메뉴 건너뛰기




Volumn 203, Issue 4, 2001, Pages 659-669

Engagement of CD147 molecule-induced cell aggregation through the activation of protein kinases and reorganization of the cytoskeleton

Author keywords

[No Author keywords available]

Indexed keywords

CD147 ANTIGEN; CYTOCHALASIN B; GENISTEIN; HERBIMYCIN A; MEMBRANE PROTEIN; MONOCLONAL ANTIBODY; PROTEIN KINASE C; PROTEIN KINASE C INHIBITOR; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE KINASE INHIBITOR; SPHINGOSINE; UNCLASSIFIED DRUG;

EID: 0035005551     PISSN: 01712985     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0171-2985(01)80015-2     Document Type: Article
Times cited : (24)

References (38)
  • 2
    • 0032910855 scopus 로고    scopus 로고
    • T cell activation-associated epitopes of CD147 in regulation of the T cell response, and their definition by antibody affinity and antigen density
    • KOCH, C., G. STAFFLER, R. HUTTINGER, I. HILGERT, E. PRAGER, J. GERNY, P. STEINLEIN, O. MAJDC, V. HOREJSI, and H. STOCKINGER. 1999. T cell activation-associated epitopes of CD147 in regulation of the T cell response, and their definition by antibody affinity and antigen density. Int. Immunol. 11: 777.
    • (1999) Int. Immunol. , vol.11 , pp. 777
    • Koch, C.1    Staffler, G.2    Huttinger, R.3    Hilgert, I.4    Prager, E.5    Gerny, J.6    Steinlein, P.7    Majdc, O.8    Horejsi, V.9    Stockinger, H.10
  • 3
    • 0026659128 scopus 로고
    • Human leukocyte activation antigen M6, a member of the ig superfamily, is the species homologue of rat OX-47, mouse basigin, and chicken HT7 molecule
    • KASINRERK, W., E. FIEBINGER, I. STEFANOVA, T. BAUMRUKER, W. KNAPP, and H. STOCKINGER. 1992. Human leukocyte activation antigen M6, a member of the Ig superfamily, is the species homologue of rat OX-47, mouse basigin, and chicken HT7 molecule. J. Immunol. 149: 847.
    • (1992) J. Immunol. , vol.149 , pp. 847
    • Kasinrerk, W.1    Fiebinger, E.2    Stefanova, I.3    Baumruker, T.4    Knapp, W.5    Stockinger, H.6
  • 4
    • 0028795147 scopus 로고
    • The human cell-derived collagenase stimulatory factor (renamed EMMPRIN) is a member of the immunoglobuhn superfamily
    • BISWAS, C., Y. ZHANG, R. DECASTRO, H. GUO, T. NAKAMURA, H. KATAOKA, and K. KAHESHIMA. 1995. The human cell-derived collagenase stimulatory factor (renamed EMMPRIN) is a member of the immunoglobuhn superfamily. Cancer Res. 55: 434.
    • (1995) Cancer Res. , vol.55 , pp. 434
    • Biswas, C.1    Zhang, Y.2    Decastro, R.3    Guo, H.4    Nakamura, T.5    Kataoka, H.6    Kaheshima, K.7
  • 5
    • 0025718981 scopus 로고
    • The basigin group of the immunoglobulin superfamily: Complete conservation of a segment in and around transmembrane domains of human and mouse basigin and chicken HT7 antigen
    • MIYAUCHI, T., Y. MASUZAWA, and T. MURAMATSU. 1991. The basigin group of the immunoglobulin superfamily: complete conservation of a segment in and around transmembrane domains of human and mouse basigin and chicken HT7 antigen. J. Riochem. 110: 770.
    • (1991) J. Riochem. , vol.110 , pp. 770
    • Miyauchi, T.1    Masuzawa, Y.2    Muramatsu, T.3
  • 6
    • 0032956758 scopus 로고    scopus 로고
    • CD147 monoclonal antibodies induce homotypic cell aggregation of monocytic cell line U937 via LFA-1/ICAM-1 pathway
    • KASINRERK, W., N. TOKRASINWIK, P. PHUNPAE. 1999. CD147 monoclonal antibodies induce homotypic cell aggregation of monocytic cell line U937 via LFA-1/ICAM-1 pathway. Immunology 96: 184.
    • (1999) Immunology , vol.96 , pp. 184
    • Kasinrerk, W.1    Tokrasinwik, N.2    Phunpae, P.3
  • 7
    • 0031036521 scopus 로고    scopus 로고
    • Stimulation of matrix metalloproteinase production by recombinant extracellular matrix metalloproteinase inducer from transfected Chinese hamster ovary cells
    • GUO, H., S. ZUCKER, M. K. GORDON, B. P. TOOLE, and C. BISWAS. 1997. Stimulation of matrix metalloproteinase production by recombinant extracellular matrix metalloproteinase inducer from transfected Chinese hamster ovary cells. J. Biol. Chem. 272: 24.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24
    • Guo, H.1    Zucker, S.2    Gordon, M.K.3    Toole, B.P.4    Biswas, C.5
  • 8
    • 0343768912 scopus 로고    scopus 로고
    • CD 147 workshop: Expression, modulation, and involvement in homotypic aggregation and adhesion to matrix of molecules recognized by monoclonal antibodies to CD147 on breast cancer cell lines
    • T. KISHIMOTO, H. KIKUKANI, A. E. G. KR V. D. BORNE, et al., eds. Garland Publishing, New York, 764 pp.
    • SCHIAVONE, E. M., V. TORTORA, I. ARMETTA, P. BONTIEMPO, M. R. MOSTI, L. PEZONE, E. NOLA, G. A. PUCA, C. VACCA, and A. M. MOLINARI. 1997. CD 147 workshop: expression, modulation, and involvement in homotypic aggregation and adhesion to matrix of molecules recognized by monoclonal antibodies to CD147 on breast cancer cell lines. In: Leukocyte typing VI. T. KISHIMOTO, H. KIKUKANI, A. E. G. KR V. D. BORNE, et al., eds. Garland Publishing, New York, 764 pp.
    • (1997) Leukocyte Typing VI
    • Schiavone, E.M.1    Tortora, V.2    Armetta, I.3    Bontiempo, P.4    Mosti, M.R.5    Pezone, L.6    Nola, E.7    Puca, G.A.8    Vacca, C.9    Molinari, A.M.10
  • 11
    • 0000358981 scopus 로고
    • Storing and purifying antibodies
    • E. HARIOW, and D. LANE, eds. Cold Spring Harbor Laboratory, New York, 283 pp.
    • HARLOW, E., and D. LANE. 1988. Storing and purifying antibodies. In: Antibodies: a Laboratory Manual. E. HARIOW, and D. LANE, eds. Cold Spring Harbor Laboratory, New York, 283 pp.
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 12
    • 0030907287 scopus 로고    scopus 로고
    • A novel human monoclonal antibody rapidly induces homotypic cell aggregation and promotes antibody-secreting activity by human B lymphoblastoid cell line IM-9
    • IKEWAKI, N. 1997. A novel human monoclonal antibody rapidly induces homotypic cell aggregation and promotes antibody-secreting activity by human B lymphoblastoid cell line IM-9. J. Clin. Immunol. 17: 127.
    • (1997) J. Clin. Immunol. , vol.17 , pp. 127
    • Ikewaki, N.1
  • 13
    • 0030865394 scopus 로고    scopus 로고
    • Integrins and inside-out signal transduction: Converging signals from PKC and PIP3
    • KOLANUS, W., and B. SEEDS. 1997. Integrins and inside-out signal transduction: converging signals from PKC and PIP3. Curr. Opin. Cell Biol. 9: 725.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 725
    • Kolanus, W.1    Seeds, B.2
  • 14
    • 0032481269 scopus 로고    scopus 로고
    • Signal transduction via CD43 (Leukosialin, Sialophorin) and associated biological effects in a human mast cell line (HMC-1)
    • BABINA, M., S. WEBER, K. MAMMERI, and B. M. HENZ. 1998. Signal transduction via CD43 (Leukosialin, Sialophorin) and associated biological effects in a human mast cell line (HMC-1). Biochem. Biophysic. Res. Com. 243: 163.
    • (1998) Biochem. Biophysic. Res. Com. , vol.243 , pp. 163
    • Babina, M.1    Weber, S.2    Mammeri, K.3    Henz, B.M.4
  • 15
    • 0033959765 scopus 로고    scopus 로고
    • CD99 monoclonal antibody induces homotypic cell aggregation of Jurkat cells through protein ryrosine kinase and protein kinase C-dependent pathways
    • KASINRERK, W., N. TOKRASINWIT, S. MOONSOM, and H. STOCKINGER. 2000. CD99 monoclonal antibody induces homotypic cell aggregation of Jurkat cells through protein ryrosine kinase and protein kinase C-dependent pathways. Immunol. Letters 71: 33.
    • (2000) Immunol. Letters , vol.71 , pp. 33
    • Kasinrerk, W.1    Tokrasinwit, N.2    Moonsom, S.3    Stockinger, H.4
  • 16
    • 0025157997 scopus 로고
    • Engagement of the monocyte surface antigen CD14 induces lymphocyte function-associated antigen 1/intercellular adhesion molecule-1 dependent homotypic adhesion
    • LAUENER, R. P., R. S. GEHA, and D. VERCELLI. 1990. Engagement of the monocyte surface antigen CD14 induces lymphocyte function-associated antigen 1/intercellular adhesion molecule-1 dependent homotypic adhesion. J. Immunol. 145: 1390.
    • (1990) J. Immunol. , vol.145 , pp. 1390
    • Lauener, R.P.1    Geha, R.S.2    Vercelli, D.3
  • 17
    • 0025083811 scopus 로고
    • Engagement of major histocompatibility complex class II molecules induces sustained lymphocyte function associated molecule-1 dependent cell adhesion
    • MOURAD, W., R. S. GEHA, and T. CHATILA. 1990. Engagement of major histocompatibility complex class II molecules induces sustained lymphocyte function associated molecule-1 dependent cell adhesion. J. Exp. Med. 172: 1513.
    • (1990) J. Exp. Med. , vol.172 , pp. 1513
    • Mourad, W.1    Geha, R.S.2    Chatila, T.3
  • 18
    • 0025735031 scopus 로고
    • Stimulation of B lymphocytes through surface Ig receptors induces LFA-1 and ICAM-1 dependent adhesion
    • DANG, L. H., and K. L. ROCK. 1991. Stimulation of B lymphocytes through surface Ig receptors induces LFA-1 and ICAM-1 dependent adhesion. J. Immunol. 146: 3273.
    • (1991) J. Immunol. , vol.146 , pp. 3273
    • Dang, L.H.1    Rock, K.L.2
  • 19
    • 0026343687 scopus 로고
    • Transmembrane signals generated through MHC class II, CD19, CD20, CD39, and CD40 antigens induce LFA1-dependent and independent adhesion in human B cells through a tyrosine kinase-dependent and in-dependent pathway
    • KANSAS, G. S., and T. F. TEDDER. 1991. Transmembrane signals generated through MHC class II, CD19, CD20, CD39, and CD40 antigens induce LFA1-dependent and independent adhesion in human B cells through a tyrosine kinase-dependent and in-dependent pathway. J. Immunol. 147: 4094.
    • (1991) J. Immunol. , vol.147 , pp. 4094
    • Kansas, G.S.1    Tedder, T.F.2
  • 21
    • 0027419878 scopus 로고
    • CD45 mAb induces cell adhesion in peripheral blood mononuclear cells via lymphocyte function-associated antigen-1 (LEA-1) and intracellular cell adhesion molecule (ICAM-1)
    • LORENZ, H. M., T. HARRER, A. S. LAGOO, A. BAUR, G. EGER, and J. R. KALDEN, 1993. CD45 mAb induces cell adhesion in peripheral blood mononuclear cells via lymphocyte function-associated antigen-1 (LEA-1) and intracellular cell adhesion molecule (ICAM-1). Cell Immunol. 147: 110.
    • (1993) Cell Immunol. , vol.147 , pp. 110
    • Lorenz, H.M.1    Harrer, T.2    Lagoo, A.S.3    Baur, A.4    Eger, G.5    Kalden, J.R.6
  • 23
    • 0022974603 scopus 로고
    • Sphingosine inhibition of protein kinase C activity and of phobol diburyrate binding in vitro and in human platelets
    • HANNUN, Y. A., C. A. LOOMIS, A. H. MERRIEL, and R. M. BELL. 1986. Sphingosine inhibition of protein kinase C activity and of phobol diburyrate binding in vitro and in human platelets. J. Biol. Chem. 261: 12604.
    • (1986) J. Biol. Chem. , vol.261 , pp. 12604
    • Hannun, Y.A.1    Loomis, C.A.2    Merriel, A.H.3    Bell, R.M.4
  • 24
    • 0024541436 scopus 로고
    • Functions of sphingolipids and sphingolipid breakdown products in cellular regulation
    • HANNUN, Y. A., and R. M. BELL. 1989. Functions of sphingolipids and sphingolipid breakdown products in cellular regulation. Science 243: 500.
    • (1989) Science , vol.243 , pp. 500
    • Hannun, Y.A.1    Bell, R.M.2
  • 26
    • 0022967572 scopus 로고
    • Phenotypic change from transformed to normal induced by benzoquinonoid ansamycins inactivation of p60src in rat kidney cells infected with Ro sarcomar virus
    • UEHARA, Y., M. HORI, T. TAKEUCHI, and H. UMEZAWA. 1986. Phenotypic change from transformed to normal induced by benzoquinonoid ansamycins inactivation of p60src in rat kidney cells infected with Ro sarcomar virus. Mol. Cell Biol. 6: 2198.
    • (1986) Mol. Cell Biol. , vol.6 , pp. 2198
    • Uehara, Y.1    Hori, M.2    Takeuchi, T.3    Umezawa, H.4
  • 27
    • 0025947138 scopus 로고
    • Use and selectively of herbimycin a as inhibitor of protein-tyrosine kinases
    • UEHARA, Y, and H. FUKAZAWA. 1991. Use and selectively of herbimycin A as inhibitor of protein-tyrosine kinases. Methods Enzymol. 201: 370.
    • (1991) Methods Enzymol. , vol.201 , pp. 370
    • Uehara, Y.1    Fukazawa, H.2
  • 29
    • 0026075305 scopus 로고
    • Use and specificity of genistein as inhibitor of protein tyrosine kinases
    • AKIYAMA, T., and H. OGAWARA. 1991. Use and specificity of genistein as inhibitor of protein tyrosine kinases. Method Enzymol. 201: 362.
    • (1991) Method Enzymol. , vol.201 , pp. 362
    • Akiyama, T.1    Ogawara, H.2
  • 31
    • 0026526512 scopus 로고
    • The protein tyrosine kinase inhibitor herbimycin a, but not genistein, specifically inhibits signal transduction by the T cell antigen receptor
    • GRABER, M., C. H. JUNE, L. E. SAMELSON, and A. WEISS. 1992. The protein tyrosine kinase inhibitor herbimycin A, but not genistein, specifically inhibits signal transduction by the T cell antigen receptor. Int. Immunol. 4: 1201.
    • (1992) Int. Immunol. , vol.4 , pp. 1201
    • Graber, M.1    June, C.H.2    Samelson, L.E.3    Weiss, A.4
  • 32
    • 0027427616 scopus 로고
    • Genistein exhibits preferential cytotoxicity to a leukemogenic variant but induces differentiation of a non-leukemogenic variant of the mouse monocytic leukemia Mm cell line
    • KANATANI, Y., T. KASUKABE, M. HOZUMI, K. MOTOYOSHI, N. NAGATA, and Y. HONMA. 1993. Genistein exhibits preferential cytotoxicity to a leukemogenic variant but induces differentiation of a non-leukemogenic variant of the mouse monocytic leukemia Mm cell line. Leuk. Res. 17: 847.
    • (1993) Leuk. Res. , vol.17 , pp. 847
    • Kanatani, Y.1    Kasukabe, T.2    Hozumi, M.3    Motoyoshi, K.4    Nagata, N.5    Honma, Y.6
  • 33
    • 0033582247 scopus 로고    scopus 로고
    • Activation of Cl-channel and Na+/K+2Cl-cotransporter in renal epithelial A6 cells by flavonoids: Genistein, daidzein, and apigenin
    • NISSATO, N., Y. ITO, and Y. MARUNAKA. 1999. Activation of Cl-channel and Na+/K+2Cl-cotransporter in renal epithelial A6 cells by flavonoids: genistein, daidzein, and apigenin. Biochem. Biophys. Res. Commun. 254: 368.
    • (1999) Biochem. Biophys. Res. Commun. , vol.254 , pp. 368
    • Nissato, N.1    Ito, Y.2    Marunaka, Y.3
  • 34
    • 0026764121 scopus 로고
    • Genistein inhibits protein histidine kinase
    • HUANG, J., M. NASR, Y. KIM, and H. R. MATTHEWS. 1992. Genistein inhibits protein histidine kinase. J. Biol. Chem. 267: 15511.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15511
    • Huang, J.1    Nasr, M.2    Kim, Y.3    Matthews, H.R.4
  • 35
    • 0026742965 scopus 로고
    • Genistein differentially inhibits postreceptor effects of insulin in rat adipoCytes without inhibiting the insulin receptor kinase
    • ABLER, A., J. A. SMITH, P. A. RANDAZZO, P. L. ROTHENBERG, and L. JARETT. 1992. Genistein differentially inhibits postreceptor effects of insulin in rat adipoCytes without inhibiting the insulin receptor kinase. J. Biol. Chem. 267: 3946.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3946
    • Abler, A.1    Smith, J.A.2    Randazzo, P.A.3    Rothenberg, P.L.4    Jarett, L.5
  • 36
    • 0024150623 scopus 로고
    • Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton
    • BURRIDGE, K., K. FATH, T. KELLY, B. NUCKOLIS, and C. TURNKR. 1988. Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu. Rev. Cell Biol. 4: 487.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 487
    • Burridge, K.1    Fath, K.2    Kelly, T.3    Nuckolis, B.4    Turnkr, C.5
  • 38
    • 0034637522 scopus 로고    scopus 로고
    • Integrin modulation by lateral association
    • WOODS, A., and J. R. COUCHMAN. 2000. Integrin Modulation by lateral association. J. Biol. Chem. 276: 24233.
    • (2000) J. Biol. Chem. , vol.276 , pp. 24233
    • Woods, A.1    Couchman, J.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.