메뉴 건너뛰기




Volumn 173, Issue 2, 2004, Pages 1313-1320

TNF-induced β2 integrin activation involves Src kinases and a redox-regulated activation of p38 MAPK

Author keywords

[No Author keywords available]

Indexed keywords

4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; ACETYLCYSTEINE; BETA2 INTEGRIN; CD11B ANTIGEN; COMPLEMENT COMPONENT C3B RECEPTOR; DIPHENYLIODONIUM SALT; EDETIC ACID; FLAVOPROTEIN; MITOGEN ACTIVATED PROTEIN KINASE P38; OXIDOREDUCTASE; PROTEIN TYROSINE KINASE; TUMOR NECROSIS FACTOR; CD18 ANTIGEN; MITOGEN ACTIVATED PROTEIN KINASE; TUMOR NECROSIS FACTOR ALPHA;

EID: 3142766828     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.173.2.1313     Document Type: Article
Times cited : (44)

References (54)
  • 1
    • 0025195758 scopus 로고
    • Leukocyte adhesion molecules deficiency: Its structural basis, pathophysiology and implications for modulating the inflammatory response
    • Arnaout, M. A. 1990. Leukocyte adhesion molecules deficiency: its structural basis, pathophysiology and implications for modulating the inflammatory response. Immunol. Rev. 114:145.
    • (1990) Immunol. Rev. , vol.114 , pp. 145
    • Arnaout, M.A.1
  • 2
    • 0030475975 scopus 로고    scopus 로고
    • Neutrophil activation by adhesion: Mechanisms and pathophysiological implications
    • Berton, G., S. R. Yan, L. Fumagalli, and C. A. Lowell. 1996. Neutrophil activation by adhesion: mechanisms and pathophysiological implications. Int. J. Clin. Lab. Res. 26:160.
    • (1996) Int. J. Clin. Lab. Res. , vol.26 , pp. 160
    • Berton, G.1    Yan, S.R.2    Fumagalli, L.3    Lowell, C.A.4
  • 4
    • 0033824065 scopus 로고    scopus 로고
    • Avidity regulation of integrins: The driving force in leukocyte adhesion
    • van Kooyk, Y., and C. G. Figdor. 2000. Avidity regulation of integrins: the driving force in leukocyte adhesion. Curr. Opin. Cell Biol. 12:542.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 542
    • Van Kooyk, Y.1    Figdor, C.G.2
  • 5
    • 0141756175 scopus 로고    scopus 로고
    • Integrin avidity regulation: Are changes in affinity and conformation underemphasized?
    • Carman, C. V., and T. A. Springer. 2003. Integrin avidity regulation: are changes in affinity and conformation underemphasized? Curr. Opin. Cell Biol. 15:547.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 547
    • Carman, C.V.1    Springer, T.A.2
  • 6
    • 0042739086 scopus 로고    scopus 로고
    • New insights into the structural basis of integrin activation
    • Xiong, J. P., T. Stehle, S. L. Goodman, and M. A. Arnaout. 2003. New insights into the structural basis of integrin activation. Blood 102:1155.
    • (2003) Blood , vol.102 , pp. 1155
    • Xiong, J.P.1    Stehle, T.2    Goodman, S.L.3    Arnaout, M.A.4
  • 8
    • 0037031906 scopus 로고    scopus 로고
    • Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling
    • Takagi, J., B. M. Petre, T. Walz, and T. A. Springer. 2002. Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling. Cell 110:599.
    • (2002) Cell , vol.110 , pp. 599
    • Takagi, J.1    Petre, B.M.2    Walz, T.3    Springer, T.A.4
  • 9
    • 0036696097 scopus 로고    scopus 로고
    • Integrin structure: New twists and turns in dynamic cell adhesion
    • Arnaout, M. A. 2002. Integrin structure: new twists and turns in dynamic cell adhesion. Immunol. Rev. 186:125.
    • (2002) Immunol. Rev. , vol.186 , pp. 125
    • Arnaout, M.A.1
  • 10
    • 0042681786 scopus 로고    scopus 로고
    • Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins
    • Kim, M., C. V. Carman, and T. A. Springer. 2003. Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins. Science 301:1720.
    • (2003) Science , vol.301 , pp. 1720
    • Kim, M.1    Carman, C.V.2    Springer, T.A.3
  • 12
    • 0024814732 scopus 로고
    • 2+ binding epitope on leukocyte integrin α subunits
    • 2+ binding epitope on leukocyte integrin α subunits. EMBO J. 8:3759.
    • (1989) EMBO J. , vol.8 , pp. 3759
    • Dransfield, I.1    Hogg, N.2
  • 13
    • 0035341132 scopus 로고    scopus 로고
    • Epitope mapping of antibodies to the C-terminal region of the integrin β2 subunit reveals regions that become exposed upon receptor activation
    • Lu, C., M. Ferzly, J. Takagi, and T. A. Springer. 2001. Epitope mapping of antibodies to the C-terminal region of the integrin β2 subunit reveals regions that become exposed upon receptor activation. J. Immunol. 166:5629.
    • (2001) J. Immunol. , vol.166 , pp. 5629
    • Lu, C.1    Ferzly, M.2    Takagi, J.3    Springer, T.A.4
  • 16
    • 0032529398 scopus 로고    scopus 로고
    • Role of stress-activated mitogen-activated protein kinase (p38) in β2-integrin-dependent neutrophil adhesion and the adhesion-dependent oxidative burst
    • Detmers, P. A., D. Zhou, E. Polizzi, R. Thieringer, W. A. Hanlon, S. Vaidya, and V. Bansal. 1998. Role of stress-activated mitogen-activated protein kinase (p38) in β2-integrin-dependent neutrophil adhesion and the adhesion-dependent oxidative burst. J. Immunol. 161:1921.
    • (1998) J. Immunol. , vol.161 , pp. 1921
    • Detmers, P.A.1    Zhou, D.2    Polizzi, E.3    Thieringer, R.4    Hanlon, W.A.5    Vaidya, S.6    Bansal, V.7
  • 17
    • 0033555864 scopus 로고    scopus 로고
    • Adhesion-dependent degranulation of neutrophils requires the Src family kinases Fgr and Hck
    • Mocsai, A., E. Ligeti, C. A. Lowell, and G. Berton. 1999. Adhesion-dependent degranulation of neutrophils requires the Src family kinases Fgr and Hck. J. Immunol. 162:1120.
    • (1999) J. Immunol. , vol.162 , pp. 1120
    • Mocsai, A.1    Ligeti, E.2    Lowell, C.A.3    Berton, G.4
  • 18
    • 0032519736 scopus 로고    scopus 로고
    • p38 mitogen-activated protein kinase activation is required for human neutrophil function triggered by TNF-α or fMLP stimulation
    • Zu, Y. L., J. Qi, A. Gilchrist, G. A. Fernandez, D. Vazquez-Abad, D. L. Kreutzer, C. K. Huang, and R. I. Sha'afi. 1998. p38 mitogen-activated protein kinase activation is required for human neutrophil function triggered by TNF-α or fMLP stimulation. J. Immunol. 160:1982.
    • (1998) J. Immunol. , vol.160 , pp. 1982
    • Zu, Y.L.1    Qi, J.2    Gilchrist, A.3    Fernandez, G.A.4    Vazquez-Abad, D.5    Kreutzer, D.L.6    Huang, C.K.7    Sha'afi, R.I.8
  • 20
    • 0032589682 scopus 로고    scopus 로고
    • Redox regulation of β2-integrin CD11b/CD18 activation
    • Blouin, E., L. Halbwachs-Mecarelli, and P. Rieu. 1999. Redox regulation of β2-integrin CD11b/CD18 activation. Eur. J. Immunol. 29:3419.
    • (1999) Eur. J. Immunol. , vol.29 , pp. 3419
    • Blouin, E.1    Halbwachs-Mecarelli, L.2    Rieu, P.3
  • 21
    • 0030803542 scopus 로고    scopus 로고
    • Leukosialin (CD43, sialophorin) redistribution in uropods of polarized neutrophils is induced by CD43 cross-linking by antibodies, by colchicine or by chemotactic peptides
    • Seveau, S., S. Lopez, P. Lesavre, J. Guichard, E. M. Cramer, and L. Halbwachs-Mecarelli. 1997. Leukosialin (CD43, sialophorin) redistribution in uropods of polarized neutrophils is induced by CD43 cross-linking by antibodies, by colchicine or by chemotactic peptides. J Cell Sci. 110:1465.
    • (1997) J. Cell Sci. , vol.110 , pp. 1465
    • Seveau, S.1    Lopez, S.2    Lesavre, P.3    Guichard, J.4    Cramer, E.M.5    Halbwachs-Mecarelli, L.6
  • 22
    • 0037146798 scopus 로고    scopus 로고
    • Immunoblotting and sequential lysis protocols for the analysis of tyrosine phosphorylation-dependent signaling
    • Gilbert, C., E. Rollet-Labelle, A. C. Caon, and P. H. Naccache. 2002. Immunoblotting and sequential lysis protocols for the analysis of tyrosine phosphorylation-dependent signaling. J. Immunol. Methods 271:185.
    • (2002) J. Immunol. Methods , vol.271 , pp. 185
    • Gilbert, C.1    Rollet-Labelle, E.2    Caon, A.C.3    Naccache, P.H.4
  • 23
    • 0034268796 scopus 로고    scopus 로고
    • Src tyrosine kinase is a novel direct effector of G proteins
    • Ma, Y. C., J. Huang, S. Ali, W. Lowry, and X. Y. Huang. 2000. Src tyrosine kinase is a novel direct effector of G proteins. Cell 102:635.
    • (2000) Cell , vol.102 , pp. 635
    • Ma, Y.C.1    Huang, J.2    Ali, S.3    Lowry, W.4    Huang, X.Y.5
  • 24
    • 0033755863 scopus 로고    scopus 로고
    • Src kinase-mediated signaling in leukocytes
    • Korade-Mimics, Z., and S. J. Corey. 2000. Src kinase-mediated signaling in leukocytes. J. Leukocyte Biol. 68:603.
    • (2000) J. Leukocyte Biol. , vol.68 , pp. 603
    • Korade-Mimics, Z.1    Corey, S.J.2
  • 25
    • 0031012781 scopus 로고    scopus 로고
    • Chemotactic peptide N-formyl-met-leu-phe activation of p38 mitogen-activated protein kinase (MAPK) and MAPK-activated protein kinase-2 in human neutrophils
    • Krump, E., J. S. Sanghera, S. L. Pelech, W. Furuya, and S. Grinstein. 1997. Chemotactic peptide N-formyl-met-leu-phe activation of p38 mitogen-activated protein kinase (MAPK) and MAPK-activated protein kinase-2 in human neutrophils. J. Biol. Chem. 272:937.
    • (1997) J. Biol. Chem. , vol.272 , pp. 937
    • Krump, E.1    Sanghera, J.S.2    Pelech, S.L.3    Furuya, W.4    Grinstein, S.5
  • 26
    • 0030026237 scopus 로고    scopus 로고
    • Activation of SRC family kinases in human neutrophils: Evidence that p58C-FGR and p53/56LYN redistributed to a Triton X-100-insoluble cytoskeletal fraction, also enriched in the caveolar protein caveolin, display an enhanced kinase activity
    • Yan, S. R., L. Fumagalli, and G. Berton, 1996. Activation of SRC family kinases in human neutrophils: evidence that p58C-FGR and p53/56LYN redistributed to a Triton X-100-insoluble cytoskeletal fraction, also enriched in the caveolar protein caveolin, display an enhanced kinase activity. FEBS Lett. 380:198.
    • (1996) FEBS Lett. , vol.380 , pp. 198
    • Yan, S.R.1    Fumagalli, L.2    Berton, G.3
  • 27
    • 0028167979 scopus 로고
    • β2 integrin-dependent protein tyrosine phosphorylation and activation of the FGR protein tyrosine kinase in human neutrophils
    • Berton, G., L. Fumagalli, C. Laudanna, and C. Sorio. 1994. β2 integrin-dependent protein tyrosine phosphorylation and activation of the FGR protein tyrosine kinase in human neutrophils. J. Cell Biol. 126:1111.
    • (1994) J. Cell Biol. , vol.126 , pp. 1111
    • Berton, G.1    Fumagalli, L.2    Laudanna, C.3    Sorio, C.4
  • 28
    • 0029414430 scopus 로고
    • Activation of p58c-fgr and p53/56lyn in adherent human neutrophils: Evidence for a role of divalent cations in regulating neutrophil adhesion and protein tyrosine kinase activities
    • Yan, S. R., L. Fumagalli, and G. Berton. 1995. Activation of p58c-fgr and p53/56lyn in adherent human neutrophils: evidence for a role of divalent cations in regulating neutrophil adhesion and protein tyrosine kinase activities. J. Inflamm. 45:297.
    • (1995) J. Inflamm. , vol.45 , pp. 297
    • Yan, S.R.1    Fumagalli, L.2    Berton, G.3
  • 29
    • 0027479814 scopus 로고
    • Studies on the inhibitory mechanism of iodonium compounds with special reference to neutrophil NADPH oxidase
    • O'Donnell, B. V., D. G. Tew, O. T. Jones, and P. J. England. 1993. Studies on the inhibitory mechanism of iodonium compounds with special reference to neutrophil NADPH oxidase. Biochem. J. 290:41.
    • (1993) Biochem. J. , vol.290 , pp. 41
    • O'Donnell, B.V.1    Tew, D.G.2    Jones, O.T.3    England, P.J.4
  • 30
    • 0030008394 scopus 로고    scopus 로고
    • Deficiency of Src family kinases p59/61hck and p58c-fgr results in defective adhesion-dependent neutrophil functions
    • Lowell, C. A., L. Fumagalli, and G. Berton. 1996. Deficiency of Src family kinases p59/61hck and p58c-fgr results in defective adhesion-dependent neutrophil functions. J. Cell Biol. 133:895.
    • (1996) J. Cell Biol. , vol.133 , pp. 895
    • Lowell, C.A.1    Fumagalli, L.2    Berton, G.3
  • 31
    • 0041344445 scopus 로고    scopus 로고
    • The Lyn tyrosine kinase negatively regulates neutrophil integrin signaling
    • Pereira, S., and C. Lowell. 2003. The Lyn tyrosine kinase negatively regulates neutrophil integrin signaling. J. Immunol. 171:1319,
    • (2003) J. Immunol. , vol.171 , pp. 1319
    • Pereira, S.1    Lowell, C.2
  • 32
    • 0037078334 scopus 로고    scopus 로고
    • An intracellular signaling hierarchy determines direction of migration in opposing chemotactic gradients
    • Heit, B., S. Tavener, E. Raharjo, and P. Kubes. 2002. An intracellular signaling hierarchy determines direction of migration in opposing chemotactic gradients. J. Cell Biol. 159:91.
    • (2002) J. Cell Biol. , vol.159 , pp. 91
    • Heit, B.1    Tavener, S.2    Raharjo, E.3    Kubes, P.4
  • 36
    • 0035576199 scopus 로고    scopus 로고
    • Role of p38 mitogen-activated protein kinase in chemokine-induced emigration and chemotaxis in vivo
    • Cara, D. C., J. Kaur, M. Forster, D. M. McCafferty, and P. Kubes. 2001. Role of p38 mitogen-activated protein kinase in chemokine-induced emigration and chemotaxis in vivo. J. Immunol. 167:6552.
    • (2001) J. Immunol. , vol.167 , pp. 6552
    • Cara, D.C.1    Kaur, J.2    Forster, M.3    McCafferty, D.M.4    Kubes, P.5
  • 38
    • 0030903025 scopus 로고    scopus 로고
    • Interleukin 8-stimulated phosphatidylinositol-3-kinase activity regulates the migration of human neutrophils independent of extracellular signal-regulated kinase and p38 mitogen-activated protein kinases
    • Knall, C., G. S. Worthen, and G. L. Johnson. 1997. Interleukin 8-stimulated phosphatidylinositol-3-kinase activity regulates the migration of human neutrophils independent of extracellular signal-regulated kinase and p38 mitogen-activated protein kinases. Proc. Natl. Acad. Sci. USA 94:3052.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3052
    • Knall, C.1    Worthen, G.S.2    Johnson, G.L.3
  • 39
    • 0036569440 scopus 로고    scopus 로고
    • Signaling pathways involved in IL-8-dependent activation of adhesion through Mac-1
    • Takami, M., V. Terry, and L. Petruzzelli. 2002. Signaling pathways involved in IL-8-dependent activation of adhesion through Mac-1. J. Immunol. 168:4559.
    • (2002) J. Immunol. , vol.168 , pp. 4559
    • Takami, M.1    Terry, V.2    Petruzzelli, L.3
  • 40
    • 0023484511 scopus 로고
    • Neutrophil activation on biological surfaces: Massive secretion of hydrogen peroxide in response to products of macrophages and lymphocytes
    • Nathan, C. F. 1987. Neutrophil activation on biological surfaces: massive secretion of hydrogen peroxide in response to products of macrophages and lymphocytes. J. Clin. Invest. 80:1550.
    • (1987) J. Clin. Invest. , vol.80 , pp. 1550
    • Nathan, C.F.1
  • 42
    • 0001376760 scopus 로고    scopus 로고
    • Regulation of Src family tyrosine kinase activities in adherent human neutrophils: Evidence that reactive oxygen intermediates produced by adherent neutrophils increase the activity of the p58c-fgr and p53/56lyn tyrosine kinases
    • Yan, S. R., and G. Berton. 1996. Regulation of Src family tyrosine kinase activities in adherent human neutrophils: evidence that reactive oxygen intermediates produced by adherent neutrophils increase the activity of the p58c-fgr and p53/56lyn tyrosine kinases. J. Biol. Chem. 271:23464.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23464
    • Yan, S.R.1    Berton, G.2
  • 43
    • 0025218905 scopus 로고
    • Flow cytometric analysis of respiratory burst activity in phagocytes with hydroethidine and 2′,7′-dichlorofluorescin
    • Rothe, G., and G. Valet. 1990. Flow cytometric analysis of respiratory burst activity in phagocytes with hydroethidine and 2′,7′- dichlorofluorescin. J. Leukocyte Biol. 47:440.
    • (1990) J. Leukocyte Biol. , vol.47 , pp. 440
    • Rothe, G.1    Valet, G.2
  • 44
    • 0031574105 scopus 로고    scopus 로고
    • Development of neutrophil granule diversity
    • Borregaard, N. 1997. Development of neutrophil granule diversity. Ann. NY Acad. Sci. 832:62.
    • (1997) Ann. NY Acad. Sci. , vol.832 , pp. 62
    • Borregaard, N.1
  • 45
    • 0025910044 scopus 로고
    • Neutrophil CR3 expression and specific granule exocytosis are controlled by different signal transduction pathways
    • Brown, G. E., E. B. Reed, and M. E. Lanser. 1991. Neutrophil CR3 expression and specific granule exocytosis are controlled by different signal transduction pathways. J. Immunol. 147:965.
    • (1991) J. Immunol. , vol.147 , pp. 965
    • Brown, G.E.1    Reed, E.B.2    Lanser, M.E.3
  • 46
    • 0022405825 scopus 로고
    • Calcium requirements for increased complement receptor expression during neutrophil activation
    • Berger, M., D. L. Birx, E. M. Wetzler, J. J. O'Shea, E. J. Brown, and A. S. Cross. 1985. Calcium requirements for increased complement receptor expression during neutrophil activation. J. Immunol. 135:1342.
    • (1985) J. Immunol. , vol.135 , pp. 1342
    • Berger, M.1    Birx, D.L.2    Wetzler, E.M.3    O'Shea, J.J.4    Brown, E.J.5    Cross, A.S.6
  • 47
    • 0034013301 scopus 로고    scopus 로고
    • Regulation by intracellular glutathione of TNF-α-induced p38 MAP kinase activation and RANTES production by human pulmonary vascular endothelial cells
    • Hashimoto, S., Y. Gon, K. Matsumoto, I. Takeshita, Y. Asai, T. Machino, and T. Horie. 2000. Regulation by intracellular glutathione of TNF-α-induced p38 MAP kinase activation and RANTES production by human pulmonary vascular endothelial cells. Allergy 55:463.
    • (2000) Allergy , vol.55 , pp. 463
    • Hashimoto, S.1    Gon, Y.2    Matsumoto, K.3    Takeshita, I.4    Asai, Y.5    Machino, T.6    Horie, T.7
  • 49
    • 0034326430 scopus 로고    scopus 로고
    • Sensing electrons: Protein phosphatase redox regulation
    • Rusnak, F., and T. Reiter. 2000. Sensing electrons: protein phosphatase redox regulation. Trends Biochem. Sci. 25:527.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 527
    • Rusnak, F.1    Reiter, T.2
  • 50
    • 0027510941 scopus 로고
    • Inactivation of a redox-sensitive protein phosphatase during the early events of tumor necrosis factor/ interleukin-1 signal transduction
    • Guy, G. R., J. Cairns, S. B. Ng, and Y. H. Tan. 1993. Inactivation of a redox-sensitive protein phosphatase during the early events of tumor necrosis factor/ interleukin-1 signal transduction. J. Biol. Chem. 268:2141.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2141
    • Guy, G.R.1    Cairns, J.2    Ng, S.B.3    Tan, Y.H.4
  • 51
    • 0032554611 scopus 로고    scopus 로고
    • Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: Evidence for a sulfenic acid intermediate and implications for redox regulation
    • Denu, J. M., and K. G. Tanner. 1998. Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation. Biochemistry 37:5633.
    • (1998) Biochemistry , vol.37 , pp. 5633
    • Denu, J.M.1    Tanner, K.G.2
  • 52
    • 0030772417 scopus 로고    scopus 로고
    • Spectroscopic and enzymatic characterization of the active site dinuclear metal center of calcineurin: Implications for a mechanistic role
    • Yu, L., J. Golbeck, J. Yao, and F. Rusnak. 1997. Spectroscopic and enzymatic characterization of the active site dinuclear metal center of calcineurin: implications for a mechanistic role. Biochemistry 36:10727.
    • (1997) Biochemistry , vol.36 , pp. 10727
    • Yu, L.1    Golbeck, J.2    Yao, J.3    Rusnak, F.4
  • 53
    • 0034062098 scopus 로고    scopus 로고
    • Inactivation of calcineurin by hydrogen peroxide and phenylarsine oxide: Evidence for a dithiol-disulfide equilibrium and implications for redox regulation
    • Bogumil, R., D. Namgaladze, D. Schaarschmidt, T. Schmachtel, S. Hellstern, R. Mutzel, and V. Ullrich. 2000. Inactivation of calcineurin by hydrogen peroxide and phenylarsine oxide: evidence for a dithiol-disulfide equilibrium and implications for redox regulation. Eur. J. Biochem. 267:1407.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1407
    • Bogumil, R.1    Namgaladze, D.2    Schaarschmidt, D.3    Schmachtel, T.4    Hellstern, S.5    Mutzel, R.6    Ullrich, V.7
  • 54
    • 0042195824 scopus 로고    scopus 로고
    • Talin forges the links between integrins and actin
    • Calderwood, D. A., and M. H. Ginsberg. 2003. Talin forges the links between integrins and actin. Nat. Cell Biol. 5:694.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 694
    • Calderwood, D.A.1    Ginsberg, M.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.