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Volumn 186, Issue 11, 2011, Pages 6485-6496

Priming of eosinophils by GM-CSF is mediated by protein kinase CbII-phosphorylated L-plastin

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN BINDING PROTEIN; ALPHAMBETA2 INTEGRIN; COFILIN; EOSINOPHIL CATIONIC PROTEIN; EOSINOPHIL PEROXIDASE; EOTAXIN; GLYCOPROTEIN; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR RECEPTOR; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR RECEPTOR ALPHA CHAIN; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR RECEPTOR BETA CHAIN; L PLASTIN; PAXILLIN; PROTEIN KINASE C BETA; PROTEIN KINASE C BETA2; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 79958031003     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1001868     Document Type: Article
Times cited : (41)

References (67)
  • 1
    • 0026443197 scopus 로고
    • T cells and eosinophils in the pathogenesis of asthma
    • Corrigan, C. J., and A. B. Kay. 1992. T cells and eosinophils in the pathogenesis of asthma. Immunol. Today 13: 501-507.
    • (1992) Immunol. Today , vol.13 , pp. 501-507
    • Corrigan, C.J.1    Kay, A.B.2
  • 2
    • 0002543851 scopus 로고
    • The pathology of asthma, with special reference to changes in the bronchial mucosa
    • Dunnill, M. S. 1960. The pathology of asthma, with special reference to changes in the bronchial mucosa. J. Clin. Pathol. 13: 27-33.
    • (1960) J. Clin. Pathol. , vol.13 , pp. 27-33
    • Dunnill, M.S.1
  • 6
    • 0035104951 scopus 로고    scopus 로고
    • Mast cells, basophils, and eosinophils: Distinct but overlapping pathways for recruitment
    • Bochner, B. S., and R. P. Schleimer. 2001. Mast cells, basophils, and eosinophils: distinct but overlapping pathways for recruitment. Immunol. Rev. 179: 5-15.
    • (2001) Immunol. Rev. , vol.179 , pp. 5-15
    • Bochner, B.S.1    Schleimer, R.P.2
  • 7
    • 0035105112 scopus 로고    scopus 로고
    • IL-5-induced airway eosinophilia: The key to asthma?
    • Hamelmann, E., and E. W. Gelfand. 2001. IL-5-induced airway eosinophilia: the key to asthma? Immunol. Rev. 179: 182-191.
    • (2001) Immunol. Rev. , vol.179 , pp. 182-191
    • Hamelmann, E.1    Gelfand, E.W.2
  • 10
    • 0027235684 scopus 로고
    • Upregulation of formyl-peptide and interleukin-8-induced eosinophil chemotaxis in patients with allergic asthma
    • Warringa, R. A., H. J. Mengelers, J. A. Raaijmakers, P. L. Bruijnzeel, and L. Koenderman. 1993. Upregulation of formyl-peptide and interleukin-8- induced eosinophil chemotaxis in patients with allergic asthma. J. Allergy Clin. Immunol. 91: 1198-1205.
    • (1993) J. Allergy Clin. Immunol. , vol.91 , pp. 1198-1205
    • Warringa, R.A.1    Mengelers, H.J.2    Raaijmakers, J.A.3    Bruijnzeel, P.L.4    Koenderman, L.5
  • 11
    • 0027762770 scopus 로고
    • Interleukin-8 is a chemo-attractant for eosinophils purified from subjects with a blood eosinophilia but not from normal healthy subjects
    • Sehmi, R., O. Cromwell, A. J. Wardlaw, R. Moqbel, and A. B. Kay. 1993. Interleukin-8 is a chemo-attractant for eosinophils purified from subjects with a blood eosinophilia but not from normal healthy subjects. Clin. Exp. Allergy 23: 1027-1036.
    • (1993) Clin. Exp. Allergy , vol.23 , pp. 1027-1036
    • Sehmi, R.1    Cromwell, O.2    Wardlaw, A.J.3    Moqbel, R.4    Kay, A.B.5
  • 12
    • 0026546493 scopus 로고
    • In vivo priming of platelet-activating factor-induced eosinophil chemotaxis in allergic asthmatic individuals
    • Warringa, R. A., H. J. Mengelers, P. H. Kuijper, J. A. Raaijmakers, P. L. Bruijnzeel, and L. Koenderman. 1992. In vivo priming of platelet-activating factor-induced eosinophil chemotaxis in allergic asthmatic individuals. Blood 79: 1836-1841.
    • (1992) Blood , vol.79 , pp. 1836-1841
    • Warringa, R.A.1    Mengelers, H.J.2    Kuijper, P.H.3    Raaijmakers, J.A.4    Bruijnzeel, P.L.5    Koenderman, L.6
  • 13
    • 0027269542 scopus 로고
    • Granulocyte-macrophage colony-stimulating factor induces sequential activation and deactivation of binding via a low-affinity IgG Fc receptor, hFcγRII, on human eosinophils
    • Koenderman, L., S. W. Hermans, P. J. Capel, and J. G. van de Winkel. 1993. Granulocyte-macrophage colony-stimulating factor induces sequential activation and deactivation of binding via a low-affinity IgG Fc receptor, hFcγRII, on human eosinophils. Blood 81: 2413-2419. (Pubitemid 23127079)
    • (1993) Blood , vol.81 , Issue.9 , pp. 2413-2419
    • Koenderman, L.1    Hermans, S.W.G.2    Capel, P.J.A.3    Van De, W.J.G.J.4
  • 14
    • 0026755576 scopus 로고
    • Interleukin-5 selectively enhances the chemotactic response of eosinophils obtained from normal but not eosinophilic subjects
    • Sehmi, R., A. J. Wardlaw, O. Cromwell, K. Kurihara, P. Waltmann, and A. B. Kay. 1992. Interleukin-5 selectively enhances the chemotactic response of eosinophils obtained from normal but not eosinophilic subjects. Blood 79: 2952-2959.
    • (1992) Blood , vol.79 , pp. 2952-2959
    • Sehmi, R.1    Wardlaw, A.J.2    Cromwell, O.3    Kurihara, K.4    Waltmann, P.5    Kay, A.B.6
  • 16
    • 0025313761 scopus 로고
    • The effects of recombinant granulocyte-macrophage colony-stimulating factor (GM-CSF) and interleukin-3 on the secretory capacity of human blood eosinophils
    • Tai, P. C., and C. J. Spry. 1990. The effects of recombinant granulocyte-macrophage colony-stimulating factor (GM-CSF) and interleukin-3 on the secretory capacity of human blood eosinophils. Clin. Exp. Immunol. 80: 426-434.
    • (1990) Clin. Exp. Immunol. , vol.80 , pp. 426-434
    • Tai, P.C.1    Spry, C.J.2
  • 17
    • 0036679853 scopus 로고    scopus 로고
    • GM-CSF in inflammation and autoimmunity
    • DOI 10.1016/S1471-4906(02)02260-3, PII S1471490602022603
    • Hamilton, J. A. 2002. GM-CSF in inflammation and autoimmunity. Trends Immunol. 23: 403-408. (Pubitemid 34804636)
    • (2002) Trends in Immunology , vol.23 , Issue.8 , pp. 403-408
    • Hamilton, J.A.1
  • 18
    • 30344449182 scopus 로고    scopus 로고
    • Functions of granulocyte-macrophage colony-stimulating factor
    • Fleetwood, A. J., A. D. Cook, and J. A. Hamilton. 2005. Functions of granulocyte-macrophage colony-stimulating factor. Crit. Rev. Immunol. 25: 405-428.
    • (2005) Crit. Rev. Immunol. , vol.25 , pp. 405-428
    • Fleetwood, A.J.1    Cook, A.D.2    Hamilton, J.A.3
  • 21
    • 0028332666 scopus 로고
    • CD11b/CD18 (Mac-1) is required for degranulation of human eosinophils induced by human recombinant granulocyte-macrophage colony-stimulating factor and platelet-activating factor
    • Horie, S., and H. Kita. 1994. CD11b/CD18 (Mac-1) is required for degranulation of human eosinophils induced by human recombinant granulocyte-macrophage colony-stimulating factor and platelet-activating factor. J. Immunol. 152: 5457-5467. (Pubitemid 24152995)
    • (1994) Journal of Immunology , vol.152 , Issue.11 , pp. 5457-5467
    • Horie, S.1    Kita, H.2
  • 22
    • 0031018338 scopus 로고    scopus 로고
    • Dual role of the actin cytoskeleton in regulating cell adhesion mediated by the integrin lymphocyte function-associated molecule-1
    • Lub, M., Y. van Kooyk, S. J. van Vliet, and C. G. Figdor. 1997. Dual role of the actin cytoskeleton in regulating cell adhesion mediated by the integrin lymphocyte function-associated molecule-1. Mol. Biol. Cell 8: 341-351.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 341-351
    • Lub, M.1    Van Kooyk, Y.2    Van Vliet, S.J.3    Figdor, C.G.4
  • 23
    • 0028274282 scopus 로고
    • Granulocyte-macrophage colony-stimulating factor, interleukin-3 (IL-3), and IL-5 greatly enhance the interaction of human eosinophils with opsonized particles by changing the affinity of complement receptor type 3
    • Blom, M., A. T. Tool, P. T. Kok, L. Koenderman, D. Roos, and A. J. Verhoeven. 1994. Granulocyte-macrophage colony-stimulating factor, interleukin-3 (IL-3), and IL-5 greatly enhance the interaction of human eosinophils with opsonized particles by changing the affinity of complement receptor type 3. Blood 83: 2978-2984.
    • (1994) Blood , vol.83 , pp. 2978-2984
    • Blom, M.1    Tool, A.T.2    Kok, P.T.3    Koenderman, L.4    Roos, D.5    Verhoeven, A.J.6
  • 24
    • 0028169823 scopus 로고
    • Cooperation between Fcg receptor II and complement receptor type 3 during activation of platelet-activating factor release by cytokine-primed human eosinophils
    • van der Bruggen, T., P. T. Kok, J. A. Raaijmakers, J. W. Lammers, and L. Koenderman. 1994. Cooperation between Fcg receptor II and complement receptor type 3 during activation of platelet-activating factor release by cytokine-primed human eosinophils. J. Immunol. 153: 2729-2735.
    • (1994) J. Immunol. , vol.153 , pp. 2729-2735
    • Van Der Bruggen, T.1    Kok, P.T.2    Raaijmakers, J.A.3    Lammers, J.W.4    Koenderman, L.5
  • 26
    • 0027511422 scopus 로고
    • Human plastin genes: Comparative gene structure, chromosome location, and differential expression in normal and neoplastic cells
    • Lin, C. S., T. Park, Z. P. Chen, and J. Leavitt. 1993. Human plastin genes: comparative gene structure, chromosome location, and differential expression in normal and neoplastic cells. J. Biol. Chem. 268: 2781-2792.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2781-2792
    • Lin, C.S.1    Park, T.2    Chen, Z.P.3    Leavitt, J.4
  • 27
    • 0023391588 scopus 로고
    • Calcium control of macrophage cytoplasmic gelation: Evidence for the involvement of the 70,000 Mr actin-bundling protein
    • Pacaud, M., and M. C. Harricane. 1987. Calcium control of macrophage cytoplasmic gelation: evidence for the involvement of the 70,000 Mr actin-bundling protein. J. Cell Sci. 88: 81-94.
    • (1987) J. Cell Sci. , vol.88 , pp. 81-94
    • Pacaud, M.1    Harricane, M.C.2
  • 28
    • 0032442866 scopus 로고    scopus 로고
    • Analysis and mapping of plastin phosphorylation
    • Lin, C. S., A. Lau, and T. F. Lue. 1998. Analysis and mapping of plastin phosphorylation. DNA Cell Biol. 17: 1041-1046.
    • (1998) DNA Cell Biol. , vol.17 , pp. 1041-1046
    • Lin, C.S.1    Lau, A.2    Lue, T.F.3
  • 29
    • 33744536569 scopus 로고    scopus 로고
    • Phosphorylation on Ser5 increases the F-actin-binding activity of L-plastin and promotes its targeting to sites of actin assembly in cells
    • DOI 10.1242/jcs.02874
    • Janji, B., A. Giganti, V. De Corte, M. Catillon, E. Bruyneel, D. Lentz, J. Plastino, J. Gettemans, and E. Friederich. 2006. Phosphorylation on Ser5 increases the F-actin- binding activity of L-plastin and promotes its targeting to sites of actin assembly in cells. J. Cell Sci. 119: 1947-1960. (Pubitemid 43811019)
    • (2006) Journal of Cell Science , vol.119 , Issue.9 , pp. 1947-1960
    • Janji, B.1    Giganti, A.2    De Corte, V.3    Catillon, M.4    Bruyneel, E.5    Lentz, D.6    Plastino, J.7    Gettemans, J.8    Friederich, E.9
  • 30
    • 0033527066 scopus 로고    scopus 로고
    • An invasion-related complex of cortactin, paxillin and PKCm associates with invadopodia at sites of extracellular matrix degradation
    • Bowden, E. T., M. Barth, D. Thomas, R. I. Glazer, and S. C. Mueller. 1999. An invasion-related complex of cortactin, paxillin and PKCm associates with invadopodia at sites of extracellular matrix degradation. Oncogene 18: 4440-4449.
    • (1999) Oncogene , vol.18 , pp. 4440-4449
    • Bowden, E.T.1    Barth, M.2    Thomas, D.3    Glazer, R.I.4    Mueller, S.C.5
  • 32
    • 1342304266 scopus 로고    scopus 로고
    • Possible Involvement of Optimally Phosphorylated L-Plastin in Activation of Superoxide-Generating NADPH Oxidase
    • DOI 10.1093/jb/mvg208
    • Oshizawa, T., T. Yamaguchi, K. Suzuki, Y. Yamamoto, and T. Hayakawa. 2003. Possible involvement of optimally phosphorylated L-plastin in activation of superoxide-generating NADPH oxidase. J. Biochem. 134: 827-834. (Pubitemid 38248357)
    • (2003) Journal of Biochemistry , vol.134 , Issue.6 , pp. 827-834
    • Oshizawa, T.1    Yamaguchi, T.2    Suzuki, K.3    Yamamoto, Y.4    Hayakawa, T.5
  • 33
    • 0032483008 scopus 로고    scopus 로고
    • A role for the actin-bundling protein L-plastin in the regulation of leukocyte integrin function
    • Jones, S. L., J. Wang, C. W. Turck, and E. J. Brown. 1998. A role for the actin-bundling protein L-plastin in the regulation of leukocyte integrin function. Proc. Natl. Acad. Sci. USA 95: 9331-9336.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9331-9336
    • Jones, S.L.1    Wang, J.2    Turck, C.W.3    Brown, E.J.4
  • 34
    • 22144496125 scopus 로고    scopus 로고
    • Plastins: Versatile modulators of actin organization in (patho)physiological cellular processes
    • Delanote, V., J. Vandekerckhove, and J. Gettemans. 2005. Plastins: versatile modulators of actin organization in (patho)physiological cellular processes. Acta Pharmacol. Sin. 26: 769-779.
    • (2005) Acta Pharmacol. Sin. , vol.26 , pp. 769-779
    • Delanote, V.1    Vandekerckhove, J.2    Gettemans, J.3
  • 35
    • 0033588228 scopus 로고    scopus 로고
    • Immune complex-induced integrin activation and L-plastin phosphorylation require protein kinase A
    • Wang, J., and E. J. Brown. 1999. Immune complex-induced integrin activation and L-plastin phosphorylation require protein kinase A. J. Biol. Chem. 274: 24349-24356.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24349-24356
    • Wang, J.1    Brown, E.J.2
  • 36
    • 0942268724 scopus 로고    scopus 로고
    • N-formyl peptide receptor subtypes in human neutrophils activate L-plastin phosphorylation through different signal transduction intermediates
    • Paclet, M. H., C. Davis, P. Kotsonis, J. Godovac-Zimmermann, A. W. Segal, and L. V. Dekker. 2004. N-formyl peptide receptor subtypes in human neutrophils activate L-plastin phosphorylation through different signal transduction intermediates. Biochem. J. 377: 469-477.
    • (2004) Biochem. J. , vol.377 , pp. 469-477
    • Paclet, M.H.1    Davis, C.2    Kotsonis, P.3    Godovac-Zimmermann, J.4    Segal, A.W.5    Dekker, L.V.6
  • 38
    • 0032479926 scopus 로고    scopus 로고
    • Lyn, Jak2, and Raf-1 kinases are critical for the antiapoptotic effect of interleukin 5, whereas only Raf-1 kinase is essential for eosinophil activation and degranulation
    • Pazdrak, K., B. Olszewska-Pazdrak, S. Stafford, R. P. Garofalo, and R. Alam. 1998. Lyn, Jak2, and Raf-1 kinases are critical for the antiapoptotic effect of interleukin 5, whereas only Raf-1 kinase is essential for eosinophil activation and degranulation. J. Exp. Med. 188: 421-429.
    • (1998) J. Exp. Med. , vol.188 , pp. 421-429
    • Pazdrak, K.1    Olszewska-Pazdrak, B.2    Stafford, S.3    Garofalo, R.P.4    Alam, R.5
  • 39
    • 33646729680 scopus 로고    scopus 로고
    • Functional analysis of the nuclear proteome of human A549 alveolar epithelial cells by HPLC-high resolution 2-D gel electrophoresis
    • Forbus, J., H. Spratt, J. Wiktorowicz, Z. Wu, I. Boldogh, L. Denner, A. Kurosky, R. C. Brasier, B. Luxon, and A. R. Brasier. 2006. Functional analysis of the nuclear proteome of human A549 alveolar epithelial cells by HPLC-high resolution 2-D gel electrophoresis. Proteomics 6: 2656-2672.
    • (2006) Proteomics , vol.6 , pp. 2656-2672
    • Forbus, J.1    Spratt, H.2    Wiktorowicz, J.3    Wu, Z.4    Boldogh, I.5    Denner, L.6    Kurosky, A.7    Brasier, R.C.8    Luxon, B.9    Brasier, A.R.10
  • 42
    • 0027209983 scopus 로고
    • Isolation and characterization of a regulated form of actin depolymerizing factor
    • Morgan, T. E., R. O. Lockerbie, L. S. Minamide, M. D. Browning, and J. R. Bamburg. 1993. Isolation and characterization of a regulated form of actin depolymerizing factor. J. Cell Biol. 122: 623-633.
    • (1993) J. Cell Biol. , vol.122 , pp. 623-633
    • Morgan, T.E.1    Lockerbie, R.O.2    Minamide, L.S.3    Browning, M.D.4    Bamburg, J.R.5
  • 44
    • 33845455480 scopus 로고    scopus 로고
    • Protein kinase Cb inhibition: A novel therapeutic strategy for diabetic microangiopathy
    • Idris, I., and R. Donnelly. 2006. Protein kinase Cb inhibition: a novel therapeutic strategy for diabetic microangiopathy. Diab. Vasc. Dis. Res. 3: 172-178.
    • (2006) Diab. Vasc. Dis. Res. , vol.3 , pp. 172-178
    • Idris, I.1    Donnelly, R.2
  • 46
    • 44849118633 scopus 로고    scopus 로고
    • Cross-talk between ICAM-1 and granulocyte-macrophage colony-stimulating factor receptor signaling modulates eosinophil survival and activation
    • Pazdrak, K., T. W. Young, S. Stafford, B. Olszewska-Pazdrak, C. Straub, V. Starosta, A. Brasier, and A. Kurosky. 2008. Cross-talk between ICAM-1 and granulocyte-macrophage colony-stimulating factor receptor signaling modulates eosinophil survival and activation. J. Immunol. 180: 4182-4190.
    • (2008) J. Immunol. , vol.180 , pp. 4182-4190
    • Pazdrak, K.1    Young, T.W.2    Stafford, S.3    Olszewska-Pazdrak, B.4    Straub, C.5    Starosta, V.6    Brasier, A.7    Kurosky, A.8
  • 47
    • 0035204427 scopus 로고    scopus 로고
    • A peptide carrier for the delivery of biologically active proteins into mammalian cells
    • Morris, M. C., J. Depollier, J. Mery, F. Heitz, and G. Divita. 2001. A peptide carrier for the delivery of biologically active proteins into mammalian cells. Nat. Biotechnol. 19: 1173-1176.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 1173-1176
    • Morris, M.C.1    Depollier, J.2    Mery, J.3    Heitz, F.4    Divita, G.5
  • 49
  • 50
    • 0033565261 scopus 로고    scopus 로고
    • PKCα regulates β1 integrin-dependent cell motility through association and control of integrin traffic
    • Ng, T., D. Shima, A. Squire, P. I. Bastiaens, S. Gschmeissner, M. J. Humphries, and P. J. Parker. 1999. PKCα regulates β1 integrin-dependent cell motility through association and control of integrin traffic. EMBO J. 18: 3909-3923.
    • (1999) EMBO J. , vol.18 , pp. 3909-3923
    • Ng, T.1    Shima, D.2    Squire, A.3    Bastiaens, P.I.4    Gschmeissner, S.5    Humphries, M.J.6    Parker, P.J.7
  • 51
    • 0034739854 scopus 로고    scopus 로고
    • Activated R-ras, Rac1, PI 3-kinase and PKCepsilon can each restore cell spreading inhibited by isolated integrin β1 cytoplasmic domains
    • Berrier, A. L., A. M. Mastrangelo, J. Downward, M. Ginsberg, and S. E. LaFlamme. 2000. Activated R-ras, Rac1, PI 3-kinase and PKCepsilon can each restore cell spreading inhibited by isolated integrin β1 cytoplasmic domains. J. Cell Biol. 151: 1549-1560.
    • (2000) J. Cell Biol. , vol.151 , pp. 1549-1560
    • Berrier, A.L.1    Mastrangelo, A.M.2    Downward, J.3    Ginsberg, M.4    LaFlamme, S.E.5
  • 52
    • 0034004457 scopus 로고    scopus 로고
    • Rap1 is a potent activation signal for leukocyte function-associated antigen 1 distinct from protein kinase C and phosphatidylinositol-3-OH kinase
    • Katagiri, K., M. Hattori, N. Minato, S. Irie, K. Takatsu, and T. Kinashi. 2000. Rap1 is a potent activation signal for leukocyte function-associated antigen 1 distinct from protein kinase C and phosphatidylinositol-3-OH kinase. Mol. Cell. Biol. 20: 1956-1969.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1956-1969
    • Katagiri, K.1    Hattori, M.2    Minato, N.3    Irie, S.4    Takatsu, K.5    Kinashi, T.6
  • 53
    • 0031893954 scopus 로고    scopus 로고
    • Rack1, a receptor for activated protein kinase C, interacts with integrin β subunit
    • Liliental, J., and D. D. Chang. 1998. Rack1, a receptor for activated protein kinase C, interacts with integrin β subunit. J. Biol. Chem. 273: 2379-2383.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2379-2383
    • Liliental, J.1    Chang, D.D.2
  • 54
    • 0038606044 scopus 로고    scopus 로고
    • Activation of leukocyte β2-integrins
    • Gahmberg, C. G., and S. Fagerholm. 2002. Activation of leukocyte β2-integrins. Vox Sang. 83(Suppl. 1): 355-358.
    • (2002) Vox Sang. , vol.83 , Issue.SUPPL. 1 , pp. 355-358
    • Gahmberg, C.G.1    Fagerholm, S.2
  • 55
    • 0037127257 scopus 로고    scopus 로고
    • Phosphorylation of the cytoplasmic domain of the integrin CD18 chain by protein kinase C isoforms in leukocytes
    • Fagerholm, S., N. Morrice, C. G. Gahmberg, and P. Cohen. 2002. Phosphorylation of the cytoplasmic domain of the integrin CD18 chain by protein kinase C isoforms in leukocytes. J. Biol. Chem. 277: 1728-1738.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1728-1738
    • Fagerholm, S.1    Morrice, N.2    Gahmberg, C.G.3    Cohen, P.4
  • 56
    • 0034161386 scopus 로고    scopus 로고
    • Inhibition of degranulation and interleukin-6 production in mast cells derived from mice deficient in protein kinase Cβ
    • Nechushtan, H., M. Leitges, C. Cohen, G. Kay, and E. Razin. 2000. Inhibition of degranulation and interleukin-6 production in mast cells derived from mice deficient in protein kinase Cβ. Blood 95: 1752-1757. (Pubitemid 30120839)
    • (2000) Blood , vol.95 , Issue.5 , pp. 1752-1757
    • Nechushtan, H.1    Leitges, M.2    Cohen, C.3    Kay, G.4    Razin, E.5
  • 58
    • 0036854481 scopus 로고    scopus 로고
    • Protein kinase Cβ (PKCβ): Nomal functions and dieases
    • Kawakami, T., Y. Kawakami, and J. Kitaura. 2002. Protein kinase Cβ (PKCβ): normal functions and diseases. J. Biochem. 132: 677-682. (Pubitemid 35408488)
    • (2002) Journal of Biochemistry , vol.132 , Issue.5 , pp. 677-682
    • Kawakami, T.1    Kawakami, Y.2    Kitaura, J.3
  • 59
    • 0038337728 scopus 로고    scopus 로고
    • Actin assembly is a crucial factor for superoxide anion generation from adherent human eosinophils
    • Suzuki, M., M. Kato, H. Hanaka, T. Izumi, and A. Morikawa. 2003. Actin assembly is a crucial factor for superoxide anion generation from adherent human eosinophils. J. Allergy Clin. Immunol. 112: 126-133.
    • (2003) J. Allergy Clin. Immunol. , vol.112 , pp. 126-133
    • Suzuki, M.1    Kato, M.2    Hanaka, H.3    Izumi, T.4    Morikawa, A.5
  • 60
    • 0028933571 scopus 로고
    • Complete primary structure and phosphorylation site of the 65-kDa macrophage protein phosphorylated by stimulation with bacterial lipopolysaccharide
    • Shinomiya, H., A. Hagi, M. Fukuzumi, M. Mizobuchi, H. Hirata, and S. Utsumi. 1995. Complete primary structure and phosphorylation site of the 65-kDa macrophage protein phosphorylated by stimulation with bacterial lipopolysaccharide. J. Immunol. 154: 3471-3478.
    • (1995) J. Immunol. , vol.154 , pp. 3471-3478
    • Shinomiya, H.1    Hagi, A.2    Fukuzumi, M.3    Mizobuchi, M.4    Hirata, H.5    Utsumi, S.6
  • 61
    • 0027216620 scopus 로고
    • Characterization of a 64-kd protein phosphorylated during chemotactic activation with IL-8 and fMLP of human polymorphonuclear leukocytes, I: Phosphorylation of a 64-kd protein and other proteins
    • Shibata, M., T. Ohoka, S. Mizuno, and K. Suzuki. 1993. Characterization of a 64-kd protein phosphorylated during chemotactic activation with IL-8 and fMLP of human polymorphonuclear leukocytes, I: Phosphorylation of a 64-kd protein and other proteins. J. Leukoc. Biol. 54: 1-9.
    • (1993) J. Leukoc. Biol. , vol.54 , pp. 1-9
    • Shibata, M.1    Ohoka, T.2    Mizuno, S.3    Suzuki, K.4
  • 62
    • 0029666259 scopus 로고    scopus 로고
    • FcγRII-mediated adhesion and phagocytosis induce L-plastin phosphorylation in human neutrophils
    • Jones, S. L., and E. J. Brown. 1996. FcγRII-mediated adhesion and phagocytosis induce L-plastin phosphorylation in human neutrophils. J. Biol. Chem. 271: 14623-14630.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14623-14630
    • Jones, S.L.1    Brown, E.J.2
  • 65
    • 0029913643 scopus 로고    scopus 로고
    • Adhesionactivating phorbol ester increases the mobility of leukocyte integrin LFA-1 in cultured lymphocytes
    • Kucik, D. F., M. L. Dustin, J. M. Miller, and E. J. Brown. 1996. Adhesionactivating phorbol ester increases the mobility of leukocyte integrin LFA-1 in cultured lymphocytes. J. Clin. Invest. 97: 2139-2144.
    • (1996) J. Clin. Invest. , vol.97 , pp. 2139-2144
    • Kucik, D.F.1    Dustin, M.L.2    Miller, J.M.3    Brown, E.J.4
  • 66
    • 0032516848 scopus 로고    scopus 로고
    • Kinetic analysis of the interaction of actin-depolymerizing factor (ADF)/cofilin with G- and F-actins. Comparison of plant and human ADFs and effect of phosphorylation
    • Ressad, F., D. Didry, G. X. Xia, Y. Hong, N. H. Chua, D. Pantaloni, and M. F. Carlier. 1998. Kinetic analysis of the interaction of actin-depolymerizing factor (ADF)/cofilin with G- and F-actins. Comparison of plant and human ADFs and effect of phosphorylation. J. Biol. Chem. 273: 20894-20902.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20894-20902
    • Ressad, F.1    Didry, D.2    Xia, G.X.3    Hong, Y.4    Chua, N.H.5    Pantaloni, D.6    Carlier, M.F.7


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