메뉴 건너뛰기




Volumn 322, Issue 2, 2014, Pages 249-264

Glycosylation of the laminin receptor (α3β1) regulates its association with tetraspanin CD151: Impact on cell spreading, motility, degradation and invasion of basement membrane by tumor cells

Author keywords

Basement membrane; Integrin 3 1; Invasion; Metastasis; Tetraspanin CD151; 1,6 branched N linked oligosaccharides

Indexed keywords

CD151 ANTIGEN; FIBRONECTIN; FIBRONECTIN ALPHA5 BETA1; GELATINASE B; LAMININ; LAMININ ALPHA3 BETA1; LAMININ RECEPTOR; MATRIGEL; OLIGOSACCHARIDE; TETRASPANIN; UNCLASSIFIED DRUG;

EID: 84896038546     PISSN: 00144827     EISSN: 10902422     Source Type: Journal    
DOI: 10.1016/j.yexcr.2014.02.004     Document Type: Article
Times cited : (27)

References (59)
  • 2
    • 0026584068 scopus 로고
    • Invasion and metastasis
    • Steeg P.S. Invasion and metastasis. Curr. Opin. Oncol. 1992, 4:134-141.
    • (1992) Curr. Opin. Oncol. , vol.4 , pp. 134-141
    • Steeg, P.S.1
  • 3
    • 0141988559 scopus 로고    scopus 로고
    • Molecular mechanisms of tumor invasion and metastasis: an integrated view
    • Cairns R.A., Khokha R., Hill R.P. Molecular mechanisms of tumor 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
  • 4
    • 0036990103 scopus 로고    scopus 로고
    • The organ microenvironment and cancer metastasis
    • Fidler I.J. The organ microenvironment and cancer metastasis. Differentiation 2002, 70:498-505.
    • (2002) Differentiation , vol.70 , pp. 498-505
    • Fidler, I.J.1
  • 6
    • 34447255472 scopus 로고    scopus 로고
    • The role of the organ microenvironment in the biology and therapy of cancer metastasis
    • Fidler I.J., Kim S.J., Langley R.R. The role of the organ microenvironment in the biology and therapy of cancer metastasis. J. Cell. Biochem. 2007, 101:927-936.
    • (2007) J. Cell. Biochem. , vol.101 , pp. 927-936
    • Fidler, I.J.1    Kim, S.J.2    Langley, R.R.3
  • 7
    • 0031655802 scopus 로고    scopus 로고
    • Multistep nature of metastatic inefficiency: dormancy of solitary cells after successful extravasation and limited survival of early micrometastases
    • Luzzi K.J., MacDonald I.C., Schmidt E.E., Kerkvliet N., Morris V.L., Chambers A.F., Groom A.C. Multistep nature of metastatic inefficiency: dormancy of solitary cells after successful extravasation and limited survival of early micrometastases. Am. J. Pathol. 1998, 153:865-873.
    • (1998) Am. J. Pathol. , vol.153 , pp. 865-873
    • Luzzi, K.J.1    MacDonald, I.C.2    Schmidt, E.E.3    Kerkvliet, N.4    Morris, V.L.5    Chambers, A.F.6    Groom, A.C.7
  • 8
    • 0027140406 scopus 로고
    • Extracellular matrix 6: role of matrix metalloproteinases in tumor invasion and metastasis
    • Stetler-Stevenson W.G., Liotta L.A., Kleiner D.E. Extracellular matrix 6: role of matrix metalloproteinases in tumor invasion and metastasis. FASEB J. 1993, 7:1434-1441.
    • (1993) FASEB J. , vol.7 , pp. 1434-1441
    • Stetler-Stevenson, W.G.1    Liotta, L.A.2    Kleiner, D.E.3
  • 9
    • 0023255440 scopus 로고
    • Beta 1-6 branching of Asn-linked oligosaccharides is directly associated with metastasis
    • Dennis J.W., Laferte S., Waghorne C., Breitman M.L., Kerbel R.S. Beta 1-6 branching of Asn-linked oligosaccharides is directly associated with metastasis. Science 1987, 236:582-585.
    • (1987) Science , vol.236 , pp. 582-585
    • Dennis, J.W.1    Laferte, S.2    Waghorne, C.3    Breitman, M.L.4    Kerbel, R.S.5
  • 10
    • 0024435241 scopus 로고
    • Evidence that beta 1-6 branched Asn-linked oligosaccharides on metastatic tumor cells facilitate invasion of basement membranes
    • Yagel S., Feinmesser R., Waghorne C., Lala P.K., Breitman M.L., Dennis J.W. Evidence that beta 1-6 branched Asn-linked oligosaccharides on metastatic tumor cells facilitate invasion of basement membranes. Int. J. Cancer 1989, 44:685-690.
    • (1989) Int. J. Cancer , vol.44 , pp. 685-690
    • Yagel, S.1    Feinmesser, R.2    Waghorne, C.3    Lala, P.K.4    Breitman, M.L.5    Dennis, J.W.6
  • 11
    • 0035698304 scopus 로고    scopus 로고
    • N-Acetylglucosaminyltransferase V as a possible aid for the evaluation of tumor invasiveness in patients with hepatocellular carcinoma
    • Yanagi M., Aoyagi Y., Suda T., Mita Y., Asakura H. N-Acetylglucosaminyltransferase V as a possible aid for the evaluation of tumor invasiveness in patients with hepatocellular carcinoma. J. Gastroenterol. Hepatol. 2001, 16:1282-1289.
    • (2001) J. Gastroenterol. Hepatol. , vol.16 , pp. 1282-1289
    • Yanagi, M.1    Aoyagi, Y.2    Suda, T.3    Mita, Y.4    Asakura, H.5
  • 16
    • 0028981092 scopus 로고
    • The alpha-glucosidase I inhibitor castanospermine alters endothelial cell glycosylation, prevents angiogenesis, and inhibits tumor growth
    • Pili R., Chang J., Partis R.A., Mueller R.A., Chrest F.J., Passaniti A. The alpha-glucosidase I inhibitor castanospermine alters endothelial cell glycosylation, prevents angiogenesis, and inhibits tumor growth. Cancer Res. 1995, 55:2920-2926.
    • (1995) Cancer Res. , vol.55 , pp. 2920-2926
    • Pili, R.1    Chang, J.2    Partis, R.A.3    Mueller, R.A.4    Chrest, F.J.5    Passaniti, A.6
  • 17
    • 0026014062 scopus 로고
    • Beta 1-6 branched oligosaccharides as a marker of tumor progression in human breast and colon neoplasia
    • Fernandes B., Sagman U., Auger M., Demetrio M., Dennis J.W. Beta 1-6 branched oligosaccharides as a marker of tumor progression in human breast and colon neoplasia. Cancer Res. 1991, 51:718-723.
    • (1991) Cancer Res. , vol.51 , pp. 718-723
    • Fernandes, B.1    Sagman, U.2    Auger, M.3    Demetrio, M.4    Dennis, J.W.5
  • 18
    • 0025254569 scopus 로고
    • Increase of beta 1-6-branched oligosaccharides in human esophageal carcinomas invasive against surrounding tissue in vivo and in vitro
    • Takano R., Nose M., Nishihira T., Kyogoku M. Increase of beta 1-6-branched oligosaccharides in human esophageal carcinomas invasive against surrounding tissue in vivo and in vitro. Am. J. Pathol. 1990, 137:1007-1011.
    • (1990) Am. J. Pathol. , vol.137 , pp. 1007-1011
    • Takano, R.1    Nose, M.2    Nishihira, T.3    Kyogoku, M.4
  • 19
    • 34547844244 scopus 로고    scopus 로고
    • Identification of proteins bearing beta1-6 branched N-glycans in human melanoma cell lines from different progression stages by tandem mass spectrometry analysis
    • Przybylo M., Martuszewska D., Pochec E., Hoja-Lukowicz D., Litynska A. Identification of proteins bearing beta1-6 branched N-glycans in human melanoma cell lines from different progression stages by tandem mass spectrometry analysis. Biochim. Biophys. Acta 2007, 1770:1427-1435.
    • (2007) Biochim. Biophys. Acta , vol.1770 , pp. 1427-1435
    • Przybylo, M.1    Martuszewska, D.2    Pochec, E.3    Hoja-Lukowicz, D.4    Litynska, A.5
  • 20
    • 0018828414 scopus 로고
    • In vitro selection of murine B16 melanoma variants with enhanced tissue-invasive properties
    • Poste G., Doll J., Hart I.R., Fidler I.J. In vitro selection of murine B16 melanoma variants with enhanced tissue-invasive properties. Cancer Res. 1980, 40:1636-1644.
    • (1980) Cancer Res. , vol.40 , pp. 1636-1644
    • Poste, G.1    Doll, J.2    Hart, I.R.3    Fidler, I.J.4
  • 21
    • 33748677966 scopus 로고    scopus 로고
    • Sialilated beta1,6 branched N-oligosaccharides modulate adhesion, chemotaxis and motility of melanoma cells: effect on invasion and spontaneous metastasis properties
    • Reddy B.V., Kalraiya R.D. Sialilated beta1,6 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.1    Kalraiya, R.D.2
  • 22
    • 0029021007 scopus 로고
    • Reduced contact-inhibition and substratum adhesion in epithelial cells expressing GlcNAc-transferase V
    • Demetriou M., Nabi I.R., Coppolino M., Dedhar 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    Dedhar, S.4    Dennis, J.W.5
  • 23
    • 0036894568 scopus 로고    scopus 로고
    • Aberrant N-glycosylation of beta1 integrin causes reduced alpha5beta1 integrin clustering and stimulates cell migration
    • Guo H.B., Lee I., Kamar M., Akiyama S.K., Pierce M. Aberrant N-glycosylation of beta1 integrin causes reduced alpha5beta1 integrin clustering and stimulates cell migration. Cancer Res. 2002, 62:6837-6845.
    • (2002) Cancer Res. , vol.62 , pp. 6837-6845
    • Guo, H.B.1    Lee, I.2    Kamar, M.3    Akiyama, S.K.4    Pierce, M.5
  • 24
    • 0029027831 scopus 로고
    • Suppression of lung metastasis of B16 mouse melanoma by N-acetylglucosaminyltransferase III gene transfection
    • Yoshimura M., Nishikawa A., Ihara Y., Taniguchi S., Taniguchi N. Suppression of lung metastasis of B16 mouse melanoma by N-acetylglucosaminyltransferase III gene transfection. Proc. Natl. Acad. Sci. USA 1995, 92:8754-8758.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8754-8758
    • Yoshimura, M.1    Nishikawa, A.2    Ihara, Y.3    Taniguchi, S.4    Taniguchi, N.5
  • 26
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: bidirectional, allosteric signaling machines
    • Hynes R.O. Integrins: bidirectional, allosteric signaling machines. Cell 2002, 110:673-687.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 27
    • 33748306120 scopus 로고    scopus 로고
    • Integrin structures and conformational signaling
    • Luo B.H., Springer T.A. Integrin structures and conformational signaling. Curr. Opin. Cell Biol. 2006, 18:579-586.
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 579-586
    • Luo, B.H.1    Springer, T.A.2
  • 28
    • 0035207920 scopus 로고    scopus 로고
    • Complexes of tetraspanins with integrins: more than meets the eye
    • Berditchevski F. Complexes of tetraspanins with integrins: more than meets the eye. J. Cell Sci. 2001, 114:4143-4151.
    • (2001) J. Cell Sci. , vol.114 , pp. 4143-4151
    • Berditchevski, F.1
  • 29
    • 57749169272 scopus 로고    scopus 로고
    • Tetraspanins: push and pull in suppressing and promoting metastasis
    • Zoller M. Tetraspanins: push and pull in suppressing and promoting metastasis. Nat. Rev. Cancer 2009, 9:40-55.
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 40-55
    • Zoller, M.1
  • 30
    • 51049122842 scopus 로고    scopus 로고
    • Targeting of tetraspanin proteins-potential benefits and strategies
    • Hemler M.E. Targeting of tetraspanin proteins-potential benefits and strategies. Nat. Rev. Drug Discov. 2008, 7:747-758.
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 747-758
    • Hemler, M.E.1
  • 32
    • 77953064012 scopus 로고    scopus 로고
    • Laminin-binding integrins and their tetraspanin partners as potential antimetastatic targets
    • Stipp C.S. Laminin-binding integrins and their tetraspanin partners as potential antimetastatic targets. Expert Rev. Mol. Med. 2010, 12:e3.
    • (2010) Expert Rev. Mol. Med. , vol.12
    • Stipp, C.S.1
  • 35
    • 0034731368 scopus 로고    scopus 로고
    • Glycosylation effect on membrane domain (GEM) involved in cell adhesion and motility: a preliminary note on functional alpha3, alpha5-CD82 glycosylation complex in ldlD 14 cells
    • Ono M., Handa K., Withers D.A., Hakomori S. Glycosylation effect on membrane domain (GEM) involved in cell adhesion and motility: a preliminary note on functional alpha3, alpha5-CD82 glycosylation complex in ldlD 14 cells. Biochem. Biophys. Res. Commun. 2000, 279:744-750.
    • (2000) Biochem. Biophys. Res. Commun. , vol.279 , pp. 744-750
    • Ono, M.1    Handa, K.2    Withers, D.A.3    Hakomori, S.4
  • 36
    • 64149125582 scopus 로고    scopus 로고
    • Poly N-acetyllactosamine substitutions on N- and not O-oligosaccharides or Thomsen-Friedenreich antigen facilitate lung specific metastasis of melanoma cells via galectin-3
    • Srinivasan N., Bane S.M., Ahire S.D., Ingle A.D., Kalraiya R.D. Poly N-acetyllactosamine substitutions on N- and not O-oligosaccharides or Thomsen-Friedenreich antigen facilitate lung specific metastasis of melanoma cells via galectin-3. Glycoconj. J. 2009, 26:445-456.
    • (2009) Glycoconj. J. , vol.26 , pp. 445-456
    • Srinivasan, N.1    Bane, S.M.2    Ahire, S.D.3    Ingle, A.D.4    Kalraiya, R.D.5
  • 37
    • 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
  • 38
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • Peterson G.L. A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal. Biochem. 1977, 83:346-356.
    • (1977) Anal. Biochem. , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 39
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 40
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications
    • Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 1979, 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 41
    • 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
  • 42
    • 0031034352 scopus 로고    scopus 로고
    • Integrin-ligand binding properties govern cell migration speed through cell-substratum adhesiveness
    • Palecek S.P., Loftus J.C., Ginsberg M.H., Lauffenburger D.A., Horwitz A.F. Integrin-ligand binding properties govern cell migration speed through cell-substratum adhesiveness. Nature 1997, 385:537-540.
    • (1997) Nature , vol.385 , pp. 537-540
    • Palecek, S.P.1    Loftus, J.C.2    Ginsberg, M.H.3    Lauffenburger, D.A.4    Horwitz, A.F.5
  • 43
    • 0029066887 scopus 로고
    • Increased glycosylation of beta 1 integrins affects the interaction of transformed S115 mammary epithelial cells with laminin-1
    • Leppa S., Heino J., Jalkanen M. Increased glycosylation of beta 1 integrins affects the interaction of transformed S115 mammary epithelial cells with laminin-1. Cell Growth Differ. 1995, 6:853-861.
    • (1995) Cell Growth Differ. , vol.6 , pp. 853-861
    • Leppa, S.1    Heino, J.2    Jalkanen, M.3
  • 44
    • 0028239080 scopus 로고
    • Functional role of N-glycosylation in alpha 5 beta 1 integrin receptor. De-N-glycosylation induces dissociation or altered association of alpha 5 and beta 1 subunits and concomitant loss of fibronectin binding activity
    • Zheng M., Fang H., Hakomori S. Functional role of N-glycosylation in alpha 5 beta 1 integrin receptor. De-N-glycosylation induces dissociation or altered association of alpha 5 and beta 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
  • 45
    • 33845922350 scopus 로고    scopus 로고
    • N-glycosylation of the beta-propeller domain of the integrin alpha5 subunit is essential for alpha5beta1 heterodimerization, expression on the cell surface, and its biological function
    • Isaji T., Sato Y., Zhao Y., Miyoshi E., Wada Y., Taniguchi N., Gu J. N-glycosylation of the beta-propeller domain of the integrin alpha5 subunit is essential for alpha5beta1 heterodimerization, expression on the cell surface, and its biological function. J. Biol. Chem. 2006, 281:33258-33267.
    • (2006) J. Biol. Chem. , vol.281 , pp. 33258-33267
    • Isaji, T.1    Sato, Y.2    Zhao, Y.3    Miyoshi, E.4    Wada, Y.5    Taniguchi, N.6    Gu, J.7
  • 46
    • 2442450486 scopus 로고    scopus 로고
    • Introduction of bisecting GlcNAc into integrin alpha5beta1 reduces ligand binding and down-regulates cell adhesion and cell migration
    • Isaji T., Gu J., Nishiuchi R., Zhao Y., Takahashi M., Miyoshi E., Honke K., Sekiguchi K., Taniguchi N. Introduction of bisecting GlcNAc into integrin alpha5beta1 reduces ligand binding and down-regulates cell adhesion and cell migration. J. Biol. Chem. 2004, 279:19747-19754.
    • (2004) J. Biol. Chem. , vol.279 , pp. 19747-19754
    • Isaji, T.1    Gu, J.2    Nishiuchi, R.3    Zhao, Y.4    Takahashi, M.5    Miyoshi, E.6    Honke, K.7    Sekiguchi, K.8    Taniguchi, N.9
  • 47
    • 33845629320 scopus 로고    scopus 로고
    • Increase in beta1-6 GlcNAc branching caused by N-acetylglucosaminyltransferase V directs integrin beta1 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 beta1-6 GlcNAc branching caused by N-acetylglucosaminyltransferase V directs integrin beta1 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
  • 48
    • 0029958564 scopus 로고    scopus 로고
    • Distinct alpha 7A beta 1 and alpha 7B beta 1 integrin expression patterns during mouse development: alpha 7A is restricted to skeletal muscle but alpha 7B is expressed in striated muscle, vasculature, and nervous system
    • Velling T., Collo G., Sorokin L., Durbeej M., Zhang H., Gullberg D. Distinct alpha 7A beta 1 and alpha 7B beta 1 integrin expression patterns during mouse development: alpha 7A is restricted to skeletal muscle but alpha 7B is expressed in striated muscle, vasculature, and nervous system. Dev. Dyn. 1996, 207:355-371.
    • (1996) Dev. Dyn. , vol.207 , pp. 355-371
    • Velling, T.1    Collo, G.2    Sorokin, L.3    Durbeej, M.4    Zhang, H.5    Gullberg, D.6
  • 49
    • 0033158929 scopus 로고    scopus 로고
    • Expression of the alpha7beta1 laminin receptor suppresses melanoma growth and metastatic potential
    • Ziober B.L., Chen Y.Q., Ramos D.M., Waleh N., Kramer R.H. Expression of the alpha7beta1 laminin receptor suppresses melanoma growth and metastatic potential. Cell Growth Differ. 1999, 10:479-490.
    • (1999) Cell Growth Differ. , vol.10 , pp. 479-490
    • Ziober, B.L.1    Chen, Y.Q.2    Ramos, D.M.3    Waleh, N.4    Kramer, R.H.5
  • 50
    • 0027406446 scopus 로고
    • Functionally distinct roles for glycosylation of alpha and beta integrin chains in cell-matrix interactions
    • Chammas R., Veiga S.S., Travassos L.R., Brentani R.R. Functionally distinct roles for glycosylation of alpha and beta integrin chains in cell-matrix interactions. Proc. Natl. Acad. Sci. USA 1993, 90:1795-1799.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1795-1799
    • Chammas, R.1    Veiga, S.S.2    Travassos, L.R.3    Brentani, R.R.4
  • 51
    • 79551530752 scopus 로고    scopus 로고
    • Integrin alpha5beta1 facilitates cancer cell invasion through enhanced contractile forces
    • Mierke C.T., Frey B., Fellner M., Herrmann M., Fabry B. Integrin alpha5beta1 facilitates cancer cell invasion through enhanced contractile forces. J. Cell Sci. 2011, 124:369-383.
    • (2011) J. Cell Sci. , vol.124 , pp. 369-383
    • Mierke, C.T.1    Frey, B.2    Fellner, M.3    Herrmann, M.4    Fabry, B.5
  • 52
    • 0027095748 scopus 로고
    • Altered glycosylation and cell surface expression of beta 1 integrin receptors during keratinocyte activation
    • Kim L.T., Ishihara S., Lee C.C., Akiyama S.K., Yamada K.M., Grinnell F. Altered glycosylation and cell surface expression of beta 1 integrin receptors during keratinocyte activation. J. Cell Sci. 1992, 103(Pt. 3):743-753.
    • (1992) J. Cell Sci. , vol.103 , Issue.PART. 3 , pp. 743-753
    • Kim, L.T.1    Ishihara, S.2    Lee, C.C.3    Akiyama, S.K.4    Yamada, K.M.5    Grinnell, F.6
  • 53
    • 0034257182 scopus 로고    scopus 로고
    • Inverse correlation between KAI1 mRNA levels and invasive behaviour in bladder cancer cell lines
    • Jackson P., Kingsley E.A., Russell P.J. Inverse correlation between KAI1 mRNA levels and invasive behaviour in bladder cancer cell lines. Cancer Lett. 2000, 156:9-17.
    • (2000) Cancer Lett. , vol.156 , pp. 9-17
    • Jackson, P.1    Kingsley, E.A.2    Russell, P.J.3
  • 54
    • 0033563224 scopus 로고    scopus 로고
    • Selective tetraspan-integrin complexes (CD81/alpha4beta1, CD151/alpha3beta1, CD151/alpha6beta1) under conditions disrupting tetraspan interactions
    • Serru V., Le Naour F., Billard M., Azorsa D.O., Lanza F., Boucheix C., Rubinstein E. Selective tetraspan-integrin complexes (CD81/alpha4beta1, CD151/alpha3beta1, CD151/alpha6beta1) under conditions disrupting tetraspan interactions. Biochem. J. 1999, 340(Pt. 1):103-111.
    • (1999) Biochem. J. , vol.340 , Issue.PART. 1 , pp. 103-111
    • Serru, V.1    Le Naour, F.2    Billard, M.3    Azorsa, D.O.4    Lanza, F.5    Boucheix, C.6    Rubinstein, E.7
  • 56
    • 1542328915 scopus 로고    scopus 로고
    • Extracellular alpha 6 integrin cleavage by urokinase-type plasminogen activator in human prostate cancer
    • Demetriou M.C., Pennington M.E., Nagle R.B., Cress A.E. Extracellular alpha 6 integrin cleavage by urokinase-type plasminogen activator in human prostate cancer. Exp. Cell Res. 2004, 294:550-558.
    • (2004) Exp. Cell Res. , vol.294 , pp. 550-558
    • Demetriou, M.C.1    Pennington, M.E.2    Nagle, R.B.3    Cress, A.E.4
  • 57
    • 0027211896 scopus 로고
    • Expression of complete keratin filaments in mouse L cells augments cell migration and invasion
    • Chu Y.W., Runyan R.B., Oshima R.G., Hendrix M.J. Expression of complete keratin filaments in mouse L cells augments cell migration and invasion. Proc. Natl. Acad. Sci. USA 1993, 90:4261-4265.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4261-4265
    • Chu, Y.W.1    Runyan, R.B.2    Oshima, R.G.3    Hendrix, M.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.