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Volumn 117, Issue SUPPL. 1, 1998, Pages 68-71

Cross-linking of the β2 integrin, CD11b/CD18, on human eosinophils induces protein tyrosine phosphorylation and cellular degranulation

Author keywords

Degranulation; Eosinophil; Integrin; Signal transduction; Tyrosine kinase

Indexed keywords

ANTIBODY; CD11B ANTIGEN; CD18 ANTIGEN; CELL PROTEIN; INTEGRIN; PHOSPHOPROTEIN; PROTEIN TYROSINE KINASE; CROSS LINKING REAGENT; TYROSINE;

EID: 0031709950     PISSN: 10182438     EISSN: None     Source Type: Journal    
DOI: 10.1159/000053576     Document Type: Conference Paper
Times cited : (7)

References (17)
  • 1
    • 0022571546 scopus 로고
    • The eosinophil and the pathophysiology of asthma
    • Frigas E, Gleich GJ: The eosinophil and the pathophysiology of asthma. J Allergy Clin Immunol 1986;77:527-537.
    • (1986) J Allergy Clin Immunol , vol.77 , pp. 527-537
    • Frigas, E.1    Gleich, G.J.2
  • 4
    • 0025182959 scopus 로고
    • Adhesion receptors of the immune system
    • Springer TA: Adhesion receptors of the immune system. Nature 1990;346:425-434.
    • (1990) Nature , vol.346 , pp. 425-434
    • Springer, T.A.1
  • 5
    • 0025055028 scopus 로고
    • Fcγ and CD11/CD18 receptor expression on normal density and low density human eosinophils
    • Hartnell A, Moqbel R, Walsh GM, Bradley B, Kay AB: Fcγ and CD11/CD18 receptor expression on normal density and low density human eosinophils. Immunology 1990;69:264-270.
    • (1990) Immunology , vol.69 , pp. 264-270
    • Hartnell, A.1    Moqbel, R.2    Walsh, G.M.3    Bradley, B.4    Kay, A.B.5
  • 6
    • 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, Kita H: 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 1994;152: 5457-5467.
    • (1994) J Immunol , vol.152 , pp. 5457-5467
    • Horie, S.1    Kita, H.2
  • 9
    • 0028269393 scopus 로고
    • Ammonium chloride exposure inhibits cytokine-mediated eosinophil survival
    • Ide M, Weiler D, Kita H, Gleich GJ: Ammonium chloride exposure inhibits cytokine-mediated eosinophil survival. J Immunol Methods 1994;168:187-196.
    • (1994) J Immunol Methods , vol.168 , pp. 187-196
    • Ide, M.1    Weiler, D.2    Kita, H.3    Gleich, G.J.4
  • 10
    • 0028997992 scopus 로고
    • Tyrosine phosphorylation is required for eosinophil degranulation induced by immobilized immunoglobulins
    • Kato M, Abraham RT, Kita H: Tyrosine phosphorylation is required for eosinophil degranulation induced by immobilized immunoglobulins. J Immunol 1995:155:357-366.
    • (1995) J Immunol , vol.155 , pp. 357-366
    • Kato, M.1    Abraham, R.T.2    Kita, H.3
  • 11
    • 0028288927 scopus 로고
    • The role of protein tyrosine kinases and protein tyrosine phosphatases in T cell antigen receptor signal transduction
    • Chan AC, Desai DM, Weiss A: The role of protein tyrosine kinases and protein tyrosine phosphatases in T cell antigen receptor signal transduction. Annu Rev Immunol 1994;12:555-592.
    • (1994) Annu Rev Immunol , vol.12 , pp. 555-592
    • Chan, A.C.1    Desai, D.M.2    Weiss, A.3
  • 12
    • 0026535397 scopus 로고
    • Ligation of VLA-4 on T cells stimulates tyrosine phosphorylation of a 105-kD protein
    • Nojima Y, Rothstein DM, Sugita K, Schlossman SF, Morimoto C: Ligation of VLA-4 on T cells stimulates tyrosine phosphorylation of a 105-kD protein. J Exp Med 1992;175:1045-1053.
    • (1992) J Exp Med , vol.175 , pp. 1045-1053
    • Nojima, Y.1    Rothstein, D.M.2    Sugita, K.3    Schlossman, S.F.4    Morimoto, C.5
  • 14
    • 0026759309 scopus 로고
    • Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation
    • Guan JL, Schalloway D: Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation. Nature 1992;358:690-692.
    • (1992) Nature , vol.358 , pp. 690-692
    • Guan, J.L.1    Schalloway, D.2
  • 15
    • 0027455465 scopus 로고
    • Adhesion-dependent protein tyrosine phosphorylation in neutrophils treated with tumor necrosis factor
    • Fuortes M, Jin WW, Nathan C: Adhesion-dependent protein tyrosine phosphorylation in neutrophils treated with tumor necrosis factor. J Cell Biol 1993;120:777-784.
    • (1993) J Cell Biol , vol.120 , pp. 777-784
    • Fuortes, M.1    Jin, W.W.2    Nathan, C.3
  • 16
    • 0027416481 scopus 로고
    • Cell adherence to fibronectin and the aggregation of the high affinity immunoglobulin e receptor synergistically regulate tyrosine phosphorylation of a 105-115-kDa proteins
    • Hamawy MM, Mergenhagen SE, Siraganian RP: Cell adherence to fibronectin and the aggregation of the high affinity immunoglobulin E receptor synergistically regulate tyrosine phosphorylation of a 105-115-kDa proteins. J Biol Chem 1993;268:5227-5233.
    • (1993) J Biol Chem , vol.268 , pp. 5227-5233
    • Hamawy, M.M.1    Mergenhagen, S.E.2    Siraganian, R.P.3
  • 17
    • 0028938669 scopus 로고
    • Engagement of the vitronectin receptor (αVβ3) on murine T cells stimulates tyrosine phosphorylation of a 115-kDa protein
    • Brando C, Shevach EM: Engagement of the vitronectin receptor (αVβ3) on murine T cells stimulates tyrosine phosphorylation of a 115-kDa protein. J Immunol 1995;154:2005-2011.
    • (1995) J Immunol , vol.154 , pp. 2005-2011
    • Brando, C.1    Shevach, E.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.