메뉴 건너뛰기




Volumn 29, Issue 1, 1998, Pages 369-379

Entry of OpaA+ gonococci into HEp-2 cells requires concerted action of glycosaminoglycans, fibronectin and integrin receptors

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; AMINO ACID; ANTIBODY; ARGINYLGLYCYLASPARTIC ACID; CELL SURFACE RECEPTOR; FIBRONECTIN; FIBRONECTIN RECEPTOR; GLYCOSAMINOGLYCAN; HEPARIN LYASE; INTEGRIN; PROTEOHEPARAN SULFATE;

EID: 0031871416     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1998.00951.x     Document Type: Article
Times cited : (126)

References (61)
  • 2
    • 0031011324 scopus 로고    scopus 로고
    • Differential recognition of members of the carcinoembryonic antigen family by Opa variants of Neisseria gonorrhoeae
    • Bos, M.P., Grunert, F., and Belland, R.J. (1997) Differential recognition of members of the carcinoembryonic antigen family by Opa variants of Neisseria gonorrhoeae. Infect Immun 65: 2353-2361.
    • (1997) Infect Immun , vol.65 , pp. 2353-2361
    • Bos, M.P.1    Grunert, F.2    Belland, R.J.3
  • 3
    • 0026773553 scopus 로고
    • Multiple binding sites in fibronectin and the staphylococcal fibronectin receptor
    • Bozzini, S., Visai, L., Pignatti, P., Petersen, T.E., and Speziale, P. (1992) Multiple binding sites in fibronectin and the staphylococcal fibronectin receptor. Eur J Biochem 207: 327-333.
    • (1992) Eur J Biochem , vol.207 , pp. 327-333
    • Bozzini, S.1    Visai, L.2    Pignatti, P.3    Petersen, T.E.4    Speziale, P.5
  • 4
    • 0030660196 scopus 로고    scopus 로고
    • Syndecans: Multifunctional cell surface co-receptors
    • Carey, D.J. (1997) Syndecans: multifunctional cell surface co-receptors. Biochem J 327: 1-16.
    • (1997) Biochem J , vol.327 , pp. 1-16
    • Carey, D.J.1
  • 5
    • 0025248510 scopus 로고
    • The role of integrins alpha 2 beta 1 and alpha 3 beta 1 in cell-cell and cell-substrate adhesion of human epidermal cells
    • Carter, W.G., Wayner, E.A., Bouchard, T.S., and Kaur, P. (1990) The role of integrins alpha 2 beta 1 and alpha 3 beta 1 in cell-cell and cell-substrate adhesion of human epidermal cells. J Cell Biol 110: 1387-1404.
    • (1990) J Cell Biol , vol.110 , pp. 1387-1404
    • Carter, W.G.1    Wayner, E.A.2    Bouchard, T.S.3    Kaur, P.4
  • 6
    • 0028982474 scopus 로고
    • Adherence of pilus-Opa+ gonococci to epithelial cells in vitro involves heparan sulfate
    • Chen, T., Belland, R.J., Wilson, J., and Swanson, J. (1995) Adherence of pilus-Opa+ gonococci to epithelial cells in vitro involves heparan sulfate. J Exp Med 182: 511-517.
    • (1995) J Exp Med , vol.182 , pp. 511-517
    • Chen, T.1    Belland, R.J.2    Wilson, J.3    Swanson, J.4
  • 7
    • 0030924679 scopus 로고    scopus 로고
    • Several carcinoembryonic antigens (CD66) serve as receptors for gonococcal opacity proteins
    • Chen, T., Grunert, F., Medina-Marino, A., and Gotschlich, E.C. (1997) Several carcinoembryonic antigens (CD66) serve as receptors for gonococcal opacity proteins. J Exp Med 185: 1557-1564.
    • (1997) J Exp Med , vol.185 , pp. 1557-1564
    • Chen, T.1    Grunert, F.2    Medina-Marino, A.3    Gotschlich, E.C.4
  • 8
    • 0003027506 scopus 로고
    • Structure and biology of pericellular proteoglycans
    • Roberts, D.D., and Mecham, R.P. (eds). New York: Academic Press
    • Couchman, J.R., and Woods, A. (1993) Structure and biology of pericellular proteoglycans. In Cell Surface and Extracellular Conjugates. Roberts, D.D., and Mecham, R.P. (eds). New York: Academic Press, pp. 33-82.
    • (1993) Cell Surface and Extracellular Conjugates , pp. 33-82
    • Couchman, J.R.1    Woods, A.2
  • 9
    • 0029953925 scopus 로고    scopus 로고
    • Syndecans, signaling, and cell adhesion
    • Couchman, J.R., and Woods, A. (1996) Syndecans, signaling, and cell adhesion. J Cell Biochem 61: 578-584.
    • (1996) J Cell Biochem , vol.61 , pp. 578-584
    • Couchman, J.R.1    Woods, A.2
  • 10
    • 0030908268 scopus 로고    scopus 로고
    • High-frequency invasion of epithelial cells by Streptococcus pyogenes can be activated by fibrinogen and peptides containing the sequence RGD
    • Cue, D.R., and Cleary, P.P. (1997) High-frequency invasion of epithelial cells by Streptococcus pyogenes can be activated by fibrinogen and peptides containing the sequence RGD. Infect Immun 65: 2759-2764.
    • (1997) Infect Immun , vol.65 , pp. 2759-2764
    • Cue, D.R.1    Cleary, P.P.2
  • 11
    • 0032489349 scopus 로고    scopus 로고
    • Vitronectin-dependent invasion of epithelial cells by Neisseria gonorrhoeae involves alpha (V) integrin receptors
    • Dehio, M., Gomez-Duarte, O.G., Dehio, C., and Meyer, T.F. (1998) Vitronectin-dependent invasion of epithelial cells by Neisseria gonorrhoeae involves alpha (V) integrin receptors. FEBS Lett 424: 84-88.
    • (1998) FEBS Lett , vol.424 , pp. 84-88
    • Dehio, M.1    Gomez-Duarte, O.G.2    Dehio, C.3    Meyer, T.F.4
  • 12
    • 0031029922 scopus 로고    scopus 로고
    • Vitronectin mediates internalization of Neisseria gonorrhoeae by Chinese hamster ovary cells
    • Duensing, T.D., and van Putten, J.P.M. (1997) Vitronectin mediates internalization of Neisseria gonorrhoeae by Chinese hamster ovary cells. Infect Immun 65: 964-970.
    • (1997) Infect Immun , vol.65 , pp. 964-970
    • Duensing, T.D.1    Van Putten, J.P.M.2
  • 13
    • 0025036846 scopus 로고
    • Binding of human syndecan to extracellular matrix proteins
    • Elenius, K., Salmivirta, M., Inki, P., Mali, M., and Jalkanen, M. (1990) Binding of human syndecan to extracellular matrix proteins. J Biol Chem 265: 17837-17843.
    • (1990) J Biol Chem , vol.265 , pp. 17837-17843
    • Elenius, K.1    Salmivirta, M.2    Inki, P.3    Mali, M.4    Jalkanen, M.5
  • 14
    • 0028062142 scopus 로고
    • Function of the syndecans - A family of cell surface proteoglycans
    • Elenius, K., and Jalkanen, M. (1994) Function of the syndecans - a family of cell surface proteoglycans. J Cell Sci 107: 2975-2982.
    • (1994) J Cell Sci , vol.107 , pp. 2975-2982
    • Elenius, K.1    Jalkanen, M.2
  • 15
    • 0023880425 scopus 로고
    • Adhesion of enterotoxigenic (ETEC) and bovine mastitis Escherichia coli strains to rat embryonic fibroblasts: Role of amino-terminal domain of fibronectin in bacterial adhesion
    • Faris, A., Fröman, G., Switalski, L., and Höök, M. (1988) Adhesion of enterotoxigenic (ETEC) and bovine mastitis Escherichia coli strains to rat embryonic fibroblasts: role of amino-terminal domain of fibronectin in bacterial adhesion. Microbiol Immunol 32: 1-13.
    • (1988) Microbiol Immunol , vol.32 , pp. 1-13
    • Faris, A.1    Fröman, G.2    Switalski, L.3    Höök, M.4
  • 17
    • 0020512741 scopus 로고
    • Biochemical and immunological characterization of three binding sites on human plasma fibronectin with different affinities for heparin
    • Gold, L.I., Frangione, B., and Pearlstein, E. (1983) Biochemical and immunological characterization of three binding sites on human plasma fibronectin with different affinities for heparin. Biochemistry 22: 4113-4119.
    • (1983) Biochemistry , vol.22 , pp. 4113-4119
    • Gold, L.I.1    Frangione, B.2    Pearlstein, E.3
  • 18
    • 1842299317 scopus 로고    scopus 로고
    • Binding of vitronectin to Opa-expressing Neisseria gonorrhoeae mediates invasion of HeLa cells
    • Gomez-Duarte, O.G., Dehio, M., Guzman, C.A., Chhatwal, G.S., Dehio, C., and Meyer, T.F. (1997) Binding of vitronectin to Opa-expressing Neisseria gonorrhoeae mediates invasion of HeLa cells. Infect Immun 65: 3857-3866.
    • (1997) Infect Immun , vol.65 , pp. 3857-3866
    • Gomez-Duarte, O.G.1    Dehio, M.2    Guzman, C.A.3    Chhatwal, G.S.4    Dehio, C.5    Meyer, T.F.6
  • 19
    • 0030965374 scopus 로고    scopus 로고
    • CD66 carcinoembryonic antigens mediate interactions between Opa-expressing Neisseria gonorrhoeae and human polymorphonuclear phagocytes
    • Gray-Owen, S.D., Dehio, C., Haude, A., Grunert, P., and Meyer, T.F. (1997) CD66 carcinoembryonic antigens mediate interactions between Opa-expressing Neisseria gonorrhoeae and human polymorphonuclear phagocytes. EMBO J 16: 3435-3445.
    • (1997) EMBO J , vol.16 , pp. 3435-3445
    • Gray-Owen, S.D.1    Dehio, C.2    Haude, A.3    Grunert, P.4    Meyer, T.F.5
  • 20
    • 0004043397 scopus 로고
    • New York: Springer -Verlag
    • Hynes, R.O. (1990) Fibronectins. New York: Springer -Verlag.
    • (1990) Fibronectins
    • Hynes, R.O.1
  • 21
    • 0023667057 scopus 로고
    • Identification of invasin: A protein that allows enteric bacteria to penetrate cultured mammalian cells
    • Isberg, R.R., Voorhis, D.L., and Falkow, S. (1987) Identification of invasin: a protein that allows enteric bacteria to penetrate cultured mammalian cells. Cell 50: 6682-6686.
    • (1987) Cell , vol.50 , pp. 6682-6686
    • Isberg, R.R.1    Voorhis, D.L.2    Falkow, S.3
  • 22
    • 0028177278 scopus 로고
    • Fibronectin receptors from Gram-positive bacteria: Comparison of active sites
    • Joh, H.J., House-Pompeo, K., Patti, J.L., Gurusiddappa, S., and Höök, M. (1994) Fibronectin receptors from Gram-positive bacteria: comparison of active sites. Biochemistry 33: 6086-6092.
    • (1994) Biochemistry , vol.33 , pp. 6086-6092
    • Joh, H.J.1    House-Pompeo, K.2    Patti, J.L.3    Gurusiddappa, S.4    Höök, M.5
  • 23
    • 0026334144 scopus 로고
    • Two different genes encode fibronectin binding proteins in Staphylococcus aureus. The complete nucleotide sequence and characterization of the second gene
    • Jonsson, K., Signas, C., Muller, H.P., and Lindberg, M. (1991) Two different genes encode fibronectin binding proteins in Staphylococcus aureus. The complete nucleotide sequence and characterization of the second gene. Eur J Biochem 202: 1041-1048.
    • (1991) Eur J Biochem , vol.202 , pp. 1041-1048
    • Jonsson, K.1    Signas, C.2    Muller, H.P.3    Lindberg, M.4
  • 24
    • 0027398024 scopus 로고
    • Variable opacity (Opa) outer membrane proteins account for the cell displayed by Neisseria gonorrhoeae for human leukocytes and epithelial cells
    • Kupsch, E.M., Knepper, B., Kuroki, T., Heuer, I., and Meyer, T.F. (1993) Variable opacity (Opa) outer membrane proteins account for the cell displayed by Neisseria gonorrhoeae for human leukocytes and epithelial cells. EMBO J 12: 641-650.
    • (1993) EMBO J , vol.12 , pp. 641-650
    • Kupsch, E.M.1    Knepper, B.2    Kuroki, T.3    Heuer, I.4    Meyer, T.F.5
  • 25
    • 0027534280 scopus 로고
    • Characterization of the internalization of Bacillus Calmette-Guerin by human bladder tumor cells
    • Kuroda, K., Brown, E.J., Telle, W.B., Russell, D.G., and Ratliff, T.L. (1993) Characterization of the internalization of Bacillus Calmette-Guerin by human bladder tumor cells. J Clin Invest 91: 69-76.
    • (1993) J Clin Invest , vol.91 , pp. 69-76
    • Kuroda, K.1    Brown, E.J.2    Telle, W.B.3    Russell, D.G.4    Ratliff, T.L.5
  • 26
    • 0021271656 scopus 로고
    • Binding sites for streptococci and staphylococci in fibronectin
    • Kuusela, P., Vartio, T., Vuento, M., and Myhre, E.B. (1984) Binding sites for streptococci and staphylococci in fibronectin. Infect Immun 45: 433-436.
    • (1984) Infect Immun , vol.45 , pp. 433-436
    • Kuusela, P.1    Vartio, T.2    Vuento, M.3    Myhre, E.B.4
  • 27
    • 0025301659 scopus 로고
    • Identification of the integrin binding domain of the Yersinia pseudotuberculosis invasin protein
    • Leong, J.M., Fournier, R.S., and Isberg, R.R. (1990) Identification of the integrin binding domain of the Yersinia pseudotuberculosis invasin protein. EMBO J 9: 1979-1989.
    • (1990) EMBO J , vol.9 , pp. 1979-1989
    • Leong, J.M.1    Fournier, R.S.2    Isberg, R.R.3
  • 29
    • 0030903802 scopus 로고    scopus 로고
    • The fibronectin-binding protein of Streptococcus pyogenes, sfbl, is involved in the internalization of group A streptococci by epithelial cells
    • Molinari, G., Talay, S.R., Valentin-Weigand, P., Rohde, M., and Chhatwal, G.S. (1997) The fibronectin-binding protein of Streptococcus pyogenes, sfbl, is involved in the internalization of group A streptococci by epithelial cells. Infect Immun 65: 1357-1363.
    • (1997) Infect Immun , vol.65 , pp. 1357-1363
    • Molinari, G.1    Talay, S.R.2    Valentin-Weigand, P.3    Rohde, M.4    Chhatwal, G.S.5
  • 30
    • 0030298375 scopus 로고    scopus 로고
    • Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/NGF receptor family
    • Montgomery, R.I., Warner, M.S., Lum, B.J., and Spear, P.G. (1996) Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/NGF receptor family. Cell 87: 427-436.
    • (1996) Cell , vol.87 , pp. 427-436
    • Montgomery, R.I.1    Warner, M.S.2    Lum, B.J.3    Spear, P.G.4
  • 31
    • 0027209270 scopus 로고
    • The extracellular matrix proteins laminin and fibronectin contain binding domains for human plasminogen and tissue plasminogen activator
    • Moser, T.L., Enghild, J.J., Pizzo, S.V., and Stack, M.S. (1993) The extracellular matrix proteins laminin and fibronectin contain binding domains for human plasminogen and tissue plasminogen activator. J Biol Chem 268: 18917-18923.
    • (1993) J Biol Chem , vol.268 , pp. 18917-18923
    • Moser, T.L.1    Enghild, J.J.2    Pizzo, S.V.3    Stack, M.S.4
  • 32
    • 0019308612 scopus 로고
    • Binding and Factor XIIIa-mediated cross-linking of a 27-kilodalton fragment of fibronectin to Staphylococcus aureus
    • Mosher, D.F., and Proctor, R.A. (1980) Binding and Factor XIIIa-mediated cross-linking of a 27-kilodalton fragment of fibronectin to Staphylococcus aureus. Science 209: 927-929.
    • (1980) Science , vol.209 , pp. 927-929
    • Mosher, D.F.1    Proctor, R.A.2
  • 33
    • 0030889054 scopus 로고    scopus 로고
    • Syndecan-4 proteoglycan regulates the distribution and activity of protein kinase C
    • Oh, E.-S., Woods, A., and Couchman, J.R. (1997a) Syndecan-4 proteoglycan regulates the distribution and activity of protein kinase C. J Biol Chem 272: 8133-8136.
    • (1997) J Biol Chem , vol.272 , pp. 8133-8136
    • Oh, E.-S.1    Woods, A.2    Couchman, J.R.3
  • 34
    • 0030911243 scopus 로고    scopus 로고
    • Multimerization of the cytoplasmic domain of syndecan-4 is required for its ability to activate protein kinase C
    • Oh, E.-S., Woods, A., and Couchman, J.R. (1997b) Multimerization of the cytoplasmic domain of syndecan-4 is required for its ability to activate protein kinase C. J Biol Chem 272: 11805-11811.
    • (1997) J Biol Chem , vol.272 , pp. 11805-11811
    • Oh, E.-S.1    Woods, A.2    Couchman, J.R.3
  • 35
    • 0027960065 scopus 로고
    • MSCRAMM-mediated adherence of microorganisms to host tissues
    • Patti, J.M., Bradley, L.A., McGavin, M.J., and Höök, M. (1994) MSCRAMM-mediated adherence of microorganisms to host tissues. Annu Rev Microbiol 48: 585-617.
    • (1994) Annu Rev Microbiol , vol.48 , pp. 585-617
    • Patti, J.M.1    Bradley, L.A.2    McGavin, M.J.3    Höök, M.4
  • 36
    • 0019848776 scopus 로고
    • Location of the cell-attachment site in fibronectin with monoclonal antibodies and proteolytic fragments of the molecule
    • Pierschbacher, M.D., Hayman, E.G., and Ruoslahti., E. (1981) Location of the cell-attachment site in fibronectin with monoclonal antibodies and proteolytic fragments of the molecule. Cell 26: 259-267.
    • (1981) Cell , vol.26 , pp. 259-267
    • Pierschbacher, M.D.1    Hayman, E.G.2    Ruoslahti, E.3
  • 37
    • 0025285022 scopus 로고
    • Peptide analogs to a fibronectin receptor inhibit attachment of Staphylococcus aureus to fibronectin-containing substrates
    • Raja, R.H., Raucci, G., and Höök, M. (1990) Peptide analogs to a fibronectin receptor inhibit attachment of Staphylococcus aureus to fibronectin-containing substrates. Infect Immun 58: 2593-2598.
    • (1990) Infect Immun , vol.58 , pp. 2593-2598
    • Raja, R.H.1    Raucci, G.2    Höök, M.3
  • 38
    • 0031023713 scopus 로고    scopus 로고
    • Microbial adherence to and invasion through proteoglycans
    • Rostand, K.S., and Esko, J.D. (1997) Microbial adherence to and invasion through proteoglycans. Infect Immun 65: 1-8.
    • (1997) Infect Immun , vol.65 , pp. 1-8
    • Rostand, K.S.1    Esko, J.D.2
  • 39
    • 0029775681 scopus 로고    scopus 로고
    • RGD and other recognition sequences for integrins
    • Ruoslahti, E. (1996) RGD and other recognition sequences for integrins. Annu Rev Cell Dev. Biol 12: 697-715.
    • (1996) Annu Rev Cell Dev. Biol , vol.12 , pp. 697-715
    • Ruoslahti, E.1
  • 40
    • 0028825543 scopus 로고
    • Regulation of growth factor activation by proteoglycans: What is the role of low affinity receptors?
    • Schlessinger, J., Lax, I., and Lemmon, M. (1995) Regulation of growth factor activation by proteoglycans: what is the role of low affinity receptors? Cell 83: 357-360.
    • (1995) Cell , vol.83 , pp. 357-360
    • Schlessinger, J.1    Lax, I.2    Lemmon, M.3
  • 41
    • 0029070194 scopus 로고
    • A Mycobacterium leprae gene encoding a fibronectin binding protein is used for efficient invasion of epithelial cells and Schwann cells
    • Schorey, J.S., Li, Q., McCourt, D.W., Bong-Mastek, M., Clark-Curtiss, J.E., Ratliff, T.L., et al. (1995) A Mycobacterium leprae gene encoding a fibronectin binding protein is used for efficient invasion of epithelial cells and Schwann cells. Infect Immun 63: 2652-2657.
    • (1995) Infect Immun , vol.63 , pp. 2652-2657
    • Schorey, J.S.1    Li, Q.2    McCourt, D.W.3    Bong-Mastek, M.4    Clark-Curtiss, J.E.5    Ratliff, T.L.6
  • 42
    • 0020641552 scopus 로고
    • Affinity chromatography on immobilized fibrin monomer, IV. Two fibrin-binding peptides of a chymotryptic digest of human plasma fibronectin
    • Seidl, M., and Hormann, H. (1983) Affinity chromatography on immobilized fibrin monomer, IV. Two fibrin-binding peptides of a chymotryptic digest of human plasma fibronectin. Hoppe-Seylers Z Physiol Chem 364: 83-92.
    • (1983) Hoppe-Seylers Z Physiol Chem , vol.364 , pp. 83-92
    • Seidl, M.1    Hormann, H.2
  • 43
    • 0027763194 scopus 로고
    • Protein F: An adhesin of Streptococcus pyogenes binds fibronectin via two distinct domains
    • Sela, S., Aviv, A., Tovi, A., Burstein, I., Caparon, M.G., and Hanski, E. (1993) Protein F: an adhesin of Streptococcus pyogenes binds fibronectin via two distinct domains. Mol Microbiol 10: 1049-1055.
    • (1993) Mol Microbiol , vol.10 , pp. 1049-1055
    • Sela, S.1    Aviv, A.2    Tovi, A.3    Burstein, I.4    Caparon, M.G.5    Hanski, E.6
  • 44
    • 0030930267 scopus 로고    scopus 로고
    • A proposed role for the lutropin receptor in contact-inducible gonococcal invasion of Hec1B cells
    • Spence, J.M., Chen, J.C.-R., and Clark, V.L. (1997) A proposed role for the lutropin receptor in contact-inducible gonococcal invasion of Hec1B cells. Infect Immun 65: 3736-3742.
    • (1997) Infect Immun , vol.65 , pp. 3736-3742
    • Spence, J.M.1    Chen, J.C.-R.2    Clark, V.L.3
  • 45
    • 0021341550 scopus 로고
    • Fibronectin binding to a Streptococcus pyogenes strain
    • Speziale, P., Höök, M., Switalski, L.M., and Wadström, T. (1984) Fibronectin binding to a Streptococcus pyogenes strain. J Bacteriol 157: 420-427.
    • (1984) J Bacteriol , vol.157 , pp. 420-427
    • Speziale, P.1    Höök, M.2    Switalski, L.M.3    Wadström, T.4
  • 46
    • 0027216439 scopus 로고
    • Modulation of tissue plasminogen activator-catalyzed plasminogen activation by synthetic peptides derived from the amino-terminal heparin binding domain of fibronectin
    • Stack, M.S., and Pizzo, S.V. (1993) Modulation of tissue plasminogen activator-catalyzed plasminogen activation by synthetic peptides derived from the amino-terminal heparin binding domain of fibronectin. J Biol Chem 268: 18924-18928.
    • (1993) J Biol Chem , vol.268 , pp. 18924-18928
    • Stack, M.S.1    Pizzo, S.V.2
  • 47
    • 0022407510 scopus 로고
    • Fibronectin tetrapeptide is target for syphilis spirochete cytadherence
    • Thomas, D.D., Baseman, J.B., and Alderete, J.F. (1985) Fibronectin tetrapeptide is target for syphilis spirochete cytadherence. J Exp Med 162: 1715-1719.
    • (1985) J Exp Med , vol.162 , pp. 1715-1719
    • Thomas, D.D.1    Baseman, J.B.2    Alderete, J.F.3
  • 48
    • 0029027169 scopus 로고
    • Binding of syndecan-like cell surface proteoglycan receptors is required for Neisseria gonorrhoeae entry into human mucosal cells
    • van Putten, J.P.M., and Paul, S.M. (1995) Binding of syndecan-like cell surface proteoglycan receptors is required for Neisseria gonorrhoeae entry into human mucosal cells. EMBO J 14: 2144-2154.
    • (1995) EMBO J , vol.14 , pp. 2144-2154
    • Van Putten, J.P.M.1    Paul, S.M.2
  • 49
    • 0030981311 scopus 로고    scopus 로고
    • Infection of mucosal epithelial cells by Neisseria gonorrhoeae
    • van Putten, J.P.M., and Duensing, T.D. (1997) Infection of mucosal epithelial cells by Neisseria gonorrhoeae. Rev Med Microbiol 8: 51-59.
    • (1997) Rev Med Microbiol , vol.8 , pp. 51-59
    • Van Putten, J.P.M.1    Duensing, T.D.2
  • 50
    • 0028085888 scopus 로고
    • Measurements of invasion by antibody labeling and electron microscopy
    • van Putten, J.P.M., Weel, J.F.L, and Grassmé, H.U.C. (1994) Measurements of invasion by antibody labeling and electron microscopy. Methods Enzymol 236: 420-437.
    • (1994) Methods Enzymol , vol.236 , pp. 420-437
    • Van Putten, J.P.M.1    Weel, J.F.L.2    Grassmé, H.U.C.3
  • 51
    • 0030780595 scopus 로고    scopus 로고
    • Natural proteoglycan receptor analogs determine the dynamics of Opa adhesin-mediated gonococcal infection of Chang epithelial cells
    • van Putten, J.P.M., Hayes, S.F., and Duensing, T.D. (1997) Natural proteoglycan receptor analogs determine the dynamics of Opa adhesin-mediated gonococcal infection of Chang epithelial cells. Infect Immun 65: 5028-5034.
    • (1997) Infect Immun , vol.65 , pp. 5028-5034
    • Van Putten, J.P.M.1    Hayes, S.F.2    Duensing, T.D.3
  • 52
    • 0029848536 scopus 로고    scopus 로고
    • Carcinoembryonic antigens (CD66) on epithelial cells and neutrophils are receptors for Opa proteins of pathogenic neisseriae
    • Virji, M., Makepeace, K., Ferguson, D.J.P., and Watt, S.M. (1996) Carcinoembryonic antigens (CD66) on epithelial cells and neutrophils are receptors for Opa proteins of pathogenic neisseriae. Mol Microbiol 29: 941-950.
    • (1996) Mol Microbiol , vol.29 , pp. 941-950
    • Virji, M.1    Makepeace, K.2    Ferguson, D.J.P.3    Watt, S.M.4
  • 53
    • 0025850470 scopus 로고
    • Binding sites in fibronectin for an enterotoxigenic strain of E. coli B342289c
    • Visai, L., Bozzini, S., Petersen, T.E., Speziale, L., and Speziale, P. (1991) Binding sites in fibronectin for an enterotoxigenic strain of E. coli B342289c. FEBS Lett 290: 111-114.
    • (1991) FEBS Lett , vol.290 , pp. 111-114
    • Visai, L.1    Bozzini, S.2    Petersen, T.E.3    Speziale, L.4    Speziale, P.5
  • 54
    • 0027373782 scopus 로고
    • Activation of protein kinase C precedes α5β1 integrin-mediated cell spreading on fibronectin
    • Vuori, K., and Ruoslahti, E. (1993) Activation of protein kinase C precedes α5β1 integrin-mediated cell spreading on fibronectin. J Biol Chem 268: 21459-21462.
    • (1993) J Biol Chem , vol.268 , pp. 21459-21462
    • Vuori, K.1    Ruoslahti, E.2
  • 55
    • 0024110741 scopus 로고
    • The function of multiple extracellular matrix receptors in mediating cell adhesion to extracellular matrix: Preparation of monoclonal antibodies to the fibronectin receptor that specifically inhibit cell adhesion to fibronectin and react with platelet glycoprotein Ic-IIa
    • Wayner, E.A., Carter, W.G., Piotrowicz, R.S., and Kunicki, T.J. (1988) The function of multiple extracellular matrix receptors in mediating cell adhesion to extracellular matrix: preparation of monoclonal antibodies to the fibronectin receptor that specifically inhibit cell adhesion to fibronectin and react with platelet glycoprotein Ic-IIa. J Cell Biol 107: 1881-1891.
    • (1988) J Cell Biol , vol.107 , pp. 1881-1891
    • Wayner, E.A.1    Carter, W.G.2    Piotrowicz, R.S.3    Kunicki, T.J.4
  • 56
    • 0025729599 scopus 로고
    • In situ expression and localization of Neisseria gonorrhoeae opacity proteins in infected epithelial cells: Apparent role of Opa proteins in cellular invasion
    • Weel, J.F.L., Hopman, C.T.P., and van Putten, J.P.M. (1991) In situ expression and localization of Neisseria gonorrhoeae opacity proteins in infected epithelial cells: apparent role of Opa proteins in cellular invasion. J Exp Med 173: 1395-1405.
    • (1991) J Exp Med , vol.173 , pp. 1395-1405
    • Weel, J.F.L.1    Hopman, C.T.P.2    Van Putten, J.P.M.3
  • 57
    • 0027292986 scopus 로고
    • Bacterial proteins binding to the mammalian extracellular matrix
    • Westerlund, B., and Korhonen, T.K. (1993) Bacterial proteins binding to the mammalian extracellular matrix. Mol Microbiol 9: 687-694.
    • (1993) Mol Microbiol , vol.9 , pp. 687-694
    • Westerlund, B.1    Korhonen, T.K.2
  • 58
    • 0026645840 scopus 로고
    • Heparin sulfate proteoglycans and signalling in cell adhesion
    • Lane, D.A. et al. (eds). New York: Plenum Press
    • Woods, A., and Couchman, J.R. (1992a) Heparin sulfate proteoglycans and signalling in cell adhesion. In Heparin and Related Polysaccharides. Lane, D.A. et al. (eds). New York: Plenum Press, pp. 87-96.
    • (1992) Heparin and Related Polysaccharides , pp. 87-96
    • Woods, A.1    Couchman, J.R.2
  • 59
    • 0026603414 scopus 로고
    • Protein kinase C involvement in focal adhesion formation
    • Woods, A., and Couchman, J.R. (1992b) Protein kinase C involvement in focal adhesion formation. J Cell Sci 101: 277-290.
    • (1992) J Cell Sci , vol.101 , pp. 277-290
    • Woods, A.1    Couchman, J.R.2
  • 60
    • 0022707292 scopus 로고
    • Adhesion and cytoskeletal organisation of fibroblasts in response to fibronectin fragments
    • Woods, A., Couchman, J.R., Johansson, S., and Höök, M. (1986) Adhesion and cytoskeletal organisation of fibroblasts in response to fibronectin fragments. EMBO J 5: 665-670.
    • (1986) EMBO J , vol.5 , pp. 665-670
    • Woods, A.1    Couchman, J.R.2    Johansson, S.3    Höök, M.4
  • 61
    • 0024059120 scopus 로고
    • Novel purification of vitronectin from human plasma by heparin affinity chromatography
    • Yatohgo, T., Izumi, M., Kashiwagi, H., and Hayashi, M. (1988) Novel purification of vitronectin from human plasma by heparin affinity chromatography. Cell Struct Funct 13: 211-292.
    • (1988) Cell Struct Funct , vol.13 , pp. 211-292
    • Yatohgo, T.1    Izumi, M.2    Kashiwagi, H.3    Hayashi, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.