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Volumn 31, Issue 11, 2003, Pages 1057-1065

Selectins and anti-CD15 (Lewis x/a) antibodies transmit activation signals in Hodgkin's lymphoma-derived cell lines

Author keywords

[No Author keywords available]

Indexed keywords

CBL PROTEIN; CD15 ANTIBODY; CD15 ANTIGEN; ENDOTHELIAL LEUKOCYTE ADHESION MOLECULE 1; IMMOBILIZED ANTIBODY; MONOCLONAL ANTIBODY; PADGEM PROTEIN; PROTEIN; RECOMBINANT PROTEIN; SELECTIN; STRESS ACTIVATED PROTEIN KINASE; TRANSCRIPTION FACTOR AP 1; UNCLASSIFIED DRUG;

EID: 0142227043     PISSN: 0301472X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-472X(03)00237-6     Document Type: Article
Times cited : (24)

References (39)
  • 1
    • 0030939504 scopus 로고    scopus 로고
    • Hodgkin's disease: A tumor with disturbed immunological pathways
    • Gruss H.J., Pinto A., Duyster J., Poppema S., Herrman F. Hodgkin's disease: a tumor with disturbed immunological pathways. Immunol Today. 18:1997;156-163.
    • (1997) Immunol Today , vol.18 , pp. 156-163
    • Gruss, H.J.1    Pinto, A.2    Duyster, J.3    Poppema, S.4    Herrman, F.5
  • 2
    • 0029870561 scopus 로고    scopus 로고
    • IL-1 and TNF-α in Reed-Sternberg cells of Hodgkin's disease - Correlation with clinical and morphological "inflamatory" features
    • Benharroch D., Prinsloo I., Apte R.N., et al. IL-1 and TNF-α in Reed-Sternberg cells of Hodgkin's disease - correlation with clinical and morphological "inflamatory" features. Eur Cytokine Netw. 7:1996;51-56.
    • (1996) Eur Cytokine Netw , vol.7 , pp. 51-56
    • Benharroch, D.1    Prinsloo, I.2    Apte, R.N.3
  • 3
    • 0036189576 scopus 로고    scopus 로고
    • Molecular biology of Hodgkin's lymphoma
    • Kuppers R. Molecular biology of Hodgkin's lymphoma. Adv Cancer Res. 84:2002;277-312.
    • (2002) Adv Cancer Res , vol.84 , pp. 277-312
    • Kuppers, R.1
  • 4
    • 0030271766 scopus 로고    scopus 로고
    • Carbohydrate recognition systems: Functional triads in cell-cell interactions
    • Crockett P., Feizi T. Carbohydrate recognition systems: functional triads in cell-cell interactions. Curr Biol. 6:1996;679-691.
    • (1996) Curr Biol , vol.6 , pp. 679-691
    • Crockett, P.1    Feizi, T.2
  • 5
    • 0021611610 scopus 로고
    • Structure of sialylated fucossyl lactosaminoglycan isolated from human granulocytes
    • Fukuda M., Spooncer E., Oates J.E., Dell A., Clock J.C. Structure of sialylated fucossyl lactosaminoglycan isolated from human granulocytes. J Biol Chem. 259:1984;10925-10935.
    • (1984) J Biol Chem , vol.259 , pp. 10925-10935
    • Fukuda, M.1    Spooncer, E.2    Oates, J.E.3    Dell, A.4    Clock, J.C.5
  • 6
    • 0033846853 scopus 로고    scopus 로고
    • Differential expression of CD15 and sialyl-CD15 antigens on Hodgkin-Reed-Sternberg cells and its biological significance in Hodgkin's disease
    • Benharroch D., Dima E., Levy A., et al. Differential expression of CD15 and sialyl-CD15 antigens on Hodgkin-Reed-Sternberg cells and its biological significance in Hodgkin's disease. Leuk Lymphoma. 39:2000;185-194.
    • (2000) Leuk Lymphoma , vol.39 , pp. 185-194
    • Benharroch, D.1    Dima, E.2    Levy, A.3
  • 7
    • 0030865851 scopus 로고    scopus 로고
    • Classical Hodgkin's disease - Clinical impact of the immunophenotype
    • Von Wasielewski R., Mengel M., Fisher R., et al. Classical Hodgkin's disease - Clinical impact of the immunophenotype. Am J Pathol. 151:1997;1123-1130.
    • (1997) Am J Pathol , vol.151 , pp. 1123-1130
    • Von Wasielewski, R.1    Mengel, M.2    Fisher, R.3
  • 8
    • 0029001510 scopus 로고
    • Selectin-carbohydrate interactions and the initiation of the inflammatory response
    • Laurence A.L. Selectin-carbohydrate interactions and the initiation of the inflammatory response. Annu Rev Biochem. 64:1995;113-139.
    • (1995) Annu Rev Biochem , vol.64 , pp. 113-139
    • Laurence, A.L.1
  • 9
    • 0028985944 scopus 로고
    • Association between sialyl Lewis a expression and tumor progression in melanoma
    • Kageshita T., Hirai S., Kimura T., Hanai N., Ohta S., Ono T. Association between sialyl Lewis a expression and tumor progression in melanoma. Cancer Res. 55:1995;1748-1751.
    • (1995) Cancer Res , vol.55 , pp. 1748-1751
    • Kageshita, T.1    Hirai, S.2    Kimura, T.3    Hanai, N.4    Ohta, S.5    Ono, T.6
  • 10
    • 0036190078 scopus 로고    scopus 로고
    • Carbohydrate expression profile of colorectal cancer cells is relevant to metastatic pattern and prognosis
    • Konno A., Hoshino Y., Terashima S., Motoki R., Kawaguchi T. Carbohydrate expression profile of colorectal cancer cells is relevant to metastatic pattern and prognosis. Clin Exp Metastasis. 19:2002;61-70.
    • (2002) Clin Exp Metastasis , vol.19 , pp. 61-70
    • Konno, A.1    Hoshino, Y.2    Terashima, S.3    Motoki, R.4    Kawaguchi, T.5
  • 11
    • 0029150418 scopus 로고
    • Phase I clinical trial of serotherapy in patients with acute myeloid leukemia with an immunoglobulin M monoclonal antibody to CD15
    • Ball E.D., Selvaggi K., Hurd D., et al. Phase I clinical trial of serotherapy in patients with acute myeloid leukemia with an immunoglobulin M monoclonal antibody to CD15. Clin Cancer Res. 1:1995;965-972.
    • (1995) Clin Cancer Res , vol.1 , pp. 965-972
    • Ball, E.D.1    Selvaggi, K.2    Hurd, D.3
  • 12
    • 0024374526 scopus 로고
    • CD15 antibodies increase neutrophil adhesion to endothelium by an LFA-1-dependent mechanism
    • Forsyth K.D., Simpson A.C., Levinsky R. CD15 antibodies increase neutrophil adhesion to endothelium by an LFA-1-dependent mechanism. Eur J Immunol. 19:1989;1331-1334.
    • (1989) Eur J Immunol , vol.19 , pp. 1331-1334
    • Forsyth, K.D.1    Simpson, A.C.2    Levinsky, R.3
  • 13
    • 0026604330 scopus 로고
    • Activation of human phagocytes through carbohydrate antigens [CD15, sialyl-CD15, CDw17, and CDw65]
    • Lund-Johansen F., Olweus J., Horejsi V., et al. Activation of human phagocytes through carbohydrate antigens [CD15, sialyl-CD15, CDw17, and CDw65]. J Immunol. 148:1992;3221-3229.
    • (1992) J Immunol , vol.148 , pp. 3221-3229
    • Lund-Johansen, F.1    Olweus, J.2    Horejsi, V.3
  • 14
  • 15
    • 0030661712 scopus 로고    scopus 로고
    • Engagement of P-selectin glycoprotein ligand-1 enhances tyrosine phosphorylation and activates mitogen-activated kinases in human neutrophils
    • Hidari K.I., Weyrich A.S., Zimmerman G.A. Engagement of P-selectin glycoprotein ligand-1 enhances tyrosine phosphorylation and activates mitogen-activated kinases in human neutrophils. J Biol Chem. 272:1997;28750-28756.
    • (1997) J Biol Chem , vol.272 , pp. 28750-28756
    • Hidari, K.I.1    Weyrich, A.S.2    Zimmerman, G.A.3
  • 16
    • 0032936518 scopus 로고    scopus 로고
    • Platelet/polymorphonuclear leukocyte interaction: P-selectin triggers protein-tyrosine phosphorylation-dependent CD11b/CD18 adhesion: Role of PSGL-1 as a signaling molecule
    • Evangelista V., Manarini S., Sideri R., et al. Platelet/ polymorphonuclear leukocyte interaction: P-selectin triggers protein-tyrosine phosphorylation-dependent CD11b/CD18 adhesion: Role of PSGL-1 as a signaling molecule. Blood. 93:1999;876-885.
    • (1999) Blood , vol.93 , pp. 876-885
    • Evangelista, V.1    Manarini, S.2    Sideri, R.3
  • 17
    • 0031066763 scopus 로고    scopus 로고
    • T cell adhesion to P-selectin induces tyrosine phosphorylation of pp125 focal adhesion kinase and other substrates
    • Haller H., Kunzendorf U., Sacherer K., Luft F.C. T cell adhesion to P-selectin induces tyrosine phosphorylation of pp125 focal adhesion kinase and other substrates. J Immunol. 158:1997;1061-1067.
    • (1997) J Immunol , vol.158 , pp. 1061-1067
    • Haller, H.1    Kunzendorf, U.2    Sacherer, K.3    Luft, F.C.4
  • 18
    • 0035316576 scopus 로고    scopus 로고
    • Cbl: Many adaptations to regulate protein tyrosine kinases
    • Thien C.B.F., Langdon W.Y. Cbl: Many adaptations to regulate protein tyrosine kinases. Nat Rev. 2:2001;294-305.
    • (2001) Nat Rev , vol.2 , pp. 294-305
    • Thien, C.B.F.1    Langdon, W.Y.2
  • 19
    • 0035264636 scopus 로고    scopus 로고
    • Sp1-p53 heterocomplex mediates activation of HTLV-I long terminal repeat by 12-O-tetradecanoylphorbol-13-acetate that is antagonized by protein kinase C
    • Torgeman A., Mor-Vaknin N., Zelin A., et al. Sp1-p53 heterocomplex mediates activation of HTLV-I long terminal repeat by 12-O-tetradecanoylphorbol- 13-acetate that is antagonized by protein kinase C. Virology. 281:2001;10-20.
    • (2001) Virology , vol.281 , pp. 10-20
    • Torgeman, A.1    Mor-Vaknin, N.2    Zelin, A.3
  • 20
    • 0025914034 scopus 로고
    • Metastatic behavior and cell surface properties of HT-29 human colon carcinoma variant cells selected for their differential expression of sialyl-dimeric Le X antigen
    • Matsushita Y., Hoff S.D., Nudelman E.D., et al. Metastatic behavior and cell surface properties of HT-29 human colon carcinoma variant cells selected for their differential expression of sialyl-dimeric Le X antigen. Clin Exp Metastasis. 9:1991;283-299.
    • (1991) Clin Exp Metastasis , vol.9 , pp. 283-299
    • Matsushita, Y.1    Hoff, S.D.2    Nudelman, E.D.3
  • 21
    • 0033600146 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of c-Cbl facilitates adhesion and spreading while suppressing anchorage-independent growth of v-Abl-transformed NIH3T3 fibroblasts
    • Feshenko E.A., Shore S.K., Tsygankov A.Y. Tyrosine phosphorylation of c-Cbl facilitates adhesion and spreading while suppressing anchorage- independent growth of v-Abl-transformed NIH3T3 fibroblasts. Oncogene. 18:1999;3703-3715.
    • (1999) Oncogene , vol.18 , pp. 3703-3715
    • Feshenko, E.A.1    Shore, S.K.2    Tsygankov, A.Y.3
  • 22
    • 0031034681 scopus 로고    scopus 로고
    • The proto-oncogene product p120 [cbl] links c-Src and phosphatidylinositol 3′-kinase to the integrin signaling pathway
    • Ojaniemi M., Martin S.S., Dolfi F., Olefsky J.M., Vuori K. The proto-oncogene product p120 [cbl] links c-Src and phosphatidylinositol 3′-kinase to the integrin signaling pathway. J Biol Chem. 272:1997;3780-3787.
    • (1997) J Biol Chem , vol.272 , pp. 3780-3787
    • Ojaniemi, M.1    Martin, S.S.2    Dolfi, F.3    Olefsky, J.M.4    Vuori, K.5
  • 23
    • 0033980846 scopus 로고    scopus 로고
    • C-Cbl localizes to actin lamellae and regulates lemellipodia formation and cell morphology
    • Scaife R.M., Langdon W.Y. c-Cbl localizes to actin lamellae and regulates lemellipodia formation and cell morphology. J Cell Sci. 113:2000;215-226.
    • (2000) J Cell Sci , vol.113 , pp. 215-226
    • Scaife, R.M.1    Langdon, W.Y.2
  • 24
    • 0037097835 scopus 로고    scopus 로고
    • Attachment of the PSGL-1 cytoplasmic domain to the actin cytoskeleton is essential for leukocyte rolling on P-selectin
    • Snapp K.R., Heitzig C.E., Kansas G.S. Attachment of the PSGL-1 cytoplasmic domain to the actin cytoskeleton is essential for leukocyte rolling on P-selectin. Blood. 99:2002;4494-4502.
    • (2002) Blood , vol.99 , pp. 4494-4502
    • Snapp, K.R.1    Heitzig, C.E.2    Kansas, G.S.3
  • 25
    • 0032904627 scopus 로고    scopus 로고
    • Mechanisms that regulate the function of the selectins and their ligands
    • Vestweber D., Blanks J.E. Mechanisms that regulate the function of the selectins and their ligands. Physiol Rev. 79:1999;181-213.
    • (1999) Physiol Rev , vol.79 , pp. 181-213
    • Vestweber, D.1    Blanks, J.E.2
  • 26
    • 0029758146 scopus 로고    scopus 로고
    • Neutrophil-neutrophil interactions under hydrodynamic shear stress involve L-selectin and PSGL-1. A mechanism that amplifies initial leukocyte accumulation of P-selectin in vitro
    • Walcheck B.K., Moore K.L., McEver R.P., Kishimoto T.K. Neutrophil-neutrophil interactions under hydrodynamic shear stress involve L-selectin and PSGL-1. A mechanism that amplifies initial leukocyte accumulation of P-selectin in vitro. J Clin Invest. 98:1996;1081-1087.
    • (1996) J Clin Invest , vol.98 , pp. 1081-1087
    • Walcheck, B.K.1    Moore, K.L.2    McEver, R.P.3    Kishimoto, T.K.4
  • 27
    • 0030988260 scopus 로고    scopus 로고
    • Adhesion of HT-29 colon carcinoma cells to E-selectin results in increased tyrosine phosphorylation and decreased activity of c-src
    • Soltesz S.A., Powers E.A., Geng J.G., Fisher C. Adhesion of HT-29 colon carcinoma cells to E-selectin results in increased tyrosine phosphorylation and decreased activity of c-src. Int J Cancer. 71:1997;645-653.
    • (1997) Int J Cancer , vol.71 , pp. 645-653
    • Soltesz, S.A.1    Powers, E.A.2    Geng, J.G.3    Fisher, C.4
  • 28
    • 0027315157 scopus 로고
    • Recent results on the biology of Hodgkin and Reed-Sternberg cells: II. Continuous cell lines
    • Drexler H.G. Recent results on the biology of Hodgkin and Reed-Sternberg cells II. Continuous cell lines. Leuk Lymphoma. 9:1993;1-25.
    • (1993) Leuk Lymphoma , vol.9 , pp. 1-25
    • Drexler, H.G.1
  • 29
    • 0029664864 scopus 로고    scopus 로고
    • P210BCR/ABL induces formation of complexes containing focal adhesion proteins and the protooncogene product p120 c-Cbl
    • Salgia R., Sattler M., Pisick E., Li J.L., Griffin J.D. p210BCR/ABL induces formation of complexes containing focal adhesion proteins and the protooncogene product p120 c-Cbl. Exp Hematol. 24:1996;310-313.
    • (1996) Exp Hematol , vol.24 , pp. 310-313
    • Salgia, R.1    Sattler, M.2    Pisick, E.3    Li, J.L.4    Griffin, J.D.5
  • 30
    • 18544371851 scopus 로고    scopus 로고
    • Differential association of CD45 isoforms with CD4 and CD8 regulates the actions of specific pools of p56lck tyrosine kinase in T cell antigen receptor signal transduction
    • Dornan S., Sebestyen Z., Gamble J., et al. Differential association of CD45 isoforms with CD4 and CD8 regulates the actions of specific pools of p56lck tyrosine kinase in T cell antigen receptor signal transduction. J Biol Chem. 277:2002;1912-1918.
    • (2002) J Biol Chem , vol.277 , pp. 1912-1918
    • Dornan, S.1    Sebestyen, Z.2    Gamble, J.3
  • 31
    • 0032936145 scopus 로고    scopus 로고
    • The multisubstrate docking site of the MET receptor is indispensable for MET-mediated RAS signaling and cell scattering
    • Tulasne D., Paumelle R., Weidner K.M., Vandenbunder B., Fafeur V. The multisubstrate docking site of the MET receptor is indispensable for MET-mediated RAS signaling and cell scattering. Mol Biol Cell. 10:1999;551-565.
    • (1999) Mol Biol Cell , vol.10 , pp. 551-565
    • Tulasne, D.1    Paumelle, R.2    Weidner, K.M.3    Vandenbunder, B.4    Fafeur, V.5
  • 32
  • 33
    • 0035865510 scopus 로고    scopus 로고
    • Expression of the c-met proto-oncogene and its ligand, hepatocyte growth factor, in Hodgkin disease
    • Teofili L., Di Febo A.L., Pierconti F., et al. Expression of the c-met proto-oncogene and its ligand, hepatocyte growth factor, in Hodgkin disease. Blood. 97:2001;1063-1069.
    • (2001) Blood , vol.97 , pp. 1063-1069
    • Teofili, L.1    Di Febo, A.L.2    Pierconti, F.3
  • 34
    • 0035971493 scopus 로고    scopus 로고
    • AP-1 in cell proliferation and survival
    • Shaulian E., Karin M. AP-1 in cell proliferation and survival. Oncogene. 20:2001;2390-2400.
    • (2001) Oncogene , vol.20 , pp. 2390-2400
    • Shaulian, E.1    Karin, M.2
  • 35
    • 18444369000 scopus 로고    scopus 로고
    • Aberrantly expressed c-Jun and JunB are a hallmark of Hodgkin lymphoma cells, stimulate proliferation and synergize with NF-κB
    • Mathas S., Hinz M., Anagnostopulos I., et al. Aberrantly expressed c-Jun and JunB are a hallmark of Hodgkin lymphoma cells, stimulate proliferation and synergize with NF-κB. EMBO J. 21:2002;4104-4113.
    • (2002) EMBO J , vol.21 , pp. 4104-4113
    • Mathas, S.1    Hinz, M.2    Anagnostopulos, I.3
  • 36
    • 0026599664 scopus 로고
    • Correlation of c-fos/c-jun expression with histiocytic differentiation in Hodgkin's Reed-Sternberg cells. Examination in HDLM-1 subclones with spontaneous differentiation
    • Hsu S.M., Xie S.S., el-Okda M.O., Hsu P.L. Correlation of c-fos/c-jun expression with histiocytic differentiation in Hodgkin's Reed-Sternberg cells. Examination in HDLM-1 subclones with spontaneous differentiation. Am J Pathol. 140:1992;155-165.
    • (1992) Am J Pathol , vol.140 , pp. 155-165
    • Hsu, S.M.1    Xie, S.S.2    El-Okda, M.O.3    Hsu, P.L.4
  • 37
    • 0034648016 scopus 로고    scopus 로고
    • Density-dependent induction of TNF-α release from human monocytes by immobilized P-selectin
    • Koike J., Nagata K., Kudo S., Tsuji T., Irimura T. Density-dependent induction of TNF-α release from human monocytes by immobilized P-selectin. FEBS Lett. 477:2000;84-88.
    • (2000) FEBS Lett , vol.477 , pp. 84-88
    • Koike, J.1    Nagata, K.2    Kudo, S.3    Tsuji, T.4    Irimura, T.5
  • 38
    • 0032481142 scopus 로고    scopus 로고
    • Identification of a novel integrin signaling pathway involving the kinase Syk and the guanine nucleotide exchange factor Vav 1
    • Miranti C.K., Leng L., Mashberger P., Brugge J.S., Shattil S.J. Identification of a novel integrin signaling pathway involving the kinase Syk and the guanine nucleotide exchange factor Vav 1. Curr Biol. 8:1998;1289-1299.
    • (1998) Curr Biol , vol.8 , pp. 1289-1299
    • Miranti, C.K.1    Leng, L.2    Mashberger, P.3    Brugge, J.S.4    Shattil, S.J.5
  • 39
    • 0030712944 scopus 로고    scopus 로고
    • Cbl-mediated regulation of T cell receptor-mediated regulation of T cell receptor-induced AP-1 activation
    • Rellahan B.L., Graham L.J., Stocia B., DeBell K.E., Bonvivi E. Cbl-mediated regulation of T cell receptor-mediated regulation of T cell receptor-induced AP-1 activation. J Biol Chem. 272:1997;30806-30811.
    • (1997) J Biol Chem , vol.272 , pp. 30806-30811
    • Rellahan, B.L.1    Graham, L.J.2    Stocia, B.3    DeBell, K.E.4    Bonvivi, E.5


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