Reduction of Tumorigenicity by α³ Integrin in a Rhabdomyosarcoma Cell Line

References

• Albelda S. M., Mette S. A., Elder D. E., Stewart R., Damjanovich L., Herlyn M., Buck C. A. Integrin distribution in malignant melanoma: association of the (3, subunit with tumor progression. Cancer Res. 1990; 50: 6757–6764
   PubMed Web of Science ®Google Scholar
• Amchini A., Mortarini R., Supino R., Parmiani G. Human melanoma cells with high susceptibility fo cell-mediated lysis can be identified on the basis of 1CAM-1 phenotype. VLA profile, and invasive ability. Int. J. Cancer 1990; 46: 508–515
   PubMed Web of Science ®Google Scholar
• Bao Z. Z., Lakonishok M., Kaufman S., Horwitz A. F. α7β1 integrin is a component of the myotendinous junction of skeletal muscle. J. Cell. Sci. 1993; 106: 579–590
   PubMed Web of Science ®Google Scholar
• Berditchevski E, Bazzom G., Hemler M. E. Specific-association of CD63 with the VLA-3 and VLA-6 integrins. J. Biol. Chem. 1995; 270: 17784–17790
   PubMed Web of Science ®Google Scholar
• Carter W. G., Kaur P., Gil S. G., Gahr P. J., Wayner E. A. Distinct functions for integrins alpha3\betal in focal adhesions and alpha6beta4/bullous pemphigoid antigen in a new-stable anchoring contact (SAC) of keratinocytes: relation to hemidesmosome. J. Cell Biol. 1990a; 111: 3141–3154
   PubMed Web of Science ®Google Scholar
• Carter W. G., Wayner E. A., Bouchard T. S., Kaur P. The role of integrins a2(31 and a3(31 in cell-cell and cell-substrate adhesion of human epidermal cells. J. Cell Biol. 1990b; 110: 1387–1404
   PubMed Web of Science ®Google Scholar
• Carter W. G., Ryan M. C., Gahr P. J. Epiligrin, a new cell adhesion ligand for integrin α3β1 in epithelial basement membranes. Cell 1991; 65: 599–610
   PubMed Web of Science ®Google Scholar
• Chan B. M. C., Matsuura N., Takada Y., Zetter B. R., Hemler M. E. In vitro and in vivo consequences of VLA-2 expression on rhabdomyosarcoma cells. Science 1991; 251: 1600–1602
   PubMed Web of Science ®Google Scholar
• Chan B. M. C., Kassner P. D., Schiro J. A., Byers H. R., Kupper T. S., Hemler M. E. Distinct cellular functions mediated by different VLA integrin α subunit cytoplasmic domains. Cell 1992; 68: 1051–1060
   PubMed Web of Science ®Google Scholar
• Chan B. M. C., Hemler M. E. Multiple functional forms of the integrin VLA-2 derived from a single α2 cDNA clone: interconversion of the forms induced by an anti-β1, antibody. J. Cell Biol. 1993; 120: 537–543
   PubMed Web of Science ®Google Scholar
• Cho K. R., Oliner J. D., Simons J. W., Hednck L., Fearon E. R., Preisinger A. C., Hedge P., Silverman G. A., Vogelstein B. The DCC gene: structural analysis and mutations in colorectal carcinomas. Genomics 1994; 19: 525–531
   PubMed Web of Science ®Google Scholar
• Damsky C. H., Werb Z. Signal transduction by integrin receptors for extracellular matrix: cooperative processing of extracellular information. Curr Opin. Cell Biol. 1992; 4: 772–781
   PubMed Web of Science ®Google Scholar
• Dedhar S., Saulnier R., Nagle R., Overall C. M. Specific alterations in the expression of α3β, and α6β1 integrins in highly invasive and metastatic variants of human prostate carcinoma cells selected by in vitro invasion through recosntituted basement membrane. Clin. Exp. Metastasis 1993; 11: 391–400
   PubMed Web of Science ®Google Scholar
• Dedhar S., Saulnier R. Alterations in integrin receptor expression on chemically transformed human cells: specific enhancement of laminin and collagen receptor complexes. J. Cell Biol. 1990; 110: 481–489
   PubMed Web of Science ®Google Scholar
• Defreitas M. F., Yoshida C. K., Frazier W. A., Mendrick D. L., Kypta R. M., Reichardt L. F. Identification of integrin α3β1 as a neuronal thrombospondin receptor mediating neurite outgrowth. Neuron 1995; 15: 333–343
   PubMed Web of Science ®Google Scholar
• Dipersio C. M., Shah S., Hynes R. O. α3β1 integrin localizes to focal contacts in response to diverse extracellular matrix proteins. J. Cell Sci. 1995; 108: 2321–2336
   PubMed Web of Science ®Google Scholar
• Elices M. J., Urry L A., Helmer M. E. Receptor functions for the integrin VLA-3: fibronectin. collagen and laminin binding are differentially influenced by Arg-Gly-Asp peptide and by divalent cations. J. Cell Biol. 1991; 112: 169–181
   PubMed Web of Science ®Google Scholar
• Frixen U. H., Behrens J., Sachs M., Eberle G., Voss B., Warda A., Lochner D., Birchmeier W. E-cadherin-mediated cell-cell adhesion prevents invasiveness of human carcinoma cells. J. Cell Biol. 1991; 113: 173–185
   PubMed Web of Science ®Google Scholar
• Gehlsen K. R., Dillner L., Engvall E., Ruoslahti E. The human laminin receptor is a member of the integrin family of cell adhesion receptors. Science 1988; 24: 1228–1229
   Web of Science ®Google Scholar
• Gehlsen K. R., Davis G. E., Sriramarao P. Integrin expression in human melanoma cells with differing invasive and metastatic properties. Clin. Exp. Metastasis 1992; 10: 111–120
   PubMed Web of Science ®Google Scholar
• Giancotti F. G., Mainiero F. Integrin-mediated adhesion and signaling in tumorigenesis. Biochim. Biophxs. Acta 1994; 1198: 47–64
   PubMed Web of Science ®Google Scholar
• Giancotti F. G., Ruoslahti E. Elevated levels of the α5β1 fibronectin receptor suppress the transformed phenotype of Chinese hamster ovary cells. Cell 1990; 60: 849–859
   PubMed Web of Science ®Google Scholar
• Gladson C. L., Cheres D. A. Glioblastoma expression of vitronectin and the αvβ3, integrin. Adhesion mechanism for transformed glial cells. J. Clin. Invest. 1991; 88: 1924–1932
   PubMed Web of Science ®Google Scholar
• Hednck L., Cho K. R., Boyd J., Risinger J., Vogelstein B. DCC: a tumor suppressor gene expressed on the cell surface. CSH Symp. Quant. Biol. 1992; 57: 345–351
   PubMedGoogle Scholar
• Hemler M. E., Ware C. F., Strominger J. L. Characterization of a novel differentiation antigen complex recognized by a monoclonal antibody (A-1A5): unique activation-specific molecular forms on stimulated T cells. J. Immunol. 1983; 131: 334–340
   PubMed Web of Science ®Google Scholar
• Hemler M. E., Sánchez-Madrid F., Flotte T. J., Krensky A. M., Burakoff S. J., Bhan A. K., Springer T. A., Strominger J. L. Glycoproteins of 210.000 and 130.000 m.w. on activated T cells: cell distribution and antigenic relation to components on resting cells and T cell lines. J. Immunol. 1984; 132: 3011–3018
   PubMed Web of Science ®Google Scholar
• Higuchi R., Krummel B., Saiki R. K. A general method of in vitro preparation and specific mutagenesis of DNA fragments: studv of protein and DNA interactions. Nucl. Acids Res. 1988; 16: 7351–7367
   PubMed Web of Science ®Google Scholar
• Jensen P. J., Wheelock M. J. β1 integrins do not have a major role in keratinocyte intercellular adhesion. Exp. Cell Res. 1995; 219: 322–331
   PubMed Web of Science ®Google Scholar
• Juliano R. L., Varner J. A. Adhesion molecules in cancer: the role of integrins. Curr. Opin. Cell Biol. 1993; 5: 812–818
   PubMed Web of Science ®Google Scholar
• Kassner P. D., Alon R., Springer T. A., Hemler M. E. Specialized functional roles for the integrin α4 cytoplasmic domain. Mel. Biol. Cell 1995; 6: 661–674
   PubMed Web of Science ®Google Scholar
• Kassner P. D., Hemler M. E. Interchangeable alpha chain cytoplasmic domains physiopositive role in control of cell mediated by VLA-4. a β1, -integrin. J. Exp. Med. 1993; 178: 649–660
   PubMed Web of Science ®Google Scholar
• Koopman G., Keehnen R. M. J., Lindhout E., Newman W., Shimizu Y, Van Seventer G. A., de Groot C., Pals S. T. Adhesion through the LFA-1 (CD11a/CD18)-ICAM-1 (CD54) and the VLA-4- (CD49d)-VCAM-1 (CD106) pathways prevents apoptosis of germinal center B cells. J. Immunol. 1994; 152: 3760–3767
   PubMed Web of Science ®Google Scholar
• Lemke H., Hammerling G. J., Hohmann C., Rajewsky K. Hybrid cell lines secreting monoclonal antiboch specific for major histocompatibility antigens of the mouse. Nature 1978; 271: 249–251
   PubMed Web of Science ®Google Scholar
• Maselhs-Smith A., Shaw A. R. E. CD9-regulated adhesion: Anti-CD9 monoclonal antibody induce pre-B cell adhesion to bone marrow fibroblasts through de novo recognition of fibronectin. J. Immunol. 1994; 152: 2768–2777
   PubMed Web of Science ®Google Scholar
• McDonald K. A., Lakonishok M., Horwitz A. F. α1 and α3 integrin subumts are associated with myofibrils during myofibrillogenesis. J. Cell Sci. 1995; 108: 975–983
   PubMed Web of Science ®Google Scholar
• McNamee H. P., Ingber D. E., Schwartz M. A. Adhesion to fibronectin stimulates inositol lipid synthesis and enhances PDGF-induced inositol lipid breakdown. J. Cell Biol. 1993; 121: 673–678
   PubMed Web of Science ®Google Scholar
• Mechtersheimer G., Barth T., Quentmeier A., Moller P. Differential expression of pi integrins in nonneoplastic smooth and striated muscle cells and in tumors derived from these cells. Am. J. Pathol. 1994; 144: 1172–1182
   PubMed Web of Science ®Google Scholar
• Meredith J. E., Jr., Fazeli B., Schwartz M. A. The extracellular matrix as a cell survival factor. Mol. Biol. Cell 1993; 4: 953–961
   PubMed Web of Science ®Google Scholar
• Nakamura K., Iwamoto R., Mekada E. Membrane-anchored heparin-binding EGF-like growth factor (HB-EGF) and diptheria toxin receptor-associated protein (DRAP27)/CD9 form a complex with integrin α3β1 at cell-cell contact sites. J. Cell Biol. 1995; 129: 1691–1705
   PubMed Web of Science ®Google Scholar
• Natah P. G., Nicotra M. R., Bartolazzi A., Cavaliere R., Bigotti A. Integrin expression in cutaneous malignant melanoma: association of the α3β1 heterodimer with tumor progression. Int. J. Cancer 1993; 54: 68–72
   PubMed Web of Science ®Google Scholar
• Nip J., Shibata H., Loskutoff D. J., Cheresh D. A., Brodi P. Human melanoma cells derived from lymphatic metastases use integrin αvβ3 to adhere to lymph node vitronectin. J. Clin. Invest. 1992; 90: 1406–1413
   PubMed Web of Science ®Google Scholar
• Ohashi P., Mak T. W., Van den Elsen P., Yanagi Y., Yoslukai Y., Caiman A. F., Terhorst C., Stobo J. D., Weiss A. Reconstitution of an active surface T3/T-cell antigen receptor by DNA transfer. Nature 1985; 316: 606–609
   PubMed Web of Science ®Google Scholar
• Paulus W., Baur I., Schuppan D., Roggendorf W. Characterization of integrin receptors in normal and neoplastic human brain. Am. J. Pathol. 1993; 143: 154–163
   PubMed Web of Science ®Google Scholar
• Peifer M. Cancer, catenins and cuticle pattern: a complex connection. Science 1993; 262: 1667–1668
   PubMed Web of Science ®Google Scholar
• Plantefaber L. C., Hynes R. O. Changes in integrin receptors on oncogenically transformed cells. Cell 1989; 56: 281–290
   PubMed Web of Science ®Google Scholar
• Qian F., Vaux D. L., Weissman I. L. Expression of the integrin α4β1 on melanoma cells can inhibit the invasive stage of metastasis formation. Cell 1994; 77: 335–347
   PubMed Web of Science ®Google Scholar
• Raz A., Ben-Ze'ev A. Cell-contact and architecture of malignant cells and their relationship to metastasis. Cancer and Metastasis Reviews 1987; 6: 3–21
   PubMed Web of Science ®Google Scholar
• Retlig W. J., Old L. J. Immunogeneties of human cell surface differentiation. Ann. Rev. Immunol. 1989; 7: 481–511
   PubMed Web of Science ®Google Scholar
• Rousselle P., Lunstrum G. P., Keene D. R., Burgeson R. E. Kalinin: an epithelium-specific basement membrane adhesion molecule that is a component of anchoring filaments. J. Cell Biol. 1991; 114: 567–576
   PubMed Web of Science ®Google Scholar
• Rubinfeld B., Souza B., Albert I., Muller O., Chamberlain S. H., Masiarz F. R., Munemitsu S., Polakis P. Association of the APC gene product with β-catenin. Science 1993; 262: 1731–1734
   PubMed Web of Science ®Google Scholar
• Ruoslahti E., Giancotti F G. Integrins and tumor cell dissemination. Cancer Cells 1989; 1: 119–126
   PubMed Web of Science ®Google Scholar
• Sager R., Anisowicz A., Neveu M., Liang P., Sotiropoulou G. Identification by differential display of α6 integrin as a candidate tumor suppressor gene. FASEB J. 1993; 7: 964–970
   PubMed Web of Science ®Google Scholar
• Saito T., Weiss A., Miller J., Norcross M. A., Germain R. N. Specific antigen-la activation of transfected human T cells expressing Ti αβ-human T3 receptor complexes. Nature 1987; 325: 125–130
   PubMed Web of Science ®Google Scholar
• Schreiner C., Fisher M, Hussein S., Juliano R. L. Increased tumorigenicity of fibronectin receptor deficient Chinese hamster ovary cell variants. Cancer Res. 1991; 51: 1738–1740
   PubMed Web of Science ®Google Scholar
• Schwartz M. A. Signaling by integrins: Implications for tumongenesis. Cancer Res. 1993; 53: 1503–1506
   PubMed Web of Science ®Google Scholar
• Shin S. I., Freedman V. H., Risser R., Pollack R. Tumorigenicity of virus-transformed cells in nude mice is correlated specifically with anchorage-independent growth. in vitro. Proc. Natl. Acad. Sci. USA 1975; 72: 4435–4439
   PubMed Web of Science ®Google Scholar
• Sriramarao P., Steffner P., Gehlsen K. R. Biochemical evidence for a homophilic interaction of the α3B1 integrin. J. Biol. Chem. 1993; 268: 22036–22041
   PubMed Web of Science ®Google Scholar
• Stoker M., O'Neill C., Berryman S., Waxman V. Anchorage and growth regulation in normal and virus-transformed cells. Intl. J. Cancer 1968; 3: 683–693
   PubMed Web of Science ®Google Scholar
• Su L. K., Vogelstem B., Kinzler K. W. Association of the APC tumor suppressor gene with catenins. Science 1993; 262: 1734–1737
   PubMed Web of Science ®Google Scholar
• Symington B. E., Takada Y., Carter W. G. Interaction of integrins α3βl and α2βl: Potential role in keratinocyte intercellular adhesion. J. Cell Biol. 1993; 120: 523–535
   PubMed Web of Science ®Google Scholar
• Takada Y, Murphy E., Pil P., Chen C., Ginsberg M. H., Hemler M. E. Molecular cloning and expression of the cDNA for the α3 chain of human α3βl (VLA-3), an integrin receptor for fibronectin, laminin and collagen. J. Cell Biol. 1991; 115: 257–266
   PubMed Web of Science ®Google Scholar
• Takada Y, Hemler M. E. The primary structure of the VLA-2/collagen receptor α2 subunit (platelet GP Ia): homology to other integrins and the presence of a possible collagen-binding domain. J. Cell Biol. 1989; 109: 397–407
   PubMed Web of Science ®Google Scholar
• Tenchini M. L., Adams J. C., Gilberty C., Steel J., Hudson D. L., Malcovati M., Watt F M. Evidence against a major role for integrin in calcium dependent intercellular adhesion of epidermal keratinoevtes. Cell Adh. & Comm. 1993; 1: 55–66
   PubMedGoogle Scholar
• Toothill V. J., van Mourik J. A., Nieuwenhuis H. K., Metzelaar M. J., Pearson J. D. Chaiacterization of the enhanced adhesion of neutrophil leukocytes to thrombin-stimulated endothelial cells. J. Immunol. 1990; 145: 283–291
   PubMed Web of Science ®Google Scholar
• Tsuji T., Hakomori S., Osawa T. Identification of human galactoprotein b3, an oncogenic transformation-induced membrane glycoprotein, as VLA-3 α subunit: the primary structure of human integrin α3. J. Biochem 1991; 109: 659–665
   PubMed Web of Science ®Google Scholar
• Varner J. A., Emerson D. A., Juliano R. L. Integrin a5(31 expression negatively regulates cell growth-reversal by attachment to fibronectin. Mol. Biol. Cell 1995; 6: 725–740
   PubMed Web of Science ®Google Scholar
• Vleminckx K., Vakaet L., Mareel M., Fiers W., van Roy F. Genetic manipulation of E-cadherin expression by epithelial tumor cells reveals an invasion suppressor role. Cell 1991; 66: 107–119
   PubMed Web of Science ®Google Scholar
• Wayner E. A., Carter W. G. Identification of multiple cell adhesion receptors for collagen and fibronectin in human fibrosarcoma cells possessing unique alpha and common beta subunits. J. Cell Biol. 1987; 105: 1873–1884
   PubMed Web of Science ®Google Scholar
• Weinel R. J., Rosendahl A., Neumann K., Chaloupka B., Erb D., Rothmund M., Santoso S. Expression and function of VLA-α2, -α3, α5, and -α6 integrin receptors in pancreatic carcinoma. Int. J. Cancer 1992; 52: 827–833
   PubMed Web of Science ®Google Scholar
• Weitzman J. B., Pasqualini R., Takada Y., Hemler M. E. The function and distinctive regulation of the integrin VLA-3 in cell adhesion, spreading and homotypic cell aggregation. J. Biol. Chem. 1993; 268: 8651–8657
   PubMed Web of Science ®Google Scholar
• Weitzman J. B., Chen A., Hemler M. E. Investigation of the role of p, integrins in cell-cell adhesion. J. Cell Sci. 1995; 108: 3635–3644
   PubMed Web of Science ®Google Scholar
• Werb Z., Tremble P. M., Behrendtsen O., Crowley E., Damsky C. H. Signal transduction through the fibronectin receptor induces collagenase and stromelysin gene expression. J. Cell Biol. 1989; 109: 877–889
   PubMed Web of Science ®Google Scholar
• Wu C. Y., Chung A. E., McDonald J. A. A novel role for α3β1 integrins in extracellular matrix assembly. J. Cell Sci. 1995; 108: 2511–2523
   PubMed Web of Science ®Google Scholar
• Zutter M. M., Santoro S. A., Staatz W. D., Tsung Y. L. Re-expression of the a2pSl integrin abrogates the malignant phe-notype o breast carcinoma cells. Proc. Natl. Acad. Sci. USA 1995; 92: 7411–7415
   PubMed Web of Science ®Google Scholar