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Volumn 290, Issue 1, 2003, Pages 155-167

Regulation of CD43-induced U937 homotypic aggregation

Author keywords

Adhesion; CD43; CD98; Clustering; Integrin; Phosphatase; Protein kinase C; Signaling; Tyrosine phosphorylation

Indexed keywords

BETA1 INTEGRIN; CD98 ANTIGEN; CELL ADHESION MOLECULE; CYTOSKELETON PROTEIN; LEUKOSIALIN; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN KINASE C INHIBITOR; PROTEIN TYROSINE PHOSPHATASE INHIBITOR; TYROSINE;

EID: 0141569177     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-4827(03)00322-7     Document Type: Article
Times cited : (31)

References (60)
  • 1
    • 0033768928 scopus 로고    scopus 로고
    • Cell migration in the immune system: The evolving inter-related roles of adhesion molecules and proteinases
    • Madri J.A., Graesser D. Cell migration in the immune system the evolving inter-related roles of adhesion molecules and proteinases . Dev. Immunol. 7:2000;103-116.
    • (2000) Dev. Immunol. , vol.7 , pp. 103-116
    • Madri, J.A.1    Graesser, D.2
  • 2
    • 0034469343 scopus 로고    scopus 로고
    • Cell-cell interactions in synovitis: Endothelial cells and immune cell migration
    • Szekanecz Z., Koch A.E. Cell-cell interactions in synovitis endothelial cells and immune cell migration . Arthritis Res. 2:2000;368-373.
    • (2000) Arthritis Res. , vol.2 , pp. 368-373
    • Szekanecz, Z.1    Koch, A.E.2
  • 3
    • 0024362467 scopus 로고
    • Human tonsillar dendritic cell-induced T cell responses: Analysis of molecular mechanisms using monoclonal antibodies
    • King P.D., Katz D.R. Human tonsillar dendritic cell-induced T cell responses analysis of molecular mechanisms using monoclonal antibodies . Eur. J. Immunol. 19:1989;581-587.
    • (1989) Eur. J. Immunol. , vol.19 , pp. 581-587
    • King, P.D.1    Katz, D.R.2
  • 4
    • 0027523565 scopus 로고
    • T-cell-receptor engagement and tumor ICAM-1 up-regulation are required to by-pass low susceptibility of melanoma cells to autologous CTL-mediated lysis
    • Anichini A., Mortarini R., Alberti S., Mantovani A., Parmiani G. T-cell-receptor engagement and tumor ICAM-1 up-regulation are required to by-pass low susceptibility of melanoma cells to autologous CTL-mediated lysis. Int. J. Cancer. 53:1993;994-1001.
    • (1993) Int. J. Cancer. , vol.53 , pp. 994-1001
    • Anichini, A.1    Mortarini, R.2    Alberti, S.3    Mantovani, A.4    Parmiani, G.5
  • 5
    • 0035947768 scopus 로고    scopus 로고
    • Endothelial cell laminin isoforms, laminins 8 and 10, play decisive roles in T cell recruitment across the blood-brain barrier in experimental autoimmune encephalomyelitis
    • Sixt M., Engelhardt B., Pausch F., Hallmann R., Wendler O., Sorokin L.M. Endothelial cell laminin isoforms, laminins 8 and 10, play decisive roles in T cell recruitment across the blood-brain barrier in experimental autoimmune encephalomyelitis. J. Cell Biol. 153:2001;933-946.
    • (2001) J. Cell Biol. , vol.153 , pp. 933-946
    • Sixt, M.1    Engelhardt, B.2    Pausch, F.3    Hallmann, R.4    Wendler, O.5    Sorokin, L.M.6
  • 7
    • 0034544373 scopus 로고    scopus 로고
    • Altered expression and function of beta1 integrins in a highly metastatic human lung adenocarcinoma cell line
    • Takenaka K., Shibuya M., Takeda Y., Hibino S., Gemma A., Ono Y., Kudoh S. Altered expression and function of beta1 integrins in a highly metastatic human lung adenocarcinoma cell line. Int. J. Oncol. 17:2000;1187-1194.
    • (2000) Int. J. Oncol. , vol.17 , pp. 1187-1194
    • Takenaka, K.1    Shibuya, M.2    Takeda, Y.3    Hibino, S.4    Gemma, A.5    Ono, Y.6    Kudoh, S.7
  • 8
    • 0026021936 scopus 로고
    • The dimensions of the T lymphocyte glycoprotein leukosialin and identification of linear protein epitopes that can be modified by glycosylation
    • Cyster J.G., Shotton D.M., Williams A.F. The dimensions of the T lymphocyte glycoprotein leukosialin and identification of linear protein epitopes that can be modified by glycosylation. EMBO J. 10:1991;890-893.
    • (1991) EMBO J. , vol.10 , pp. 890-893
    • Cyster, J.G.1    Shotton, D.M.2    Williams, A.F.3
  • 9
    • 0022893107 scopus 로고
    • Morphological abnormalities in the lymphocytes of patients with the Wiskott-Aldrich syndrome
    • Kenney D., Cairns L., Remold-O'Donnell E., Peterson J., Rosen F.S., Parkman R. Morphological abnormalities in the lymphocytes of patients with the Wiskott-Aldrich syndrome. Blood. 68:1986;1329-1332.
    • (1986) Blood , vol.68 , pp. 1329-1332
    • Kenney, D.1    Cairns, L.2    Remold-O'Donnell, E.3    Peterson, J.4    Rosen, F.S.5    Parkman, R.6
  • 11
    • 0028141933 scopus 로고
    • Monoclonal antibodies to leucosialin (CD43) induce homotypic aggregation of the human mast cell line HMC-1: Characterization of leucosialin on HMC-1 cells
    • Weber S., Ruh B., Dippel E., Czarnetzki B.M. Monoclonal antibodies to leucosialin (CD43) induce homotypic aggregation of the human mast cell line HMC-1 characterization of leucosialin on HMC-1 cells . Immunology. 82:1994;638-644.
    • (1994) Immunology , vol.82 , pp. 638-644
    • Weber, S.1    Ruh, B.2    Dippel, E.3    Czarnetzki, B.M.4
  • 12
    • 0031225573 scopus 로고    scopus 로고
    • Antibodies against sialophorin (CD43) enhance the capacity of dendritic cells to cluster and activate T lymphocytes
    • Fanales-Belasio E., Zambruno G., Cavani A., Girolomoni G. Antibodies against sialophorin (CD43) enhance the capacity of dendritic cells to cluster and activate T lymphocytes. J. Immunol. 159:1997;2203-2211.
    • (1997) J. Immunol. , vol.159 , pp. 2203-2211
    • Fanales-Belasio, E.1    Zambruno, G.2    Cavani, A.3    Girolomoni, G.4
  • 16
    • 0029120438 scopus 로고
    • Negative regulation of T-cell adhesion and activation by CD43
    • Manjunath N., Correa M., Ardman M., Ardman B. Negative regulation of T-cell adhesion and activation by CD43. Nature. 377:1995;535-538.
    • (1995) Nature , vol.377 , pp. 535-538
    • Manjunath, N.1    Correa, M.2    Ardman, M.3    Ardman, B.4
  • 17
    • 0023755715 scopus 로고
    • Induction of aggregation and enhancement of proliferation and IL-2 secretion in human T cells bny antibodies to CD43
    • Axelsson B., Youseffi-Etemad R., Hammarstrom S., Perlmann P. Induction of aggregation and enhancement of proliferation and IL-2 secretion in human T cells bny antibodies to CD43. J. Immunol. 141:1988;2912-2917.
    • (1988) J. Immunol. , vol.141 , pp. 2912-2917
    • Axelsson, B.1    Youseffi-Etemad, R.2    Hammarstrom, S.3    Perlmann, P.4
  • 18
    • 0024375144 scopus 로고
    • A monoclonal antibody to sialophorin (CD43) induces homotypic adhesion and activation of human monocytes
    • Nong Y.H., Remold-O'Donnell E., LeBien T.W., Remold H.G. A monoclonal antibody to sialophorin (CD43) induces homotypic adhesion and activation of human monocytes. J. Exp. Med. 170:1989;259-267.
    • (1989) J. Exp. Med. , vol.170 , pp. 259-267
    • Nong, Y.H.1    Remold-O'Donnell, E.2    LeBien, T.W.3    Remold, H.G.4
  • 19
    • 0025726368 scopus 로고
    • Enhancement of T-cell activation by the CD43 molecule whose expression is defective in Wiskott-Aldrich syndrome
    • Park J.K., Rosenstein Y.J., Remold-O'Donnell E., Bierer B.E., Rosen F.S., Burakoff S.J. Enhancement of T-cell activation by the CD43 molecule whose expression is defective in Wiskott-Aldrich syndrome. Nature. 350:1991;706-709.
    • (1991) Nature , vol.350 , pp. 706-709
    • Park, J.K.1    Rosenstein, Y.J.2    Remold-O'Donnell, E.3    Bierer, B.E.4    Rosen, F.S.5    Burakoff, S.J.6
  • 21
    • 0029969645 scopus 로고    scopus 로고
    • Parallel pattern of expression of CD43 and of LFA-1 on the CD45RA+ (naïve) and CD45RO+ (memory) subsets of human CD4+ and CD8+ cells: Correlation with the aggregative response of the cells to CD43 monoclonal antibodies
    • Youseffi-Etemad R., Axelsson B. Parallel pattern of expression of CD43 and of LFA-1 on the CD45RA+ (naïve) and CD45RO+ (memory) subsets of human CD4+ and CD8+ cells correlation with the aggregative response of the cells to CD43 monoclonal antibodies . Immunology. 87:1996;439-446.
    • (1996) Immunology , vol.87 , pp. 439-446
    • Youseffi-Etemad, R.1    Axelsson, B.2
  • 22
    • 0029959827 scopus 로고    scopus 로고
    • Characterization of a CD43/leukosialin-mediated pathway for inducing apoptosis in human T-lymphoblastoid cells
    • Brown T.J., Shuford W.W., Wang W.C., Nadler S.G., Bailey T.S., Marquardt H., Mittler R.S. Characterization of a CD43/leukosialin-mediated pathway for inducing apoptosis in human T-lymphoblastoid cells. J. Biol. Chem. 271:1996;27686-27695.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27686-27695
    • Brown, T.J.1    Shuford, W.W.2    Wang, W.C.3    Nadler, S.G.4    Bailey, T.S.5    Marquardt, H.6    Mittler, R.S.7
  • 24
    • 0033400455 scopus 로고    scopus 로고
    • High level expression of CD43 inhibits T cell receptor/CD3-mediated apoptosis
    • He Y.W., Bevan M.J. High level expression of CD43 inhibits T cell receptor/CD3-mediated apoptosis. J. Exp. Med. 190:1999;1903-1908.
    • (1999) J. Exp. Med. , vol.190 , pp. 1903-1908
    • He, Y.W.1    Bevan, M.J.2
  • 26
    • 0032700438 scopus 로고    scopus 로고
    • Rho GTPases control migration and polarization of adhesion molecules and cytoskeletal ERM components in T lymphocytes
    • del Pozo M.A., Vicente-Manzanares M., Tejedor R., Serrador J.M., Sanchez-Madrid F. Rho GTPases control migration and polarization of adhesion molecules and cytoskeletal ERM components in T lymphocytes. Eur. J. Immunol. 29:1999;3609-3620.
    • (1999) Eur. J. Immunol. , vol.29 , pp. 3609-3620
    • Del Pozo, M.A.1    Vicente-Manzanares, M.2    Tejedor, R.3    Serrador, J.M.4    Sanchez-Madrid, F.5
  • 27
    • 0033612533 scopus 로고    scopus 로고
    • Direct involvement of ezrin/radixin/moesin (ERM)-binding membrane proteins in the organization of microvilli in collaboration with activated ERM proteins
    • Yonemura S., Tsukita S., Tsukita S. Direct involvement of ezrin/radixin/moesin (ERM)-binding membrane proteins in the organization of microvilli in collaboration with activated ERM proteins. J. Cell Biol. 145:1999;1497-1509.
    • (1999) J. Cell Biol. , vol.145 , pp. 1497-1509
    • Yonemura, S.1    Tsukita, S.2    Tsukita, S.3
  • 28
    • 0025724098 scopus 로고
    • Phagocytic cell molecules that bind the collagen-like region of C1q: Involvement in the C1q-mediated enhancement of phagocytosis
    • Guan E.N., Burgess W.H., Robinson S.L., Goodman E.B., McTigue K.J., Tenner A.J. Phagocytic cell molecules that bind the collagen-like region of C1q involvement in the C1q-mediated enhancement of phagocytosis . J. Biol. Chem. 266:1991;20345-22055.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20345-22055
    • Guan, E.N.1    Burgess, W.H.2    Robinson, S.L.3    Goodman, E.B.4    McTigue, K.J.5    Tenner, A.J.6
  • 29
    • 0033152305 scopus 로고    scopus 로고
    • A common signaling pathway via Syk and Lyn tyrosine kinases generated from capping of the sialomucins CD34 and CD43 in immature hematopoietic cells
    • Tada J., Omine M., Suda T., Yamaguchi N. A common signaling pathway via Syk and Lyn tyrosine kinases generated from capping of the sialomucins CD34 and CD43 in immature hematopoietic cells. Blood. 93:1999;3723-3735.
    • (1999) Blood , vol.93 , pp. 3723-3735
    • Tada, J.1    Omine, M.2    Suda, T.3    Yamaguchi, N.4
  • 31
    • 0035880225 scopus 로고    scopus 로고
    • The functional interactions between CD98, beta1-integrins, and CD147 in the induction of U937 homotypic aggregation
    • Cho J.Y., Fox D.A., Horejsi V., Sagawa K., Skubitz K.M., Katz D.R., Chain B.M. The functional interactions between CD98, beta1-integrins, and CD147 in the induction of U937 homotypic aggregation. Blood. 98:2001;374-382.
    • (2001) Blood , vol.98 , pp. 374-382
    • Cho, J.Y.1    Fox, D.A.2    Horejsi, V.3    Sagawa, K.4    Skubitz, K.M.5    Katz, D.R.6    Chain, B.M.7
  • 33
    • 0026469679 scopus 로고
    • Human neutrophils release their major membrane sialoprotein, leukosialin (CD43), during cell activation
    • Rieu P., Porteu F., Bessou G., Lesavre P., Halbwachs-Mecarelli L. Human neutrophils release their major membrane sialoprotein, leukosialin (CD43), during cell activation. Eur. J. Immunol. 22:1992;3021-3026.
    • (1992) Eur. J. Immunol. , vol.22 , pp. 3021-3026
    • Rieu, P.1    Porteu, F.2    Bessou, G.3    Lesavre, P.4    Halbwachs-Mecarelli, L.5
  • 34
    • 0031749699 scopus 로고    scopus 로고
    • CD43 (sialophorin, leukosialin) shedding is an initial event during neutrophil migration, which could be closely related to the spreading of adherent cells
    • Lopez S., Seveau S., Lesavre P., Robinson M.K., Halbwachs-Mecarelli L. CD43 (sialophorin, leukosialin) shedding is an initial event during neutrophil migration, which could be closely related to the spreading of adherent cells. Cell. Adhes. Commun. 5:1998;151-160.
    • (1998) Cell. Adhes. Commun. , vol.5 , pp. 151-160
    • Lopez, S.1    Seveau, S.2    Lesavre, P.3    Robinson, M.K.4    Halbwachs-Mecarelli, L.5
  • 35
    • 0035936848 scopus 로고    scopus 로고
    • An essential role for calmodulin in regulating human T cell aggregation
    • Fagerholm S.C., Prescott A., Cohen P., Gahmberg C.G. An essential role for calmodulin in regulating human T cell aggregation. FEBS Lett. 491:2001;131-136.
    • (2001) FEBS Lett. , vol.491 , pp. 131-136
    • Fagerholm, S.C.1    Prescott, A.2    Cohen, P.3    Gahmberg, C.G.4
  • 37
    • 3543036342 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase Shp-2 regulates cell spreading, migration, and focal adhesion
    • Yu D.H., Qu C.K., Henegariu O., Lu X., Feng G.S. Protein-tyrosine phosphatase Shp-2 regulates cell spreading, migration, and focal adhesion. J. Biol. Chem. 273:1998;21125-21131.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21125-21131
    • Yu, D.H.1    Qu, C.K.2    Henegariu, O.3    Lu, X.4    Feng, G.S.5
  • 38
    • 0030936012 scopus 로고    scopus 로고
    • The protein-tyrosine phosphatase SHP-2 binds platelet/endothelial cell adhesion molecule-1 (PECAM-1) and forms a distinct signaling complex during platelet aggregation: Evidence for a mechanistic link between PECAM-1- and integrin-mediated cellular signaling
    • Jackson D.E., Ward C.M., Wang R., Newman P.J., Garver T.D. The protein-tyrosine phosphatase SHP-2 binds platelet/endothelial cell adhesion molecule-1 (PECAM-1) and forms a distinct signaling complex during platelet aggregation evidence for a mechanistic link between PECAM-1- and integrin-mediated cellular signaling . J. Biol. Chem. 272:1997;6986-6993.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6986-6993
    • Jackson, D.E.1    Ward, C.M.2    Wang, R.3    Newman, P.J.4    Garver, T.D.5
  • 39
    • 0035794169 scopus 로고    scopus 로고
    • Fibrin clot retraction by human platelets correlates with alpha(IIb)beta(3) integrin-dependent protein tyrosine dephosphorylation
    • Osdoit S., Rosa J.P. Fibrin clot retraction by human platelets correlates with alpha(IIb)beta(3) integrin-dependent protein tyrosine dephosphorylation. J. Biol. Chem. 276:2001;6703-6710.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6703-6710
    • Osdoit, S.1    Rosa, J.P.2
  • 41
    • 0031006110 scopus 로고    scopus 로고
    • Tyrosine phosphorylation at a site highly conserved in the L1 family of cell adhesion molecules abolishes ankyrin binding and increases lateral mobility of neurofascin
    • Garver T.D., Ren Q., Tuvia S., Bennett V. Tyrosine phosphorylation at a site highly conserved in the L1 family of cell adhesion molecules abolishes ankyrin binding and increases lateral mobility of neurofascin. J. Cell Biol. 137:1997;703-714.
    • (1997) J. Cell Biol. , vol.137 , pp. 703-714
    • Garver, T.D.1    Ren, Q.2    Tuvia, S.3    Bennett, V.4
  • 42
    • 0032514916 scopus 로고    scopus 로고
    • Evidence of zeta protein kinase C involvement in polymorphonuclear neutrophil integrin-dependent adhesion and chemotaxis
    • Laudanna C., Mochly-Rosen D., Liron T., Constantin G., Butcher E.C. Evidence of zeta protein kinase C involvement in polymorphonuclear neutrophil integrin-dependent adhesion and chemotaxis. J. Biol. Chem. 273:1998;30306-30315.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30306-30315
    • Laudanna, C.1    Mochly-Rosen, D.2    Liron, T.3    Constantin, G.4    Butcher, E.C.5
  • 43
    • 0033515611 scopus 로고    scopus 로고
    • E-cadherin mediates aggregation-dependent survival of prostate and mammary epithelial cells through the retinoblastoma cell cycle control pathway
    • Day M.L., Zhao X., Vallorosi C.J., Putzi M., Powell C.T., Lin C., Day K.C. E-cadherin mediates aggregation-dependent survival of prostate and mammary epithelial cells through the retinoblastoma cell cycle control pathway. J. Biol. Chem. 274:1999;9656-9664.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9656-9664
    • Day, M.L.1    Zhao, X.2    Vallorosi, C.J.3    Putzi, M.4    Powell, C.T.5    Lin, C.6    Day, K.C.7
  • 44
    • 0026750308 scopus 로고
    • Cross-linking of sialophorin (CD43) induces neutrophil aggregation in a CD18-dependent and a CD18-independent way
    • Kuijpers T.W., Hoogerwerf M., Kuijpers K.C., Schwartz B.R., Harlan J.M. Cross-linking of sialophorin (CD43) induces neutrophil aggregation in a CD18-dependent and a CD18-independent way. J. Immunol. 149:1992;998-1003.
    • (1992) J. Immunol. , vol.149 , pp. 998-1003
    • Kuijpers, T.W.1    Hoogerwerf, M.2    Kuijpers, K.C.3    Schwartz, B.R.4    Harlan, J.M.5
  • 45
    • 0027258259 scopus 로고
    • A new CD43 monoclonal antibody induces homotypic aggregation of human leucocytes through a CD11a/CD18-dependent and independent mechanism
    • De Smet W., Walter H., van Hove L. A new CD43 monoclonal antibody induces homotypic aggregation of human leucocytes through a CD11a/ CD18-dependent and independent mechanism. Immunology. 79:1993;46-54.
    • (1993) Immunology , vol.79 , pp. 46-54
    • De Smet, W.1    Walter, H.2    Van Hove, L.3
  • 47
    • 0033120554 scopus 로고    scopus 로고
    • Structural requirements for CD43 function
    • Walker J., Green J.M. Structural requirements for CD43 function. J. Immunol. 162:1999;4109-4114.
    • (1999) J. Immunol. , vol.162 , pp. 4109-4114
    • Walker, J.1    Green, J.M.2
  • 48
    • 0030453194 scopus 로고    scopus 로고
    • Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation: Roles of integrin aggregation and occupancy of receptors
    • Miyamoto S., Teramoto H., Gutkind J.S., Yamada K.M. Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation roles of integrin aggregation and occupancy of receptors . J. Cell Biol. 135:1996;1633-1642.
    • (1996) J. Cell Biol. , vol.135 , pp. 1633-1642
    • Miyamoto, S.1    Teramoto, H.2    Gutkind, J.S.3    Yamada, K.M.4
  • 50
    • 0025159472 scopus 로고
    • The role of CD44, CD45, CD45RO, CD46 and CD55 as potential anti-adhesion molecules involved in the binding of human tonsillar T cells to phorbol 12-myristate 13-acetate-differentiated U937 cells
    • King P.D., Batchelor A.H., Lawlor P., Katz D.R. The role of CD44, CD45, CD45RO, CD46 and CD55 as potential anti-adhesion molecules involved in the binding of human tonsillar T cells to phorbol 12-myristate 13-acetate-differentiated U937 cells. Eur. J. Immunol. 20:1990;363-368.
    • (1990) Eur. J. Immunol. , vol.20 , pp. 363-368
    • King, P.D.1    Batchelor, A.H.2    Lawlor, P.3    Katz, D.R.4
  • 51
    • 0029118777 scopus 로고
    • B-cell homotypic adhesion through exon-A restricted epitopes of CD45 involves LFA-1/ICAM-1, ICAM-3 interactions, and induces coclustering of CD45 and LFA-1
    • Zapata J.M., Campanero M.R., Marazuela M., Sanchez-Madrid F., de Landazuri M.O. B-cell homotypic adhesion through exon-A restricted epitopes of CD45 involves LFA-1/ICAM-1, ICAM-3 interactions, and induces coclustering of CD45 and LFA-1. Blood. 86:1995;1861-1872.
    • (1995) Blood , vol.86 , pp. 1861-1872
    • Zapata, J.M.1    Campanero, M.R.2    Marazuela, M.3    Sanchez-Madrid, F.4    De Landazuri, M.O.5
  • 52
    • 0030589324 scopus 로고    scopus 로고
    • CD100 is associated with CD45 at the surface of human T lymphocytes: Role in T cell homotypic adhesion
    • Herold C., Elhabazi A., Bismuth G., Bensussan A., Boumsell L. CD100 is associated with CD45 at the surface of human T lymphocytes role in T cell homotypic adhesion . J. Immunol. 157:1996;5262-5268.
    • (1996) J. Immunol. , vol.157 , pp. 5262-5268
    • Herold, C.1    Elhabazi, A.2    Bismuth, G.3    Bensussan, A.4    Boumsell, L.5
  • 53
    • 0032481269 scopus 로고    scopus 로고
    • Signal transduction via CD43 (leukosialin, sialophorin) and associated biological effects in human mast cell line (HMC-1)
    • Babina M., Weber S., Mammeri K., Henz B.M. Signal transduction via CD43 (leukosialin, sialophorin) and associated biological effects in human mast cell line (HMC-1). Biochem. Biophys. Res. Commun. 243:1998;163-169.
    • (1998) Biochem. Biophys. Res. Commun. , vol.243 , pp. 163-169
    • Babina, M.1    Weber, S.2    Mammeri, K.3    Henz, B.M.4
  • 55
    • 0033516666 scopus 로고    scopus 로고
    • Protein kinase C delta is essential for etoposide-induced apoptosis in salivary gland acinar cells
    • Reyland M.E., Anderson S.M., Matassa A.A., Barzen K.A., Quissell D.O. Protein kinase C delta is essential for etoposide-induced apoptosis in salivary gland acinar cells. J. Biol. Chem. 274:1999;19115-19123.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19115-19123
    • Reyland, M.E.1    Anderson, S.M.2    Matassa, A.A.3    Barzen, K.A.4    Quissell, D.O.5
  • 56
    • 0033805221 scopus 로고    scopus 로고
    • Rottlerin, a PKC isozyme-selective inhibitor, affects signaling events and cytokine production in human monocytes
    • Kontny E., Kurowska M., Szczepanska K., Maslinski W. Rottlerin, a PKC isozyme-selective inhibitor, affects signaling events and cytokine production in human monocytes. J. Leukocyte Biol. 67:2000;249-258.
    • (2000) J. Leukocyte Biol. , vol.67 , pp. 249-258
    • Kontny, E.1    Kurowska, M.2    Szczepanska, K.3    Maslinski, W.4
  • 57
    • 0027448806 scopus 로고
    • Inhibition of protein kinase C by N-myristoylated peptide substrate analogs
    • Ward N.E., O'Brian C.A. Inhibition of protein kinase C by N-myristoylated peptide substrate analogs. Biochemistry. 32:1993;11903-11909.
    • (1993) Biochemistry , vol.32 , pp. 11903-11909
    • Ward, N.E.1    O'Brian, C.A.2
  • 58
    • 0023792601 scopus 로고
    • Phosphorylation of T cell membrane proteins by activators of protein kinase C
    • Chatila T.A., Geha R.S. Phosphorylation of T cell membrane proteins by activators of protein kinase C. J. Immunol. 140:1988;4308-4314.
    • (1988) J. Immunol. , vol.140 , pp. 4308-4314
    • Chatila, T.A.1    Geha, R.S.2
  • 59
    • 0024415403 scopus 로고
    • Persistent superphosphorylation of leukosialin (CD43) in activated T cells and in tumour cell lines
    • Axelsson B., Perlmann P. Persistent superphosphorylation of leukosialin (CD43) in activated T cells and in tumour cell lines. Scand. J. Immunol. 30:1989;539-547.
    • (1989) Scand. J. Immunol. , vol.30 , pp. 539-547
    • Axelsson, B.1    Perlmann, P.2
  • 60
    • 0033565261 scopus 로고    scopus 로고
    • PKCalpha regulates beta1 integrin-dependent cell motility through association and control of integrin traffic
    • Ng T., Shima D., Squire A., Bastiaens P.I., Gschmeissner S., Humphries M.J., Parker P.J. PKCalpha regulates beta1 integrin-dependent cell motility through association and control of integrin traffic. EMBO J. 18:1999;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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.