메뉴 건너뛰기




Volumn 158, Issue 4, 1997, Pages 1902-1910

Signaling by Adhesion in Human Neutrophils: Activation of the p72syk Tyrosine Kinase and Formation of Protein Complexes Containing p72syk and Src Family Kinases in Neutrophils Spreading over Fibrinogen

Author keywords

[No Author keywords available]

Indexed keywords

CD18 ANTIGEN; ENZYME PRECURSOR; FIBRINOGEN; MANGANESE; MULTIENZYME COMPLEX; OCTOXINOL; PROTEIN KINASE SYK; PROTEIN TYROSINE KINASE; SIGNAL PEPTIDE;

EID: 0031568669     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (122)

References (81)
  • 1
    • 0023484511 scopus 로고
    • PMN activation on biological surfaces: Massive secretion of hydrogen peroxide in response to products of macrophages and lymphocytes
    • Nathan, C. F. 1987. PMN 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
  • 2
    • 0024444326 scopus 로고
    • Cytokine-induced respiratory burst of human neutrophils: Dependence on extracellular matrix proteins and CD11/CD18 integrins
    • Nathan, C., S. Srimal, C. Farber, E. Sanchez, L. Kabbash, A. Asch, J. Gailit, and S. D. Wright. 1989. Cytokine-induced respiratory burst of human neutrophils: dependence on extracellular matrix proteins and CD11/CD18 integrins. J. Cell Biol. 109:1341.
    • (1989) J. Cell Biol. , vol.109 , pp. 1341
    • Nathan, C.1    Srimal, S.2    Farber, C.3    Sanchez, E.4    Kabbash, L.5    Asch, A.6    Gailit, J.7    Wright, S.D.8
  • 3
    • 0025013892 scopus 로고
    • Tumor necrosis factor and CD11/CD18(β2) integrins act synergistically to lower cAMP in human PMNs
    • Nathan, C. F., and E. Sanchez. 1990. Tumor necrosis factor and CD11/CD18(β2) integrins act synergistically to lower cAMP in human PMNs. J. Cell Biol. 111:2171.
    • (1990) J. Cell Biol. , vol.111 , pp. 2171
    • Nathan, C.F.1    Sanchez, E.2
  • 4
    • 0025219115 scopus 로고
    • Mac-1 (CD11b/CD18) mediates adherence-dependent hydrogen peroxide production by human and canine neutrophils
    • Shappel, S. B., C. Toman, D. C. Anderson, A. A. Taylor, M. L. Entman, and C. W. Smith. 1990. Mac-1 (CD11b/CD18) mediates adherence-dependent hydrogen peroxide production by human and canine neutrophils. J. Immunol. 144:2702.
    • (1990) J. Immunol. , vol.144 , pp. 2702
    • Shappel, S.B.1    Toman, C.2    Anderson, D.C.3    Taylor, A.A.4    Entman, M.L.5    Smith, C.W.6
  • 5
    • 0025101283 scopus 로고
    • --generating system of human neutrophils independently of the hydrolysis of phosphoinositides and the release of arachidonic acid
    • --generating system of human neutrophils independently of the hydrolysis of phosphoinositides and the release of arachidonic acid. Biochem. Biophys. Res. Commun. 166:308.
    • (1990) Biochem. Biophys. Res. Commun. , vol.166 , pp. 308
    • Laudanna, C.1    Miron, S.2    Berton, G.3    Rossi, F.4
  • 6
    • 0024996080 scopus 로고
    • 2+ and tumor necrosis factor-induced degranulation in adherent human neutrophils
    • 2+ and tumor necrosis factor-induced degranulation in adherent human neutrophils. J. Biol. Chem. 265:14358.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14358
    • Richter, J.1    Olsson, I.2    Andersson, T.3
  • 8
    • 0028028859 scopus 로고
    • 2 production in adherent human neutrophils
    • 2 production in adherent human neutrophils. J. Immunol. 152:290.
    • (1994) J. Immunol. , vol.152 , pp. 290
    • Suchard, J.1    Boxer, L.A.2
  • 9
    • 0030475975 scopus 로고    scopus 로고
    • Neutrophil activation by adhesion: Mechanisms and pathophysiological implications
    • Berton, G., S. R. Yan, F. 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, F.3    Lowell, C.A.4
  • 10
    • 0026542401 scopus 로고
    • Generation of signals activating PMN functions by leukocyte integrins: LFA-1 and gp150/95, but not CR3, are able to stimulate the respiratory burst of human PMNs
    • Berton, G., C. Laudanna, C. Sorio, and F. Rossi. 1992. Generation of signals activating PMN functions by leukocyte integrins: LFA-1 and gp150/95, but not CR3, are able to stimulate the respiratory burst of human PMNs. J. Cell Biol. 116:1007.
    • (1992) J. Cell Biol. , vol.116 , pp. 1007
    • Berton, G.1    Laudanna, C.2    Sorio, C.3    Rossi, F.4
  • 11
    • 0027218590 scopus 로고
    • Leukocyte response integrin and integrin-associated protein act as a signal transduction unit in generation of a phagocyte respiratory burst
    • Zhou, M., and E. J. Brown. 1993. Leukocyte response integrin and integrin-associated protein act as a signal transduction unit in generation of a phagocyte respiratory burst. J. Exp. Med. 178:1165.
    • (1993) J. Exp. Med. , vol.178 , pp. 1165
    • Zhou, M.1    Brown, E.J.2
  • 13
    • 0027455465 scopus 로고
    • Adhesion-dependent protein tyrosine phosphorylation in neutrophils treated with tumor necrosis factor
    • Fuortes, M., W. W. Jin, and C. Nathan. 1993. Adhesion-dependent protein tyrosine phosphorylation in neutrophils treated with tumor necrosis factor. J. Cell Biol. 120:777.
    • (1993) J. Cell Biol. , vol.120 , pp. 777
    • Fuortes, M.1    Jin, W.W.2    Nathan, C.3
  • 14
    • 0028167979 scopus 로고
    • 2 integrin-dependent protein tyrosine phosphorylation and activation of the FCR protein tyrosine kinase in human neutrophils
    • 2 integrin-dependent protein tyrosine phosphorylation and activation of the FCR protein tyrosine kinase in human neutrophils. J. Cell Biol. 126:1111.
    • (1994) J. Cell Biol. , vol.126 , pp. 1111
    • Berton, G.1    Fumagalli, F.2    Laudanna, C.3    Sorio, C.4
  • 15
    • 0028097582 scopus 로고
    • 2, CD11b/CD18) is required for tyrosine phosphorylation of paxillin in adherent and nonadherent neutrophils
    • 2, CD11b/CD18) is required for tyrosine phosphorylation of paxillin in adherent and nonadherent neutrophils. J. Cell Biol. 127:1139.
    • (1994) J. Cell Biol. , vol.127 , pp. 1139
    • Graham, I.L.1    Anderson, D.C.2    Holers, V.M.3    Brown, E.J.4
  • 16
    • 0028170990 scopus 로고
    • β2 integrin-dependent tyrosine phosphorylation of paxillin in human neutrophils treated with tumor necrosis factor
    • Fuortes, M., W. W. Jin, and C. F. Nathan. 1994. β2 integrin-dependent tyrosine phosphorylation of paxillin in human neutrophils treated with tumor necrosis factor. J. Cell Biol. 127:1477.
    • (1994) J. Cell Biol. , vol.127 , pp. 1477
    • Fuortes, M.1    Jin, W.W.2    Nathan, C.F.3
  • 17
    • 0028989085 scopus 로고
    • TNF-α induces tyrosine phosphorylation of mitogen-activated protein kinase in adherent human neutrophils
    • Rafiee, P., J. K. Lee, C. C. Leung, and T. A. Raffin. 1995. TNF-α induces tyrosine phosphorylation of mitogen-activated protein kinase in adherent human neutrophils. J. Immunol. 154:4785.
    • (1995) J. Immunol. , vol.154 , pp. 4785
    • Rafiee, P.1    Lee, J.K.2    Leung, C.C.3    Raffin, T.A.4
  • 18
    • 0027267607 scopus 로고
    • - generation in response to tumor necrosis factor-α, and antibodies against CD18 and CD11a: Evidence for a common and unique pattern of sensitivity to wortmannin and protein tyrosine kinase inhibitors. Biochem
    • - generation in response to tumor necrosis factor-α, and antibodies against CD18 and CD11a: evidence for a common and unique pattern of sensitivity to wortmannin and protein tyrosine kinase inhibitors. Biochem. Biophys. Res. Commun. 190:935.
    • (1993) Biophys. Res. Commun. , vol.190 , pp. 935
    • Laudanna, C.1    Rossi, F.2    Berton, G.3
  • 19
    • 0029414430 scopus 로고
    • lyn in adherent human neutrophils: Evidence for a role of divalent cations in regulating neutrophil adhesion and protein tyrosine kinase activities
    • lyn 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
  • 20
    • 0030008394 scopus 로고    scopus 로고
    • c-fgr results in defective adhesion-dependent neutrophil functions
    • c-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
  • 22
    • 0024437414 scopus 로고
    • A function for the lck protooncogene
    • Bolen, J. B., and A. Veillette. 1989. A function for the lck protooncogene. Trends Biol. Sci. 14:404.
    • (1989) Trends Biol. Sci. , vol.14 , pp. 404
    • Bolen, J.B.1    Veillette, A.2
  • 24
    • 0025971630 scopus 로고
    • T cell antigen receptor activation pathways: The tyrosine kinase connection
    • Klausner, R. D., and L. E. Samelson. 1991. T cell antigen receptor activation pathways: the tyrosine kinase connection. Cell 64:875.
    • (1991) Cell , vol.64 , pp. 875
    • Klausner, R.D.1    Samelson, L.E.2
  • 25
    • 0026244947 scopus 로고
    • Protein tyrosine phosphorylation and the adhesive functions of platelets
    • Shattil, S. J., and J. S. Brugge. 1991. Protein tyrosine phosphorylation and the adhesive functions of platelets. Curr. Opin. Cell Biol. 3:869.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 869
    • Shattil, S.J.1    Brugge, J.S.2
  • 26
    • 0025966241 scopus 로고
    • T-cell development and transmembrane signaling: Changing biological responses through an unchanging receptor
    • Finkel, T. H., R. T. Kubo, and J. C. Cambier. 1991. T-cell development and transmembrane signaling: changing biological responses through an unchanging receptor. Immunol. Today 12:79.
    • (1991) Immunol. Today , vol.12 , pp. 79
    • Finkel, T.H.1    Kubo, R.T.2    Cambier, J.C.3
  • 27
    • 0026681679 scopus 로고
    • The T cell receptor as a multicomponent signalling machine: CD4/CD8 coreceptors and CD45 in T cell activation
    • Janeway, C. A., Jr. 1992. The T cell receptor as a multicomponent signalling machine: CD4/CD8 coreceptors and CD45 in T cell activation. Annu. Rev. Immunol. 10:645.
    • (1992) Annu. Rev. Immunol. , vol.10 , pp. 645
    • Janeway Jr., C.A.1
  • 28
    • 0029040199 scopus 로고
    • Protein tyrosine kinases in the initiation of antigen receptor signaling
    • Bolen, J. B. 1995. Protein tyrosine kinases in the initiation of antigen receptor signaling. Curr. Opin. Cell Biol. 7:306.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 306
    • Bolen, J.B.1
  • 29
    • 0029082078 scopus 로고
    • Antigen and Fc receptor signaling: The awesome power of the immunoreceptor tyrosine-based activation motif (ITAM)
    • Cambier, J. C. 1995. Antigen and Fc receptor signaling: the awesome power of the immunoreceptor tyrosine-based activation motif (ITAM). J. Immunol. 155:3281.
    • (1995) J. Immunol. , vol.155 , pp. 3281
    • Cambier, J.C.1
  • 31
    • 0028783322 scopus 로고
    • Syk tyrosine kinase required for mouse viability and B-cell development
    • Cheng, A. M., B. Rowley, W. Pao, A. Hayday, J. B. Bolen, and T. Pawson. 1995. Syk tyrosine kinase required for mouse viability and B-cell development. Nature 378:303.
    • (1995) Nature , vol.378 , pp. 303
    • Cheng, A.M.1    Rowley, B.2    Pao, W.3    Hayday, A.4    Bolen, J.B.5    Pawson, T.6
  • 32
    • 0027433055 scopus 로고
    • syk in high affinity IgE receptor signaling: Identification as a component of pp72 and association with the receptor γ chain after receptor aggregation
    • syk in high affinity IgE receptor signaling: identification as a component of pp72 and association with the receptor γ chain after receptor aggregation. J. Biol. Chem. 268:23318.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23318
    • Benhamou, M.1    Ryba, N.J.P.2    Kihara, H.3    Nishikata, H.4    Siraganian, R.P.5
  • 33
    • 0027998862 scopus 로고
    • Differential control of the tyrosine kinase Lyn and Syk by the two signaling chains of the high affinity immunoglobulin e receptor
    • Jouvin, M. H. E., M. Adamczewski, R. Numerof, O. Letourneur, A. Vallé, and J. P. Kinet. 1994. Differential control of the tyrosine kinase Lyn and Syk by the two signaling chains of the high affinity immunoglobulin E receptor. J. Biol. Chem. 269:5918.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5918
    • Jouvin, M.H.E.1    Adamczewski, M.2    Numerof, R.3    Letourneur, O.4    Vallé, A.5    Kinet, J.P.6
  • 35
    • 0027998631 scopus 로고
    • Src homology 2 domains of Syk and Lyn bind to tyrosine-phosphorylated subunits of the high affinity IgE receptor
    • Kihara, H., and R. P. Siraganian. 1994. Src homology 2 domains of Syk and Lyn bind to tyrosine-phosphorylated subunits of the high affinity IgE receptor. J. Biol. Chem. 269:22427.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22427
    • Kihara, H.1    Siraganian, R.P.2
  • 36
    • 0028985471 scopus 로고
    • Distinct functions of the Fc∈RI γ and β subunits in the control of Fc∈RI-mediated tyrosine kinase activation and signaling responses in RBL-2H3 mast cells
    • Wilson, B. S., N. Kapp, R. J. Lee, J. R. Pfeifer, A. M. Martinez, Y. Platt, F. Letourner, and J. M. Oliver. 1995. Distinct functions of the Fc∈RI γ and β subunits in the control of Fc∈RI-mediated tyrosine kinase activation and signaling responses in RBL-2H3 mast cells. J. Biol. Chem. 270:4013.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4013
    • Wilson, B.S.1    Kapp, N.2    Lee, R.J.3    Pfeifer, J.R.4    Martinez, A.M.5    Platt, Y.6    Letourner, F.7    Oliver, J.M.8
  • 37
    • 0028800756 scopus 로고
    • Clustering of Syk is sufficient to induce tyrosine phosphorylation and release of allergic mediators from rat basophilic leukemia cells
    • Rivera, V. M., and J. S. Brugge. 1995. Clustering of Syk is sufficient to induce tyrosine phosphorylation and release of allergic mediators from rat basophilic leukemia cells. Mol. Cell Biol. 15:1582.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 1582
    • Rivera, V.M.1    Brugge, J.S.2
  • 38
    • 0028072499 scopus 로고
    • Inhibition of mast cell Fc∈RI-mediated signaling and effector function by the Syk-selective inhibitor, piceatannol
    • Oliver, J. M., D. L. Burg, B. S. Wilson, J. L. McLaughlin, and R. L. Geahlen 1994. Inhibition of mast cell Fc∈RI-mediated signaling and effector function by the Syk-selective inhibitor, piceatannol. J. Biol. Chem. 269:29697.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29697
    • Oliver, J.M.1    Burg, D.L.2    Wilson, B.S.3    McLaughlin, J.L.4    Geahlen, R.L.5
  • 39
    • 0028916595 scopus 로고
    • A requirement for Syk in the activation of the microtubule-associated protein kinase/phospholipase A2 pathway by Fc epsilon RI is not shared by a G protein-coupled receptor
    • Hirasawa, N., A. Scharenberg, H. Yamamura, M. A. Beaven, and J. P. Kinet. 1995. A requirement for Syk in the activation of the microtubule-associated protein kinase/phospholipase A2 pathway by Fc epsilon RI is not shared by a G protein-coupled receptor. J. Biol. Chem. 270:10960.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10960
    • Hirasawa, N.1    Scharenberg, A.2    Yamamura, H.3    Beaven, M.A.4    Kinet, J.P.5
  • 40
    • 0028905060 scopus 로고
    • Syk is activated by phosphotyrosine-containing peptides representing the tyrosine-based motifs of the high affinity receptor for IgE
    • Shiue, L., M. J. Zoller, and J. S. Brugge. 1995. Syk is activated by phosphotyrosine-containing peptides representing the tyrosine-based motifs of the high affinity receptor for IgE. J. Biol. Chem. 270:10498.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10498
    • Shiue, L.1    Zoller, M.J.2    Brugge, J.S.3
  • 41
    • 0029045870 scopus 로고
    • Reconstitution of interactions between tyrosine kinases and the high affinity IgE receptor which are controlled by receptor clustering
    • Scharenberg, A. M., S. Lin, B. Cuenod, H. Yamamura, and J. P. Kinet. 1995. Reconstitution of interactions between tyrosine kinases and the high affinity IgE receptor which are controlled by receptor clustering. EMBO J. 14:3385.
    • (1995) EMBO J. , vol.14 , pp. 3385
    • Scharenberg, A.M.1    Lin, S.2    Cuenod, B.3    Yamamura, H.4    Kinet, J.P.5
  • 42
    • 0029058030 scopus 로고
    • Activation of high affinity immunoglobulin e receptor Fc epsilon RI in RBL-2H3 cells is inhibited by Syk SH2 domains
    • Taylor, J. A., J. L. Karas, M. K. Ram, O. M. Green, and C. Seidel-Dugan. 1995. Activation of high affinity immunoglobulin E receptor Fc epsilon RI in RBL-2H3 cells is inhibited by Syk SH2 domains. Mol. Cell. Biol. 15:4149.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4149
    • Taylor, J.A.1    Karas, J.L.2    Ram, M.K.3    Green, O.M.4    Seidel-Dugan, C.5
  • 43
    • 0027420792 scopus 로고
    • Cross-linking of Fcγ receptor I (FcγRI) and receptor II (FcγRII) on monocytic cells activates a signal transduction pathway common to both Fc receptors that involves the stimulation of p72 Syk protein tyrosine kinase
    • Kiener, P. A., B. M. Rankin, A. L. Burkhardt, G. L. Schieven, L. K. Gilliland, R. B. Rowley, J. B. Bolen, and J. A. Ledbetter. 1993. Cross-linking of Fcγ receptor I (FcγRI) and receptor II (FcγRII) on monocytic cells activates a signal transduction pathway common to both Fc receptors that involves the stimulation of p72 Syk protein tyrosine kinase. J. Biol. Chem. 268:24442.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24442
    • Kiener, P.A.1    Rankin, B.M.2    Burkhardt, A.L.3    Schieven, G.L.4    Gilliland, L.K.5    Rowley, R.B.6    Bolen, J.B.7    Ledbetter, J.A.8
  • 44
    • 0027338195 scopus 로고
    • syk, a protein tyrosine kinase, in Fc gamma receptor signaling
    • syk, a protein tyrosine kinase, in Fc gamma receptor signaling. J. Biol. Chem. 268:15900.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15900
    • Agarwal, A.1    Salem, P.2    Robbins, K.C.3
  • 45
  • 46
    • 0028179898 scopus 로고
    • Stimulation of macrophage FcγRIIIA activates the receptor-associated protein tyrosine kinase Syk and induces phosphorylation of multiple proteins including p95Vav and p62/GAP-associated protein
    • Darby, C., R. L. Geahlen, and A. D. Schreiber. 1994. Stimulation of macrophage FcγRIIIA activates the receptor-associated protein tyrosine kinase Syk and induces phosphorylation of multiple proteins including p95Vav and p62/GAP-associated protein. J. Immunol. 152:5429.
    • (1994) J. Immunol. , vol.152 , pp. 5429
    • Darby, C.1    Geahlen, R.L.2    Schreiber, A.D.3
  • 47
    • 0028519195 scopus 로고
    • syk in FcγRI receptor signaling
    • syk in FcγRI receptor signaling. Blood 84:2102.
    • (1994) Blood , vol.84 , pp. 2102
    • Durden, D.L.1    Liu, Y.B.2
  • 49
    • 0028890716 scopus 로고
    • Tyrosine phosphorylation and association of Syk with Fc gamma RII in monocytic THP-1 cells
    • Ghazizadeh, S., J. B. Bolen, and H. B. Fleit. 1995. Tyrosine phosphorylation and association of Syk with Fc gamma RII in monocytic THP-1 cells. Biochem. J. 305:669.
    • (1995) Biochem. J. , vol.305 , pp. 669
    • Ghazizadeh, S.1    Bolen, J.B.2    Fleit, H.B.3
  • 50
    • 0028926008 scopus 로고
    • Induction of phagocytosis by a protein tyrosine kinase
    • Indik, Z. K., J. G. Park, X. Q. Pan, and A. D. Schreiber. 1995. Induction of phagocytosis by a protein tyrosine kinase. Blood 85:1175.
    • (1995) Blood , vol.85 , pp. 1175
    • Indik, Z.K.1    Park, J.G.2    Pan, X.Q.3    Schreiber, A.D.4
  • 51
    • 0029057410 scopus 로고
    • Interaction between Lck and Syk family kinases in Fc gamma receptor-initiated activation of natural killer cells
    • Ting, A. T., C. J. Dick, R. A. Schoon, L. M. Karnitz, R. T. Abraham, and P. J. Leibson. 1995. Interaction between Lck and Syk family kinases in Fc gamma receptor-initiated activation of natural killer cells. J. Biol. Chem. 270:16415.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16415
    • Ting, A.T.1    Dick, C.J.2    Schoon, R.A.3    Karnitz, L.M.4    Abraham, R.T.5    Leibson, P.J.6
  • 52
    • 0029114537 scopus 로고
    • Determinants of the phagocytic signal mediated by the type IIIA Fc gamma receptor, Fc gamma RIIIA: Sequence requirements and interaction with protein-tyrosine kinases
    • Park, J. G., and A. D. Schreiber. 1995. Determinants of the phagocytic signal mediated by the type IIIA Fc gamma receptor, Fc gamma RIIIA: sequence requirements and interaction with protein-tyrosine kinases. Proc. Natl. Acad. Sci. USA 92:7381.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7381
    • Park, J.G.1    Schreiber, A.D.2
  • 54
    • 0028364455 scopus 로고
    • Granulocyte colony-stimulating factor receptor signaling involves the formation of a three-component complex with Lyn and Syk protein-tyrosine kinases
    • Corey, S. J., A. L. Burkhardt, J. B. Bolen, R. L. Geahlen, L. S. Tkatch, and D. J. Tweardy. 1994. Granulocyte colony-stimulating factor receptor signaling involves the formation of a three-component complex with Lyn and Syk protein-tyrosine kinases. Proc. Natl. Acad. Sci. USA 91:4683.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4683
    • Corey, S.J.1    Burkhardt, A.L.2    Bolen, J.B.3    Geahlen, R.L.4    Tkatch, L.S.5    Tweardy, D.J.6
  • 55
    • 0028988329 scopus 로고
    • Protein tyrosine kinase Syk is associated with and activated by the IL-2 receptor: Possible link with the c-myc induction pathway
    • Minami, Y., Y. Nakagawa, A. Kawashara, T. Miyazaki, K. Sada, H. Yamamura, and T. Taniguchi. 1995. Protein tyrosine kinase Syk is associated with and activated by the IL-2 receptor: possible link with the c-myc induction pathway. Immunity 2:89.
    • (1995) Immunity , vol.2 , pp. 89
    • Minami, Y.1    Nakagawa, Y.2    Kawashara, A.3    Miyazaki, T.4    Sada, K.5    Yamamura, H.6    Taniguchi, T.7
  • 58
    • 0029005762 scopus 로고
    • Integrin-mediated tyrosine phosphorylation and cytokine message induction in monocytic cells: A possible signaling role for the Syk tyrosine kinase
    • Lin, T. H., C. Rosales, K. Mondal, J. B. Bolen, S. Haskill, and R. L. Juliano. 1995. Integrin-mediated tyrosine phosphorylation and cytokine message induction in monocytic cells: a possible signaling role for the Syk tyrosine kinase. J. Biol. Chem. 270:16189.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16189
    • Lin, T.H.1    Rosales, C.2    Mondal, K.3    Bolen, J.B.4    Haskill, S.5    Juliano, R.L.6
  • 60
    • 0026040946 scopus 로고
    • Occupancy of CD11b/CD18 (Mac-1) divalent ion binding sites induces leukocyte adhesion
    • Altieri, D. C. 1991. Occupancy of CD11b/CD18 (Mac-1) divalent ion binding sites induces leukocyte adhesion. J. Immunol. 147:1891.
    • (1991) J. Immunol. , vol.147 , pp. 1891
    • Altieri, D.C.1
  • 61
    • 0026717205 scopus 로고
    • Effect of divalent cations on adhesion of polymorphonuclear leukocytes to matrix molecules in vitro
    • Lundgren-Åkerlund, E., E. Berger, and K. E. Afors. 1992. Effect of divalent cations on adhesion of polymorphonuclear leukocytes to matrix molecules in vitro. J. Leukocvte Biol. 51:603.
    • (1992) J. Leukocvte Biol. , vol.51 , pp. 603
    • Lundgren-Åkerlund, E.1    Berger, E.2    Afors, K.E.3
  • 62
    • 0026601096 scopus 로고
    • Divalent cation regulation of the function of the leukocyte integrin LFA-1
    • Dransfield, I., C. Cabañas, A. Craig, and N. Hogg. 1992. Divalent cation regulation of the function of the leukocyte integrin LFA-1. J. Cell Biol. 116:219.
    • (1992) J. Cell Biol. , vol.116 , pp. 219
    • Dransfield, I.1    Cabañas, C.2    Craig, A.3    Hogg, N.4
  • 64
    • 0027170920 scopus 로고
    • SH3 domains direct cellular localization of signaling molecules
    • Bar-Sagi, D., D. Rotin, A. Batzer, V. Mandiyan, and J. Schlessinger. 1993. SH3 domains direct cellular localization of signaling molecules. Cell 74:83.
    • (1993) Cell , vol.74 , pp. 83
    • Bar-Sagi, D.1    Rotin, D.2    Batzer, A.3    Mandiyan, V.4    Schlessinger, J.5
  • 67
    • 0028901016 scopus 로고
    • Identification of the major tyrosine kinase substrate in signaling complexes formed after engagement of Fcγ receptors
    • Marcilla, A., O. M. Rivero-Lezcano, A. Agarwal, and K. C. Robbins. 1995. Identification of the major tyrosine kinase substrate in signaling complexes formed after engagement of Fcγ receptors. J. Biol. Chem. 270:9115.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9115
    • Marcilla, A.1    Rivero-Lezcano, O.M.2    Agarwal, A.3    Robbins, K.C.4
  • 70
    • 0026497661 scopus 로고
    • Cytoskeleton-plasma membrane interactions
    • Luna, E. J., and A. L. Hitt. 1992. Cytoskeleton-plasma membrane interactions. Science 258:955.
    • (1992) Science , vol.258 , pp. 955
    • Luna, E.J.1    Hitt, A.L.2
  • 71
    • 0028978448 scopus 로고
    • 2+- And calcineurin-dependent recycling of an integrin to the front of migrating neutrophils
    • 2+-and calcineurin-dependent recycling of an integrin to the front of migrating neutrophils. Nature 377:75.
    • (1995) Nature , vol.377 , pp. 75
    • Lawson, M.A.1    Maxfield, F.R.2
  • 72
    • 0024595405 scopus 로고
    • Respiratory burst in adherent human neutrophils: Triggering by colony-stimulating factors CSF-GM and CSF-G
    • Nathan, C. F. 1989. Respiratory burst in adherent human neutrophils: triggering by colony-stimulating factors CSF-GM and CSF-G. Blood 73:301.
    • (1989) Blood , vol.73 , pp. 301
    • Nathan, C.F.1
  • 73
    • 0028446566 scopus 로고
    • The dynamic regulation of integrin adhesiveness
    • Diamond, M. S., and T. A. Springer. 1994. The dynamic regulation of integrin adhesiveness. Curr. Biol. 4:506.
    • (1994) Curr. Biol. , vol.4 , pp. 506
    • Diamond, M.S.1    Springer, T.A.2
  • 74
    • 0028977990 scopus 로고
    • syk with the src homology-2 (SH2) domains of PLCγ1 in B lymphocytes
    • syk with the src homology-2 (SH2) domains of PLCγ1 in B lymphocytes. J. Biol. Chem. 270:11806.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11806
    • Sillman, A.L.1    Monroe, J.G.2
  • 75
    • 0028984269 scopus 로고
    • Regulation of Zap-70 by Src family tyrosine protein kinases in an antigen-specific T-cell line
    • Weil, R., J. F. Cloutier, M. Fournel, and A. Veillette. 1995. Regulation of Zap-70 by Src family tyrosine protein kinases in an antigen-specific T-cell line. J. Biol. Chem. 270:2791.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2791
    • Weil, R.1    Cloutier, J.F.2    Fournel, M.3    Veillette, A.4
  • 76
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark, E. A., and J. S. Brugge. 1995. Integrins and signal transduction pathways: the road taken. Science 268:233.
    • (1995) Science , vol.268 , pp. 233
    • Clark, E.A.1    Brugge, J.S.2
  • 77
    • 0029164237 scopus 로고
    • Integrin transmembrane signaling and cytoskeletal control
    • Yamada, K. M., and S. Miyamoto. 1995. Integrin transmembrane signaling and cytoskeletal control. Curr. Opin. Cell Biol. 7:681.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 681
    • Yamada, K.M.1    Miyamoto, S.2
  • 78
    • 0029965695 scopus 로고    scopus 로고
    • Integrin-mediated signalling: Regulation by protein tyrosine kinases and small GTP-binding proteins
    • Parsons, J. T. 1996. Integrin-mediated signalling: regulation by protein tyrosine kinases and small GTP-binding proteins. Curr. Opin. Cell Biol. 8:146.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 146
    • Parsons, J.T.1
  • 79
    • 0029045815 scopus 로고
    • Specific and redundant roles of Src and Fyn in organizing the cytoskeleton
    • Thomas, S. M., P. Soriano, and A. Imamoto. 1995. Specific and redundant roles of Src and Fyn in organizing the cytoskeleton. Nature 376:267.
    • (1995) Nature , vol.376 , pp. 267
    • Thomas, S.M.1    Soriano, P.2    Imamoto, A.3
  • 80
    • 0029034939 scopus 로고
    • Src enhances the spreading of src -/- Fibroblasts on fibronectin by a kinase-independent mechanism
    • Kaplan, K. B., J. R. Swedlow, D. O. Morgan, and H. E. Varmus. 1995. c-Src enhances the spreading of src -/-fibroblasts on fibronectin by a kinase-independent mechanism. Genes Dev. 9:1505.
    • (1995) Genes Dev. , vol.9 , pp. 1505
    • Kaplan, K.B.1    Swedlow, J.R.2    Morgan, D.O.3    Varmus, H.E.4
  • 81
    • 0026023289 scopus 로고
    • Targeted disruption of the c-src proto-oncogene leads to osteopetrosis in mice
    • Soriano, P., C. Montgomery, R. Geske and A. Bradley. 1991. Targeted disruption of the c-src proto-oncogene leads to osteopetrosis in mice. Cell 64:693.
    • (1991) Cell , vol.64 , pp. 693
    • Soriano, P.1    Montgomery, C.2    Geske, R.3    Bradley, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.