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Volumn 1800, Issue 6, 2010, Pages 545-555

Cell migration-The role of integrin glycosylation

Author keywords

3 1 integrin; 5 1 integrin; v 3 integrin; Migration; N oligosaccharides

Indexed keywords

ACTIN; ALPHA INTEGRIN; BETA INTEGRIN; DIMER; INTEGRIN; INTEGRIN RECEPTOR; KALININ; OLIGOSACCHARIDE; SIALIC ACID; VERY LATE ACTIVATION ANTIGEN 3; VERY LATE ACTIVATION ANTIGEN 5; VITRONECTIN RECEPTOR;

EID: 77952287201     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2010.03.013     Document Type: Review
Times cited : (128)

References (157)
  • 1
    • 0034764101 scopus 로고    scopus 로고
    • Events of wound-healing coordinated interaction among Matrix Metalloproteinases (MMPs), integrins, and extracellular matrix molecules
    • Steffensen Proteolytic B. events of wound-healing coordinated interaction among Matrix Metalloproteinases (MMPs), integrins, and extracellular matrix molecules. Crit. Rev. Oral Biol. Med. 2001, 12:373-398.
    • (2001) Crit. Rev. Oral Biol. Med. , vol.12 , pp. 373-398
    • Steffensen Proteolytic, B.1
  • 2
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: a physically integrated molecular process
    • Lauffenburger D.A., Horwitz A.F. Cell migration: a physically integrated molecular process. Cell 1996, 84:359-369.
    • (1996) Cell , vol.84 , pp. 359-369
    • Lauffenburger, D.A.1    Horwitz, A.F.2
  • 3
    • 0242456170 scopus 로고    scopus 로고
    • Axis of evil: molecular mechanisms of cancer metastasis
    • Bogenrieder T., Herlyn M. Axis of evil: molecular mechanisms of cancer metastasis. Oncogene 2003, 22:6524-6536.
    • (2003) Oncogene , vol.22 , pp. 6524-6536
    • Bogenrieder, T.1    Herlyn, M.2
  • 5
    • 34547651085 scopus 로고    scopus 로고
    • Differential cadherin expression: potential markers for epithelial to mesenchymal transformation during tumor progression
    • Agiostratidou G., Hulit J., Phillips G.R., Hazan R.B. Differential cadherin expression: potential markers for epithelial to mesenchymal transformation during tumor progression. J. Mammary Gland Biol. Neoplasia 2007, 12:127-133.
    • (2007) J. Mammary Gland Biol. Neoplasia , vol.12 , pp. 127-133
    • Agiostratidou, G.1    Hulit, J.2    Phillips, G.R.3    Hazan, R.B.4
  • 6
  • 7
    • 0034968420 scopus 로고    scopus 로고
    • An introduction to cell migration and invasion
    • Staff A.C. An introduction to cell migration and invasion. Scan. J. Clin. Lab. Investig. 2001, 61:257-268.
    • (2001) Scan. J. Clin. Lab. Investig. , vol.61 , pp. 257-268
    • Staff, A.C.1
  • 9
    • 33749350351 scopus 로고    scopus 로고
    • A cancer cell metalloprotease triad regulates the basement membrane transmigration program
    • Hotary K., Li X.-Y., Allen E., Stevens S.L., Weiss1 S.J. A cancer cell metalloprotease triad regulates the basement membrane transmigration program. Genes Dev. 2006, 20:2673-2686.
    • (2006) Genes Dev. , vol.20 , pp. 2673-2686
    • Hotary, K.1    Li, X.-Y.2    Allen, E.3    Stevens, S.L.4    Weiss1, S.J.5
  • 11
    • 34648832906 scopus 로고    scopus 로고
    • Illuminating the metastatic process
    • Sahai E. Illuminating the metastatic process. Nat. Rev. Cancer 2007, 7:737-749.
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 737-749
    • Sahai, E.1
  • 12
    • 49049119273 scopus 로고    scopus 로고
    • Caveolin-1 in cell polarization and directional migration
    • Grande-Garcia A., del Pozo M.A. Caveolin-1 in cell polarization and directional migration. Eur. J. Cell Biol. 2008, 87:641-647.
    • (2008) Eur. J. Cell Biol. , vol.87 , pp. 641-647
    • Grande-Garcia, A.1    del Pozo, M.A.2
  • 13
    • 0033527623 scopus 로고    scopus 로고
    • Cell migration - movin' on
    • Horwitz A.R., Parsons J.T. Cell migration - movin' on. Science 1999, 286:1102-1103.
    • (1999) Science , vol.286 , pp. 1102-1103
    • Horwitz, A.R.1    Parsons, J.T.2
  • 14
    • 37249083542 scopus 로고    scopus 로고
    • Cell-matrix adhesion complexes: master control machinery of cell migration
    • Lock J.G., Wehrle-Haller B., Strömblad S. Cell-matrix adhesion complexes: master control machinery of cell migration. Semin. Cancer Biol. 2008, 18:65-76.
    • (2008) Semin. Cancer Biol. , vol.18 , pp. 65-76
    • Lock, J.G.1    Wehrle-Haller, B.2    Strömblad, S.3
  • 16
    • 0034715924 scopus 로고    scopus 로고
    • The structural basis of dynamic cell adhesion: heads, tails, and allostery
    • Liddington R.C., Bankston L.A. The structural basis of dynamic cell adhesion: heads, tails, and allostery. Exp. Cell Res. 2000, 261:37-43.
    • (2000) Exp. Cell Res. , vol.261 , pp. 37-43
    • Liddington, R.C.1    Bankston, L.A.2
  • 17
    • 0037145037 scopus 로고    scopus 로고
    • Integrin: bidirectional allosteric signalling machines
    • Hynes R.O. Integrin: bidirectional allosteric signalling machines. Cell 2002, 110:673-687.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 18
    • 50849083158 scopus 로고    scopus 로고
    • Cell adhesion receptors in mechanotransduction
    • Schwartz M.A., DeSimon D.W. Cell adhesion receptors in mechanotransduction. Curr. Opin. Cell Biol. 2008, 20:551-556.
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 551-556
    • Schwartz, M.A.1    DeSimon, D.W.2
  • 19
    • 50849142875 scopus 로고    scopus 로고
    • Temporal and spatial regulation of integrins during development
    • Meighan C.M., Schwarzbauer J.E. Temporal and spatial regulation of integrins during development. Curr. Opin. Cell Biol. 2008, 20:520-524.
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 520-524
    • Meighan, C.M.1    Schwarzbauer, J.E.2
  • 20
    • 0032721665 scopus 로고    scopus 로고
    • Role of integrins in cancer: survey of expression patterns
    • Mizejewski G.J. Role of integrins in cancer: survey of expression patterns. P. S. E. B. M. 1999, 222:124-138.
    • (1999) P. S. E. B. M. , vol.222 , pp. 124-138
    • Mizejewski, G.J.1
  • 21
    • 1542269303 scopus 로고    scopus 로고
    • Integrins: roles in cancer development and as treatment targets
    • Jin H., Varner J. Integrins: roles in cancer development and as treatment targets. Br. J. Cancer 2004, 90:561-565.
    • (2004) Br. J. Cancer , vol.90 , pp. 561-565
    • Jin, H.1    Varner, J.2
  • 22
    • 34547684485 scopus 로고    scopus 로고
    • Multifaceted roles of integrins in breast cancer metastasis
    • White D.E., Muller W.J. Multifaceted roles of integrins in breast cancer metastasis. J. Mammary Gland Biol. Neoplasia 2007, 12:135-142.
    • (2007) J. Mammary Gland Biol. Neoplasia , vol.12 , pp. 135-142
    • White, D.E.1    Muller, W.J.2
  • 28
  • 30
    • 0031866394 scopus 로고    scopus 로고
    • Ligand recognition by the I domain-containing integrins
    • Dickeson S.K., Santoro S.A. Ligand recognition by the I domain-containing integrins. Cell. Mol. Life Sci. 1998, 54:556-566.
    • (1998) Cell. Mol. Life Sci. , vol.54 , pp. 556-566
    • Dickeson, S.K.1    Santoro, S.A.2
  • 31
    • 0037031906 scopus 로고    scopus 로고
    • Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling
    • Takagi J., Petre B.M., Walz T., Springer T.A. Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling. Cell 2002, 110:599-611.
    • (2002) Cell , vol.110 , pp. 599-611
    • Takagi, J.1    Petre, B.M.2    Walz, T.3    Springer, T.A.4
  • 32
    • 35548939067 scopus 로고    scopus 로고
    • Structural basis for ligand recognition by integrins
    • Takagi J. Structural basis for ligand recognition by integrins. Curr. Opin. Cell Biol. 2007, 19:557-564.
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 557-564
    • Takagi, J.1
  • 33
    • 1642396353 scopus 로고    scopus 로고
    • Involvement of transmembrane domain interactions in signal transduction by α /β integrins
    • Schneider D., Engelman D.M. Involvement of transmembrane domain interactions in signal transduction by α /β integrins. J. Biol. Chem. 2004, 279:9840-9846.
    • (2004) J. Biol. Chem. , vol.279 , pp. 9840-9846
    • Schneider, D.1    Engelman, D.M.2
  • 34
    • 0034715923 scopus 로고    scopus 로고
    • Focal adhesions: a nexus for intracellular signaling and cytoskeletal dynamics
    • Sastry S.K., Burridge K. Focal adhesions: a nexus for intracellular signaling and cytoskeletal dynamics. Exp. Cell Res. 2000, 261:25-36.
    • (2000) Exp. Cell Res. , vol.261 , pp. 25-36
    • Sastry, S.K.1    Burridge, K.2
  • 38
    • 33845329178 scopus 로고    scopus 로고
    • Signalling via integrins: implications for cell survival and anticancer strategies
    • Hehlgans S., Haase M., Cordes N. Signalling via integrins: implications for cell survival and anticancer strategies. Biochim. Biophys. Acta 2007, 1775:163-180.
    • (2007) Biochim. Biophys. Acta , vol.1775 , pp. 163-180
    • Hehlgans, S.1    Haase, M.2    Cordes, N.3
  • 39
    • 33846554255 scopus 로고    scopus 로고
    • Focal adhesion kinase: a potential target in cancer therapy
    • van Nimwegen M.J., van de Water B. Focal adhesion kinase: a potential target in cancer therapy. Biochem. Pharmacol. 2007, 73:597-609.
    • (2007) Biochem. Pharmacol. , vol.73 , pp. 597-609
    • van Nimwegen, M.J.1    van de Water, B.2
  • 41
    • 3142521875 scopus 로고    scopus 로고
    • Control of motile and invasive cell phenotypes by focal adhesion kinase
    • Schlaepfer D.D., Mitra S.K., Ilic D. Control of motile and invasive cell phenotypes by focal adhesion kinase. Biochim. Biophys. Acta 2004, 1692:77-102.
    • (2004) Biochim. Biophys. Acta , vol.1692 , pp. 77-102
    • Schlaepfer, D.D.1    Mitra, S.K.2    Ilic, D.3
  • 43
    • 0037904987 scopus 로고    scopus 로고
    • The integrin-actin connection, an eternal love affair
    • Brakebusch C., Fässler R. The integrin-actin connection, an eternal love affair. EMBO J. 2003, 22:2324-2333.
    • (2003) EMBO J. , vol.22 , pp. 2324-2333
    • Brakebusch, C.1    Fässler, R.2
  • 45
    • 67349161798 scopus 로고    scopus 로고
    • Regulation of fibronectin matrix assembly and capillary morphogenesis in endothelial cells by Rho family GTPases
    • Fernandez-Sauze S., Grall D., Cseh B., Van Obberghen-Schilling E. Regulation of fibronectin matrix assembly and capillary morphogenesis in endothelial cells by Rho family GTPases. Exp. Cell Res. 2009, 315:2092-2104.
    • (2009) Exp. Cell Res. , vol.315 , pp. 2092-2104
    • Fernandez-Sauze, S.1    Grall, D.2    Cseh, B.3    Van Obberghen-Schilling, E.4
  • 47
    • 0033620657 scopus 로고    scopus 로고
    • R-Ras signals through specific integrin a cytoplasmic domains to promote migration and invasion of breast epithelial cells
    • Keely P.J., Rusyn E.V., Cox A.D., Parise L.V. R-Ras signals through specific integrin a cytoplasmic domains to promote migration and invasion of breast epithelial cells. J. Cell Biol. 1999, 145:1077-1088.
    • (1999) J. Cell Biol. , vol.145 , pp. 1077-1088
    • Keely, P.J.1    Rusyn, E.V.2    Cox, A.D.3    Parise, L.V.4
  • 48
    • 0141988559 scopus 로고    scopus 로고
    • Molecular mechanisms of tumour invasion and metastasis: an integrated view
    • Cairns R.A., Khokha R., Hill R.P. Molecular mechanisms of tumour invasion and metastasis: an integrated view. Curr. Mol. Med. 2003, 3:659-671.
    • (2003) Curr. Mol. Med. , vol.3 , pp. 659-671
    • Cairns, R.A.1    Khokha, R.2    Hill, R.P.3
  • 49
    • 0031976733 scopus 로고    scopus 로고
    • Physical and biochemical regulation of integrin release during rear detachment of migrating cells
    • Palecek S.P., Huttenlocher A., Horwitz A.F., Lauffenburger D.A. Physical and biochemical regulation of integrin release during rear detachment of migrating cells. J. Cell Sci. 1998, 111:929-940.
    • (1998) J. Cell Sci. , vol.111 , pp. 929-940
    • Palecek, S.P.1    Huttenlocher, A.2    Horwitz, A.F.3    Lauffenburger, D.A.4
  • 50
    • 0033094580 scopus 로고    scopus 로고
    • Kinetic model for integrin-mediated adhesion release during cell migration
    • Palecek S.P., Horwitz A.F., Lauffenburger D.A. Kinetic model for integrin-mediated adhesion release during cell migration. Ann. Biomed. Eng. 1999, 27:219-235.
    • (1999) Ann. Biomed. Eng. , vol.27 , pp. 219-235
    • Palecek, S.P.1    Horwitz, A.F.2    Lauffenburger, D.A.3
  • 51
    • 0042681786 scopus 로고    scopus 로고
    • Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins
    • Kim M., Carman C.V., Springer T.A. Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins. Science 2003, 301:1720-1725.
    • (2003) Science , vol.301 , pp. 1720-1725
    • Kim, M.1    Carman, C.V.2    Springer, T.A.3
  • 53
  • 54
    • 0034715891 scopus 로고    scopus 로고
    • Multiple roles of integrins in cell motility
    • Holly S.P., Larson M.K., Parise L.V. Multiple roles of integrins in cell motility. Exp. Cell Res. 2000, 261:69-74.
    • (2000) Exp. Cell Res. , vol.261 , pp. 69-74
    • Holly, S.P.1    Larson, M.K.2    Parise, L.V.3
  • 55
    • 33645515261 scopus 로고    scopus 로고
    • Integrin trafficking and the control of cell migration
    • Caswell P.T., Norman J.C. Integrin trafficking and the control of cell migration. Traffic 2006, 7:14-21.
    • (2006) Traffic , vol.7 , pp. 14-21
    • Caswell, P.T.1    Norman, J.C.2
  • 57
    • 1442331993 scopus 로고    scopus 로고
    • Integrin activation
    • Calderwood D.A. Integrin activation. J. Cell Sci. 2004, 117:657-666.
    • (2004) J. Cell Sci. , vol.117 , pp. 657-666
    • Calderwood, D.A.1
  • 59
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation deduced from analysis of the SWISS-PROT database
    • Apweiler R., Hermjakob H., Sharon N. On the frequency of protein glycosylation deduced from analysis of the SWISS-PROT database. Biochim. Biophys. Acta 1999, 1473:4-8.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 60
    • 0022462129 scopus 로고
    • Biosynthetic controls that determine the branching and microheterogeneity of protein-bound oligosaccharide
    • Schachter H. Biosynthetic controls that determine the branching and microheterogeneity of protein-bound oligosaccharide. Biochem. Cell Biol. 1986, 64:163-181.
    • (1986) Biochem. Cell Biol. , vol.64 , pp. 163-181
    • Schachter, H.1
  • 61
    • 0032321747 scopus 로고    scopus 로고
    • Protein N-glycosylation: molecular genetics and functional significance
    • Kukuruzinska M.A., Lennon K. Protein N-glycosylation: molecular genetics and functional significance. Crit. Rev. Oral Biol. Med. 1998, 9:415-448.
    • (1998) Crit. Rev. Oral Biol. Med. , vol.9 , pp. 415-448
    • Kukuruzinska, M.A.1    Lennon, K.2
  • 62
    • 27744597289 scopus 로고    scopus 로고
    • Prediction of glycan structures from gene expression data based on glycosyltransferase reactions
    • Kawano S., Hashimoto K., Miyama T., Goto S., Kanehisa M. Prediction of glycan structures from gene expression data based on glycosyltransferase reactions. Bioinformatics 2005, 21:3976-3982.
    • (2005) Bioinformatics , vol.21 , pp. 3976-3982
    • Kawano, S.1    Hashimoto, K.2    Miyama, T.3    Goto, S.4    Kanehisa, M.5
  • 64
    • 0032714567 scopus 로고    scopus 로고
    • Review: glycoprotein glycosylation and cancer progression
    • Dennis J.W., Granovsky M., Warren C.E. Review: glycoprotein glycosylation and cancer progression. Biochim. Biophys. Acta 1999, 1473:21-34.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 21-34
    • Dennis, J.W.1    Granovsky, M.2    Warren, C.E.3
  • 66
    • 0034014642 scopus 로고    scopus 로고
    • N-glycans influence the in vitro adhesive and invasive behavior of the three metastatic cell lines
    • Bironaite D., Nesland J.M., Risberg B., Bryne M. N-glycans influence the in vitro adhesive and invasive behavior of the three metastatic cell lines. Tumor Biol. 2000, 21:165-175.
    • (2000) Tumor Biol. , vol.21 , pp. 165-175
    • Bironaite, D.1    Nesland, J.M.2    Risberg, B.3    Bryne, M.4
  • 68
    • 22944456543 scopus 로고    scopus 로고
    • Altered glycosylation of proteins produced by malignant cells, and application for the diagnosis and immunotherapy of tumours
    • Kobata A., Amano J. Altered glycosylation of proteins produced by malignant cells, and application for the diagnosis and immunotherapy of tumours. Immunol. Cell Biol. 2005, 83:429-439.
    • (2005) Immunol. Cell Biol. , vol.83 , pp. 429-439
    • Kobata, A.1    Amano, J.2
  • 73
    • 0037031943 scopus 로고    scopus 로고
    • Hyposialylation of integrins stimulates the activity of myeloid fibronectin receptors
    • Semel A.C., Seales E.C., Singhal A., Eklund E.A., Colley K.J., Bellis S.L. Hyposialylation of integrins stimulates the activity of myeloid fibronectin receptors. J. Biol. Chem. 2002, 277:32830-32836.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32830-32836
    • Semel, A.C.1    Seales, E.C.2    Singhal, A.3    Eklund, E.A.4    Colley, K.J.5    Bellis, S.L.6
  • 75
    • 3142695658 scopus 로고    scopus 로고
    • Effects of glycosylation on peptide conformation: a synergistic experimental and computational study
    • Bosques C.J., Tschampel S.M., Woods R.J., Imperiali B. Effects of glycosylation on peptide conformation: a synergistic experimental and computational study. J. Am. Chem. Soc. 2004, 126:8421-8425.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8421-8425
    • Bosques, C.J.1    Tschampel, S.M.2    Woods, R.J.3    Imperiali, B.4
  • 78
    • 66449112293 scopus 로고    scopus 로고
    • An N-glycosylation site on the β-propeller domain of the integrin α5 subunit plays key roles in both its function and site-specific modification by β1, 4-N-acetylglucosaminyltransferase III
    • Sato Y., Isaji T., Tajiri M., Yoshida-Yamamoto S., Yoshinaka T., Somehara T., Fukuda T., Wada Y., Gu J. An N-glycosylation site on the β-propeller domain of the integrin α5 subunit plays key roles in both its function and site-specific modification by β1, 4-N-acetylglucosaminyltransferase III. J. Biol. Chem. 2009, 284:11873-11881.
    • (2009) J. Biol. Chem. , vol.284 , pp. 11873-11881
    • Sato, Y.1    Isaji, T.2    Tajiri, M.3    Yoshida-Yamamoto, S.4    Yoshinaka, T.5    Somehara, T.6    Fukuda, T.7    Wada, Y.8    Gu, J.9
  • 79
    • 68249103612 scopus 로고    scopus 로고
    • Core fucose and bisecting GlcNAc, the direct modifiers of the N-glycan core: their functions and target proteins
    • Takahashi M., Kuroki Y., Ohtsubo K., Taniguchi N. Core fucose and bisecting GlcNAc, the direct modifiers of the N-glycan core: their functions and target proteins. Carbohydr. Res. 2009, 344:1387-1390.
    • (2009) Carbohydr. Res. , vol.344 , pp. 1387-1390
    • Takahashi, M.1    Kuroki, Y.2    Ohtsubo, K.3    Taniguchi, N.4
  • 80
    • 1642309129 scopus 로고    scopus 로고
    • Glycosylation defining cancer cell motility and invasiveness
    • Ono M., Hakomori S. Glycosylation defining cancer cell motility and invasiveness. Glycoconj. J. 2004, 20:71-78.
    • (2004) Glycoconj. J. , vol.20 , pp. 71-78
    • Ono, M.1    Hakomori, S.2
  • 81
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: all of the theories are correct
    • Varki A. Biological roles of oligosaccharides: all of the theories are correct. Glycobiology 1993, 3:97-130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 83
    • 0037418254 scopus 로고    scopus 로고
    • Stabilizing the open conformation of the integrin headpiece with a glycan wedge increases affinity for ligand
    • Luo B.-H., Springer T.A., Takagi J. Stabilizing the open conformation of the integrin headpiece with a glycan wedge increases affinity for ligand. PNAS 2003, 100:2403-2408.
    • (2003) PNAS , vol.100 , pp. 2403-2408
    • Luo, B.-H.1    Springer, T.A.2    Takagi, J.3
  • 85
    • 0036677372 scopus 로고    scopus 로고
    • Glycosylation defining cancer malignancy. New wine in an old bottle
    • Hakomori S. Glycosylation defining cancer malignancy. New wine in an old bottle. Proc. Natl. Acad. Sci. U.S.A. 2002, 99:10231-10233.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 10231-10233
    • Hakomori, S.1
  • 86
    • 0034467007 scopus 로고    scopus 로고
    • Metastases: the glycan connection
    • Couldrey C., Green J.E. Metastases: the glycan connection. Breast Cancer Res. 2000, 2:321-323.
    • (2000) Breast Cancer Res. , vol.2 , pp. 321-323
    • Couldrey, C.1    Green, J.E.2
  • 87
    • 0035740634 scopus 로고    scopus 로고
    • On the role of cell surface carbohydrates and their binding proteins (lectins) in tumor metastasis
    • Gorelik E., Galili U., Raz A. On the role of cell surface carbohydrates and their binding proteins (lectins) in tumor metastasis. Cancer Metastasis Rev. 2001, 20:245-277.
    • (2001) Cancer Metastasis Rev. , vol.20 , pp. 245-277
    • Gorelik, E.1    Galili, U.2    Raz, A.3
  • 88
    • 53049084874 scopus 로고    scopus 로고
    • N-glycans in cancer progression
    • Lau K.S., Dennis J.W. N-glycans in cancer progression. Glycobiology 2008, 18:750-760.
    • (2008) Glycobiology , vol.18 , pp. 750-760
    • Lau, K.S.1    Dennis, J.W.2
  • 89
    • 0034351214 scopus 로고    scopus 로고
    • The sialyl-α2, 6-lactosaminyl-structure: biosynthesis and functional role
    • Dall'Olio F. The sialyl-α2, 6-lactosaminyl-structure: biosynthesis and functional role. Glycoconj. J. 2000, 17:669-676.
    • (2000) Glycoconj. J. , vol.17 , pp. 669-676
    • Dall'Olio, F.1
  • 90
    • 31444433687 scopus 로고    scopus 로고
    • Altered glycosylation in cancer: sialic acids and sialyltransferases
    • Wang P.H. Altered glycosylation in cancer: sialic acids and sialyltransferases. J. Cancer Mol. 2005, 1:73-81.
    • (2005) J. Cancer Mol. , vol.1 , pp. 73-81
    • Wang, P.H.1
  • 92
    • 67349087158 scopus 로고    scopus 로고
    • ST6Gal-I expression in ovarian cancer cells promotes an invasive phenotype by altering integrin glycosylation and function
    • Christie D.R., Shaikh F.M., Lucas J.A., Lucas J.A., Bellis S.L. ST6Gal-I expression in ovarian cancer cells promotes an invasive phenotype by altering integrin glycosylation and function. J. Ovarian Res. 2008, 1:3. 10.1186/1757-2215-1-3.
    • (2008) J. Ovarian Res. , vol.1 , pp. 3
    • Christie, D.R.1    Shaikh, F.M.2    Lucas, J.A.3    Lucas, J.A.4    Bellis, S.L.5
  • 93
    • 33748677966 scopus 로고    scopus 로고
    • Sialilated β1, 6 branched N-oligosaccharides modulate adhesion, chemotaxis and motility of melanoma cells: Effect on invasion and spontaneous metastasis properties
    • Reddy B.V.V.G., Kalraiya R.D. Sialilated β1, 6 branched N-oligosaccharides modulate adhesion, chemotaxis and motility of melanoma cells: Effect on invasion and spontaneous metastasis properties. Biochim. Biophys. Acta 2006, 1760:1393-1402.
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 1393-1402
    • Reddy, B.V.V.G.1    Kalraiya, R.D.2
  • 95
    • 23944471882 scopus 로고    scopus 로고
    • Altered melanoma cell surface glycosylation mediates organ specific adhesion and metastasis via lectin receptors on the lung vascular endothelium
    • Krishnan V., Bane S.M., Kawle P.D., Naresh K.N., Kalraiya R.D. Altered melanoma cell surface glycosylation mediates organ specific adhesion and metastasis via lectin receptors on the lung vascular endothelium. Clin. Exp. Metastasis 2005, 22:11-24.
    • (2005) Clin. Exp. Metastasis , vol.22 , pp. 11-24
    • Krishnan, V.1    Bane, S.M.2    Kawle, P.D.3    Naresh, K.N.4    Kalraiya, R.D.5
  • 96
    • 0033595784 scopus 로고    scopus 로고
    • Increased susceptibility to apoptosis of human hepatocarcinoma cells transfected with antisense N-acetylglucosaminyltransferase V cDNA
    • Guo H.B., Liu F., Chen H.L. Increased susceptibility to apoptosis of human hepatocarcinoma cells transfected with antisense N-acetylglucosaminyltransferase V cDNA. Biochem. Biophys. Res. Commun. 1999, 264:509-517.
    • (1999) Biochem. Biophys. Res. Commun. , vol.264 , pp. 509-517
    • Guo, H.B.1    Liu, F.2    Chen, H.L.3
  • 97
    • 28644451894 scopus 로고    scopus 로고
    • Coexpression of β1,6-N-acetylglucosaminyltransferase V glycoprotein substrates defines aggressive breast cancers with poor outcome
    • Siddiqui S.F., Pawelek J., Handerson T., Lin C.Y., Dickson R.B., Rimm D.L., Camp R.L. Coexpression of β1,6-N-acetylglucosaminyltransferase V glycoprotein substrates defines aggressive breast cancers with poor outcome. Cancer Epidemiol. Biomark. Prev. 2005, 14:2517-2523.
    • (2005) Cancer Epidemiol. Biomark. Prev. , vol.14 , pp. 2517-2523
    • Siddiqui, S.F.1    Pawelek, J.2    Handerson, T.3    Lin, C.Y.4    Dickson, R.B.5    Rimm, D.L.6    Camp, R.L.7
  • 98
    • 34547610472 scopus 로고    scopus 로고
    • Inhibition of a specific N-glycosylation activity results in attenuation of breast carcinoma cell invasiveness-related phenotypes: inhibition of epidermal growth factor-induced dephosphorylation of focal adhesion kinase
    • Guo H.B., Randolph M., Pierce M. Inhibition of a specific N-glycosylation activity results in attenuation of breast carcinoma cell invasiveness-related phenotypes: inhibition of epidermal growth factor-induced dephosphorylation of focal adhesion kinase. J. Biol. Chem. 2007, 282:22150-22162.
    • (2007) J. Biol. Chem. , vol.282 , pp. 22150-22162
    • Guo, H.B.1    Randolph, M.2    Pierce, M.3
  • 99
    • 33845629320 scopus 로고    scopus 로고
    • Increase in β1-6 GlcNAc branching caused by N-acetylglucosaminyltransferase V directs integrin β1 stability in human hepatocellular carcinoma cell line SMMC-7721
    • Wang L., Liang Y., Li Z., Cai X., Zhang W., Wu G., Jin J., Fang Z., Yang Y., Zha X. Increase in β1-6 GlcNAc branching caused by N-acetylglucosaminyltransferase V directs integrin β1 stability in human hepatocellular carcinoma cell line SMMC-7721. J. Cell. Biochem. 2007, 100:230-241.
    • (2007) J. Cell. Biochem. , vol.100 , pp. 230-241
    • Wang, L.1    Liang, Y.2    Li, Z.3    Cai, X.4    Zhang, W.5    Wu, G.6    Jin, J.7    Fang, Z.8    Yang, Y.9    Zha, X.10
  • 100
    • 38649097214 scopus 로고    scopus 로고
    • N-acetylglucosaminyltransferase V mediates cell migration and invasion of mouse mammary tumor cells 4TO7 via RhoA and Rac1 signaling pathway
    • Zhao Y., Li J., Xing Y., Wang J., Lu C., Xin X., Geng M. N-acetylglucosaminyltransferase V mediates cell migration and invasion of mouse mammary tumor cells 4TO7 via RhoA and Rac1 signaling pathway. Mol. Cell Biochem. 2008, 309:199-208.
    • (2008) Mol. Cell Biochem. , vol.309 , pp. 199-208
    • Zhao, Y.1    Li, J.2    Xing, Y.3    Wang, J.4    Lu, C.5    Xin, X.6    Geng, M.7
  • 103
    • 5444266511 scopus 로고    scopus 로고
    • Regulation of integrin functions by N-glycans
    • Gu J., Taniguchi N. Regulation of integrin functions by N-glycans. Glycoconj. J. 2004, 21:9-15.
    • (2004) Glycoconj. J. , vol.21 , pp. 9-15
    • Gu, J.1    Taniguchi, N.2
  • 106
    • 33645822097 scopus 로고    scopus 로고
    • Galectin binding to Mgat5- modified N-glycans regulates fibronectin matrix remodeling in tumor cells
    • Lagana A., Goetz J.G., Cheung P., Raz A., Dennis J.W., Nabi I.R. Galectin binding to Mgat5- modified N-glycans regulates fibronectin matrix remodeling in tumor cells. Mol. Cell. Biol. 2006, 26:3181-3193.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3181-3193
    • Lagana, A.1    Goetz, J.G.2    Cheung, P.3    Raz, A.4    Dennis, J.W.5    Nabi, I.R.6
  • 107
    • 0037330988 scopus 로고    scopus 로고
    • 1 integrin in determining the supramolecular organization of laminin-5 in the extracellular matrix of keratinocytes
    • 1 integrin in determining the supramolecular organization of laminin-5 in the extracellular matrix of keratinocytes. Exp. Cell Res. 2003, 283:67-79.
    • (2003) Exp. Cell Res. , vol.283 , pp. 67-79
    • DeHart, G.W.1    Healy, K.E.2    Jones, J.C.R.3
  • 109
    • 33344461837 scopus 로고    scopus 로고
    • Integrins and angiogenesis: a sticky business
    • Serini G., Valdembri D., Bussolino F. Integrins and angiogenesis: a sticky business. Exp. Cell Res. 2006, 312:651-658.
    • (2006) Exp. Cell Res. , vol.312 , pp. 651-658
    • Serini, G.1    Valdembri, D.2    Bussolino, F.3
  • 111
    • 0037278885 scopus 로고    scopus 로고
    • Integrin adhesion receptors in tumor metastasis
    • Felding-Habermann B. Integrin adhesion receptors in tumor metastasis. Clin. Exp. Metastasis 2003, 20:203-213.
    • (2003) Clin. Exp. Metastasis , vol.20 , pp. 203-213
    • Felding-Habermann, B.1
  • 112
    • 58149308800 scopus 로고    scopus 로고
    • Effect of altered glycosylation on the structure of the I-like domain of β1 integrin: a molecular dynamics study
    • Liu Y., Pan D., Bellis S.L., Song Y. Effect of altered glycosylation on the structure of the I-like domain of β1 integrin: a molecular dynamics study. Proteins 2008, 73:989-1000.
    • (2008) Proteins , vol.73 , pp. 989-1000
    • Liu, Y.1    Pan, D.2    Bellis, S.L.3    Song, Y.4
  • 113
    • 0028239080 scopus 로고
    • 1 subunits and concomitant loss of fibronectin binding activity
    • 1 subunits and concomitant loss of fibronectin binding activity. J. Biol. Chem. 1994, 269:12325-12331.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12325-12331
    • Zheng, M.1    Fang, H.2    Hakomori, S.3
  • 114
    • 0024436107 scopus 로고
    • Analysis of the role of glycosylation of the human fibronectin receptor
    • Akiyama S.K., Yamada S.S., Yamada K.M. Analysis of the role of glycosylation of the human fibronectin receptor. J. Biol. Chem. 1989, 264:18011-18018.
    • (1989) J. Biol. Chem. , vol.264 , pp. 18011-18018
    • Akiyama, S.K.1    Yamada, S.S.2    Yamada, K.M.3
  • 115
    • 4344590221 scopus 로고    scopus 로고
    • Relations of the type and branch of surface N-glycans to cell adhesion, migration and integrin expressions
    • Zhang Y., Zhao J., Zhang X., Guo H., Liu F., Chen H. Relations of the type and branch of surface N-glycans to cell adhesion, migration and integrin expressions. Mol. Cell. Biochem. 2004, 260:137-146.
    • (2004) Mol. Cell. Biochem. , vol.260 , pp. 137-146
    • Zhang, Y.1    Zhao, J.2    Zhang, X.3    Guo, H.4    Liu, F.5    Chen, H.6
  • 116
    • 0024278682 scopus 로고
    • Cell sialylation and tumor metastasis: metastatic potential of B16 melanoma variants correlates with their relative numbers of specific penultimate oligosaccharide structures
    • Passaniti A., Hart G.W. Cell sialylation and tumor metastasis: metastatic potential of B16 melanoma variants correlates with their relative numbers of specific penultimate oligosaccharide structures. J. Biol. Chem. 1988, 263:7591-7603.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7591-7603
    • Passaniti, A.1    Hart, G.W.2
  • 118
    • 0029021007 scopus 로고
    • Reduced contact-inhibition and substratum adhesion in epithelial cells expressing GlcNAc-transferase V
    • Demetriou M., Nabi I.R., Coppolino M., Dedher S., Dennis J.W. Reduced contact-inhibition and substratum adhesion in epithelial cells expressing GlcNAc-transferase V. J. Cell Biol. 1995, 130:383-392.
    • (1995) J. Cell Biol. , vol.130 , pp. 383-392
    • Demetriou, M.1    Nabi, I.R.2    Coppolino, M.3    Dedher, S.4    Dennis, J.W.5
  • 121
    • 51649085488 scopus 로고    scopus 로고
    • Tumor cell migration and invasion are regulated by expression of variant integrin glycoforms
    • Shaikh F.M., Seales E.C., Clem W.C., Hennessy K.M., Zhuo Y., Bellis S.L. Tumor cell migration and invasion are regulated by expression of variant integrin glycoforms. Exp. Cell Res. 2008, 314:2941-2950.
    • (2008) Exp. Cell Res. , vol.314 , pp. 2941-2950
    • Shaikh, F.M.1    Seales, E.C.2    Clem, W.C.3    Hennessy, K.M.4    Zhuo, Y.5    Bellis, S.L.6
  • 124
    • 0037312180 scopus 로고    scopus 로고
    • The immunoglobulin-superfamily molecule basigin is a binding protein for oligomannosidic carbohydrates: an anti-idiotypic approach
    • Heller M., von der Ohe M., Kleene R., Mohajeri H., Schachner M. The immunoglobulin-superfamily molecule basigin is a binding protein for oligomannosidic carbohydrates: an anti-idiotypic approach. J. Neurochem. 2003, 84:557-565.
    • (2003) J. Neurochem. , vol.84 , pp. 557-565
    • Heller, M.1    von der Ohe, M.2    Kleene, R.3    Mohajeri, H.4    Schachner, M.5
  • 125
    • 62149091091 scopus 로고    scopus 로고
    • Signal co-operation between integrins and other receptor systems
    • Streuli Ch.H., Akhtar N. Signal co-operation between integrins and other receptor systems. Biochem. J. 2009, 418:491-506.
    • (2009) Biochem. J. , vol.418 , pp. 491-506
    • Streuli, C.1    Akhtar, N.2
  • 127
    • 35748975965 scopus 로고    scopus 로고
    • Tetraspanin CD151 promotes cell migration by regulating integrin trafficking
    • Liu L., He B., Liu W.M., Zhou D., Cox J.V., Zhang X.A. Tetraspanin CD151 promotes cell migration by regulating integrin trafficking. J. Biol. Chem. 2007, 282:31631-31642.
    • (2007) J. Biol. Chem. , vol.282 , pp. 31631-31642
    • Liu, L.1    He, B.2    Liu, W.M.3    Zhou, D.4    Cox, J.V.5    Zhang, X.A.6
  • 130
  • 136
    • 0032910126 scopus 로고    scopus 로고
    • Laminins of the dermo-epidermal junction
    • Aumailley M., Roussel P. Laminins of the dermo-epidermal junction. Matrix Biol. 1999, 18:19-28.
    • (1999) Matrix Biol. , vol.18 , pp. 19-28
    • Aumailley, M.1    Roussel, P.2
  • 137
    • 0034858098 scopus 로고    scopus 로고
    • Biological and clinical relevance of Laminin-5 in cancer
    • Giannelli G., Antonaci S. Biological and clinical relevance of Laminin-5 in cancer. Clin. Exp. Metastasis 2000, 18:439-443.
    • (2000) Clin. Exp. Metastasis , vol.18 , pp. 439-443
    • Giannelli, G.1    Antonaci, S.2
  • 140
    • 0027217908 scopus 로고
    • Expression of integrins and basement membrane components by wound keratinocyes
    • Larjava H., Salo T., Haapasalmi K., Kramer R.H., Heino J. Expression of integrins and basement membrane components by wound keratinocyes. J. Clin. Invest. 1993, 92:1425-1435.
    • (1993) J. Clin. Invest. , vol.92 , pp. 1425-1435
    • Larjava, H.1    Salo, T.2    Haapasalmi, K.3    Kramer, R.H.4    Heino, J.5
  • 142
    • 4444361792 scopus 로고    scopus 로고
    • 1 directs the stabilization of a polarized lamellipodium in epithelial cells through activation of Rac1
    • 1 directs the stabilization of a polarized lamellipodium in epithelial cells through activation of Rac1. J. Cell Sci. 2004, 117:3947-3959.
    • (2004) J. Cell Sci. , vol.117 , pp. 3947-3959
    • Choma, D.P.1    Pumiglia, K.2    DiPersio, C.M.3
  • 146
    • 0041375315 scopus 로고    scopus 로고
    • Adhesion properties of human bladder cell lines with extracellular matrix components: the role of integrins and glycosylation
    • Lityńska A., Przybył M., Pocheć E., Laidler P. Adhesion properties of human bladder cell lines with extracellular matrix components: the role of integrins and glycosylation. Acta Biochim. Pol. 2002, 49:643-650.
    • (2002) Acta Biochim. Pol. , vol.49 , pp. 643-650
    • Lityńska, A.1    Przybyło, M.2    Pocheć, E.3    Laidler, P.4
  • 149
    • 19544362066 scopus 로고    scopus 로고
    • Adhesion, migration and communication in melanocytes and melanoma
    • Haass N.K., Smalley K.S.M., Li L., Herlyn M. Adhesion, migration and communication in melanocytes and melanoma. Pigment Cell Res. 2005, 18:150-159.
    • (2005) Pigment Cell Res. , vol.18 , pp. 150-159
    • Haass, N.K.1    Smalley, K.S.M.2    Li, L.3    Herlyn, M.4
  • 150
    • 35349023688 scopus 로고    scopus 로고
    • Alpha-v-beta3 integrin expression in melanocytic nevi and cutaneous melanoma
    • Neto D.S., Pantaleão L., Soares de Sá B.C., Landman G. Alpha-v-beta3 integrin expression in melanocytic nevi and cutaneous melanoma. J. Cutan. Pathol. 2007, 34:851-856.
    • (2007) J. Cutan. Pathol. , vol.34 , pp. 851-856
    • Neto, D.S.1    Pantaleão, L.2    Soares de Sá, B.C.3    Landman, G.4
  • 151
    • 0031983123 scopus 로고    scopus 로고
    • Stack intact vitronectin induces Matrix Metalloproteinase-2 and Tissue Inhibitor of Metalloproteinases-2 expression and enhanced cellular invasion by melanoma cells
    • Bafetti L.M., Young T.N., Itoh Y., Sharon M. Stack intact vitronectin induces Matrix Metalloproteinase-2 and Tissue Inhibitor of Metalloproteinases-2 expression and enhanced cellular invasion by melanoma cells. J. Biol. Chem. 1998, 273:143-149.
    • (1998) J. Biol. Chem. , vol.273 , pp. 143-149
    • Bafetti, L.M.1    Young, T.N.2    Itoh, Y.3    Sharon, M.4
  • 152
    • 0037155874 scopus 로고    scopus 로고
    • v subunit by Membrane Type 1 Matrix Metalloproteinase stimulates migration of breast carcinoma cells on vitronectin and enhances tyrosine phosphorylation of Focal Adhesion Kinase
    • v subunit by Membrane Type 1 Matrix Metalloproteinase stimulates migration of breast carcinoma cells on vitronectin and enhances tyrosine phosphorylation of Focal Adhesion Kinase. J. Biol. Chem. 2002, 277:9749-9756.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9749-9756
    • Deryugina, E.I.1    Ratnikov, B.I.2    Postnova, T.I.3    Rozanov, D.V.4    Strongin, A.Y.5
  • 154
    • 0030960367 scopus 로고    scopus 로고
    • The cell adhesion domain in plasma vitronecitn is cryptic
    • Seiffert D., Smith J.W. The cell adhesion domain in plasma vitronecitn is cryptic. J. Biol. Chem. 1997, 272:13705-13710.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13705-13710
    • Seiffert, D.1    Smith, J.W.2
  • 155
    • 0036510394 scopus 로고    scopus 로고
    • Incorporation of vitronectin into fibrin clots. Evidence for a binding interaction between vitronectin and gammaA/gamma' fibrinogen
    • Podor T.J., Campbell S., Chindemi P., Foulon D.M., Farrell D.H., Walton P.D., Weitz J.I., Peterson C.B. Incorporation of vitronectin into fibrin clots. Evidence for a binding interaction between vitronectin and gammaA/gamma' fibrinogen. J. Biol. Chem. 2002, 277:7520-7528.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7520-7528
    • Podor, T.J.1    Campbell, S.2    Chindemi, P.3    Foulon, D.M.4    Farrell, D.H.5    Walton, P.D.6    Weitz, J.I.7    Peterson, C.B.8
  • 156
    • 34447499051 scopus 로고    scopus 로고
    • The contributions of integrin affinity and integrin-cytoskeletal engagement in endothelial and smooth muscle cell adhesion to vitronectin
    • Stefansson S., Su E.J., Ishigami S., Cale J.M., Gao Y., Gorlatova N., Lawrence D.A. The contributions of integrin affinity and integrin-cytoskeletal engagement in endothelial and smooth muscle cell adhesion to vitronectin. J. Biol. Chem. 2007, 282:15679-15689.
    • (2007) J. Biol. Chem. , vol.282 , pp. 15679-15689
    • Stefansson, S.1    Su, E.J.2    Ishigami, S.3    Cale, J.M.4    Gao, Y.5    Gorlatova, N.6    Lawrence, D.A.7
  • 157
    • 0037365930 scopus 로고    scopus 로고
    • Cutaneous biology: early vitronectin receptor downregulation in a melanoma cell line during all-trans retinoic acid-induced apoptosis
    • Baroni A., Paoletti I., Silvestri I., Buommin E., Carriero M.V. Cutaneous biology: early vitronectin receptor downregulation in a melanoma cell line during all-trans retinoic acid-induced apoptosis. Br. J. Dermatol. 2003, 148:424-433.
    • (2003) Br. J. Dermatol. , vol.148 , pp. 424-433
    • Baroni, A.1    Paoletti, I.2    Silvestri, I.3    Buommin, E.4    Carriero, M.V.5


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