 scopus 로고
    • IκB-β regulates the persistent response in a biophasic activation of NF-κB
    • Thompson J. E., Phillips R. J., Erdjument B. H., Tempst P., Ghosh S. IκB-β regulates the persistent response in a biophasic activation of NF-κB. Cell. 80:1995;573-582.
    • (1995) Cell , vol.80 , pp. 573-582
    • Thompson, J.E.1    Phillips, R.J.2    Erdjument, B.H.3    Tempst, P.4    Ghosh, S.5
  • 40
    • 0028464391 scopus 로고
    • IL-1ra suppresses endotoxin-induced IL-1β and TNF-α release from mononuclear phagocytes
    • Marsh C. B., Moore S. A., Pope H. A., Wewers M. D. IL-1ra suppresses endotoxin-induced IL-1β and TNF-α release from mononuclear phagocytes. Am. J. Physiol. 267:1994;39-45.
    • (1994) Am. J. Physiol. , vol.267 , pp. 39-45
    • Marsh, C.B.1    Moore, S.A.2    Pope, H.A.3    Wewers, M.D.4
  • 41
    • 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., Mackman N. Proteasome inhibitors block VCAM-1 and ICAM-1 gene expression in endothelial cells without affecting nuclear translocation of nuclear factor-κB. Eur. J. Immunol. 26:1996;839-845.
    • (1996) Eur. J. Immunol. , vol.26 , pp. 839-845
    • Cobb, R.R.1    Felts, K.A.2    Parry, G.C.3    MacKman, N.4
  • 42
    • 0028092992 scopus 로고
    • CD14-mediated translocation of nuclear factor-κB induced by lipopolysaccharide does not require tyrosine kinase activity
    • Delude R. L., Fenton M. J., Savedra R. J., Perera P. Y., Vogel S. N., Thieringer R., Golenbock D. T. CD14-mediated translocation of nuclear factor-κB induced by lipopolysaccharide does not require tyrosine kinase activity. J. Biol. Chem. 269:1994;22253-22260.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22253-22260
    • Delude, R.L.1    Fenton, M.J.2    Savedra, R.J.3    Perera, P.Y.4    Vogel, S.N.5    Thieringer, R.6    Golenbock, D.T.7
  • 43
    • 0028884935 scopus 로고
    • Studies into the effect of the tyrosine kinase inhibitor herbimycin A on NF-κB activation in T lymphocytes: Evidence for covalent modification of the p50 subunit
    • Mahon T. M., O'Neill L. A. Studies into the effect of the tyrosine kinase inhibitor herbimycin A on NF-κB activation in T lymphocytes: Evidence for covalent modification of the p50 subunit. J. Biol. Chem. 270:1995;28557-28564.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28557-28564
    • Mahon, T.M.1    O'Neill, L.A.2
  • 44
    • 0029827580 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase (ERK1/2) activation by shear stress and adhesion in endothelial cells: Essential role for a herbimycin-sensitive kinase
    • Takahashi M., Berk B. C. Mitogen-activated protein kinase (ERK1/2) activation by shear stress and adhesion in endothelial cells: Essential role for a herbimycin-sensitive kinase. J. Clin. Invest. 98:1996;2623-2631.
    • (1996) J. Clin. Invest. , vol.98 , pp. 2623-2631
    • Takahashi, M.1    Berk, B.C.2
  • 45
    • 0030004897 scopus 로고    scopus 로고
    • Site-specific phosphorylation of IκBα by a novel ubiquitination-dependent protein kinase activity
    • Chen Z. J., Parent L., Maniatis T. Site-specific phosphorylation of IκBα by a novel ubiquitination-dependent protein kinase activity. Cell. 84:1996;853-862.
    • (1996) Cell , vol.84 , pp. 853-862
    • Chen, Z.J.1    Parent, L.2    Maniatis, T.3
  • 47
    • 0029666261 scopus 로고    scopus 로고
    • Characterization of IκB kinases. IκB-α is not phosphorylated by Raf-1 or protein kinase C isozymes, but is a casein kinase II substrate
    • Janosch P., Schellerer M., Seitz T., Reim P., Eulitz M., Brielmeier M., Kolch W., Sedivy J. M., Mischak H. Characterization of IκB kinases. IκB-α is not phosphorylated by Raf-1 or protein kinase C isozymes, but is a casein kinase II substrate. J. Biol. Chem. 271:1996;13868-13874.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13868-13874
    • Janosch, P.1    Schellerer, M.2    Seitz, T.3    Reim, P.4    Eulitz, M.5    Brielmeier, M.6    Kolch, W.7    Sedivy, J.M.8    Mischak, H.9
  • 48
    • 0029935860 scopus 로고    scopus 로고
    • Activation of multiple proline-directed kinases by bacterial lipopolysaccharide in murine macrophages
    • Sanghera J. S., Weinstein S. L., Aluwalia M., Girn J., Pelech S. L. Activation of multiple proline-directed kinases by bacterial lipopolysaccharide in murine macrophages. J. Immunol. 156:1996;4457-4465.
    • (1996) J. Immunol. , vol.156 , pp. 4457-4465
    • Sanghera, J.S.1    Weinstein, S.L.2    Aluwalia, M.3    Girn, J.4    Pelech, S.L.5
  • 49
    • 0029947996 scopus 로고    scopus 로고
    • MEK kinase is involved in tumor necrosis factor α-induced NF-κB activation and degradation of IκB-α
    • Hirano M., Osada S., Aoki T., Hirai S., Hosaka M., Inoue J., Ohno S. MEK kinase is involved in tumor necrosis factor α-induced NF-κB activation and degradation of IκB-α J. Biol. Chem. 271:1996;13234-13238.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13234-13238
    • Hirano, M.1    Osada, S.2    Aoki, T.3    Hirai, S.4    Hosaka, M.5    Inoue, J.6    Ohno, S.7
  • 50
    • 0029958946 scopus 로고    scopus 로고
    • Activation of c-Jun N-terminal kinase in bacterial lipopolysaccharide-stimulated macrophages
    • Hambleton J., Weinstein S. L., Lem L., DeFranco A. L. Activation of c-Jun N-terminal kinase in bacterial lipopolysaccharide-stimulated macrophages. Proc. Natl. Acad. Sci. USA. 93:1996;2774-2778.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2774-2778
    • Hambleton, J.1    Weinstein, S.L.2    Lem, L.3    Defranco, A.L.4
  • 51
    • 0030010965 scopus 로고    scopus 로고
    • Endothelial cell inflammatory responses to tumor necrosis factor-α: Ceramide-dependent and -independent mitogen-activated protein kinase cascades
    • Modur V., Zimmerman G. A., Prescott S. M., McIntyre T. M. Endothelial cell inflammatory responses to tumor necrosis factor-α: Ceramide-dependent and -independent mitogen-activated protein kinase cascades. J. Biol. Chem. 271:1996;13094-13102.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13094-13102
    • Modur, V.1    Zimmerman, G.A.2    Prescott, S.M.3    McIntyre, T.M.4
  • 52
    • 0028052255 scopus 로고
    • Anisomycin-activated protein kinases p45 and p55 but not mitogen-activated protein kinases ERK-1 and -2 are implicated in the induction of c-fos and c-jun
    • Cano E., Hazzalin C. A., Mahadevan L. C. Anisomycin-activated protein kinases p45 and p55 but not mitogen-activated protein kinases ERK-1 and -2 are implicated in the induction of c-fos and c-jun. Mol. Cell Biol. 14:1994;7352-7362.
    • (1994) Mol. Cell Biol. , vol.14 , pp. 7352-7362
    • Cano, E.1    Hazzalin, C.A.2    Mahadevan, L.C.3
  • 53
    • 0029664546 scopus 로고    scopus 로고
    • Molecular mechanisms of TNFα cytotoxicity: Activation of NF-κB and nuclear translocation
    • Claudio E., Segade F., Wrobel K., Ramos S., Bravo R., Lazo P. S. Molecular mechanisms of TNFα cytotoxicity: Activation of NF-κB and nuclear translocation. Exp. Cell Res. 224:1996;63-71.
    • (1996) Exp. Cell Res. , vol.224 , pp. 63-71
    • Claudio, E.1    Segade, F.2    Wrobel, K.3    Ramos, S.4    Bravo, R.5    Lazo, P.S.6
  • 54
    • 0031285250 scopus 로고    scopus 로고
    • Activation of the IκBα kinase complex by MEKK1, a kinase of the JNK pathway
    • Lee F. S., Hagler J., Chen Z. J., Maniatis T. Activation of the IκBα kinase complex by MEKK1, a kinase of the JNK pathway. Cell. 88:1997;213-222.
    • (1997) Cell , vol.88 , pp. 213-222
    • Lee, F.S.1    Hagler, J.2    Chen, Z.J.3    Maniatis, T.4
  • 55
    • 0029879315 scopus 로고    scopus 로고
    • Interaction between c-Rel and the mitogen-activated protein kinase kinase kinase 1 signaling cascade in mediating κb enhancer activation
    • Meyer C. F., Wang X., Chang C., Templeton D., Tan T. H. Interaction between c-Rel and the mitogen-activated protein kinase kinase kinase 1 signaling cascade in mediating κB enhancer activation. J. Biol. Chem. 271:1996;8971-8976.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8971-8976
    • Meyer, C.F.1    Wang, X.2    Chang, C.3    Templeton, D.4    Tan, T.H.5
  • 56
    • 0031017618 scopus 로고    scopus 로고
    • MAP3K-related kinase involved in NF-κB induction by TNF, CD95 and IL-1
    • Malinin N. L., Boldin M. P., Kovalenko A. V., Wallach D. MAP3K-related kinase involved in NF-κB induction by TNF, CD95 and IL-1. Nature. 385:1997;540-544.
    • (1997) Nature , vol.385 , pp. 540-544
    • Malinin, N.L.1    Boldin, M.P.2    Kovalenko, A.V.3    Wallach, D.4
  • 57
    • 0030610362 scopus 로고    scopus 로고
    • A cytokine-responsive IκB kinase that activates the transcription factor NF-κB
    • DiDonato J. A., Hayakawa M., Rothwarf D. M., Zandi E., Karin M. A cytokine-responsive IκB kinase that activates the transcription factor NF-κB. Nature. 388:1997;548-554.
    • (1997) Nature , vol.388 , pp. 548-554
    • Didonato, J.A.1    Hayakawa, M.2    Rothwarf, D.M.3    Zandi, E.4    Karin, M.5
  • 60
    • 0030070975 scopus 로고    scopus 로고
    • Bacterial lipopolysaccharide induces the association and coordinate activation of p53/56lyn and phosphatidylinositol 3-kinase in human monocytes
    • Herrera V. P., Reiner N. E. Bacterial lipopolysaccharide induces the association and coordinate activation of p53/56lyn and phosphatidylinositol 3-kinase in human monocytes. J. Immunol. 156:1996;1157-1165.
    • (1996) J. Immunol. , vol.156 , pp. 1157-1165
    • Herrera, V.P.1    Reiner, N.E.2
  • 61
    • 0027434028 scopus 로고
    • Lipopolysaccharide induces activation of CD14-associated protein tyrosine kinase p53/56lyn
    • Stefanova, Corcoran M. L., Horak E. M., Wahl L. M., Bolen J. B., Horak I. D. Lipopolysaccharide induces activation of CD14-associated protein tyrosine kinase p53/56lyn. J. Biol. Chem. 268:1993;20725-20728.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20725-20728
    • Stefanova1    Corcoran, M.L.2    Horak, E.M.3    Wahl, L.M.4    Bolen, J.B.5    Horak, I.D.6
  • 62
    • 0030912071 scopus 로고    scopus 로고
    • Lipopolysaccharide (LPS)-induced macrophage activation and signal transduction in the absence of Src-family kinases Hck, Fgr, and Lyn
    • Meng F., Lowell C. A. Lipopolysaccharide (LPS)-induced macrophage activation and signal transduction in the absence of Src-family kinases Hck, Fgr, and Lyn. J. Exp. Med. 185:1997;1661-1670.
    • (1997) J. Exp. Med. , vol.185 , pp. 1661-1670
    • Meng, F.1    Lowell, C.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.