Characterization of mouse integrin α3 subunit gene

Journal of Biochemistry

Volumn 125, Issue 6, 1999, Pages 1183-1188

  Tsuji, Tsutomu ^a,b   Han, Seon Ae ^a   Takeuchi, Ken Ichi ^a,e   Takahashi, Naoki ^c   Hakomori, Sen Itiroh ^d   Irimura, Tatsuro ^a  

^a UNIVERSITY OF TOKYO   (Japan)

^b HOSHI UNIVERSITY   (Japan)

^c NARA INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

^d UNIVERSITY OF WASHINGTON   (United States)

^e TOKYO METROPOLITAN INSTITUTE OF MEDICAL SCIENCE   (Japan)

Author keywords

Adhesion molecule; Genomic cloning; Integrin; Oncogenic transformation; Very late antigen

Indexed keywords

CELL ADHESION MOLECULE; INTEGRIN; LAMININ; LUCIFERASE; MESSENGER RNA; RECEPTOR; SCLEROPROTEIN; VERY LATE ACTIVATION ANTIGEN 3;

ALPHA CHAIN; ANIMAL CELL; ARTICLE; EXON; FIBROBLAST; FLOW CYTOMETRY; GENE EXPRESSION; GENE STRUCTURE; GENETIC TRANSFECTION; GENETIC TRANSFORMATION; HAMSTER; HUMAN; HUMAN CELL; INTRON; MOUSE; NONHUMAN; ONCOVIRINAE; POLYOMA VIRUS; PROMOTER REGION; PROTEIN DOMAIN; PROTEIN EXPRESSION; RNA SPLICING; SIMIAN VIRUS 40; TUMOR CELL LINE; VIRUS ONCOGENE;

ANIMALIA; CRICETINAE; ONCOVIRINAE; POLYOMAVIRUS; RODENTIA; SIMIAE; SIMIAN VIRUS; SIMIAN VIRUS 40; TUMOR VIRUS;

EID: 0344731153     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022402     Document Type: Article

References (42)

1. Carter, W.G., Ryan, M.C., and Gahr, P.J. (1991) Epiligrin, a new cell adhesion ligand for integrin α3β1 in epithelial basement membranes. Cell 65, 599-610
2. Marinkovitch, M.P., Verrando, P., Keene, D.R., Meneguzzi, G., Lunstrum, G.P., Ortonne, J.P., and Burgeson, R.E. (1993) Basement membrane proteins kalinin and nicein are structurally and immunologically identical. Lab. Invest. 69, 295-299
3. Kikkawa, Y., Umeda, M., and Miyazaki, K. (1994) Marked stimulation of cell adhesion and motility by ladsin, a laminin-like scatter factor. J. Biochem. 116, 862-869
4. Kikkawa, Y., Sanzen, N., and Sekiguchi, K. (1988) Isolation and characterization of laminin-10/11 secreted by human lung carcinoma cells. Laminin-10/11 mediates cell adhesion through integrin α3β1. J. Biol. Chem. 273, 15854-15859
5. Symington, B.E., Takada, Y., and Carter, W.G. (1993) Interaction of integrins α3β1 and α2β1: potential role in keratinocyte intercellular adhesion. J. Cell Biol. 120, 523-535
6. Sriramarao, P., Steffner, P., and Gehlsen, K.R. (1993) Biochemical evidence for a homophilic interaction of the α3β1 integrin. J. Biol. Chem. 15, 22036-22041
7. Takeuchi, K., Tsuji, T., Hakomori, S., and Irimura T. (1994) Intercellular adhesion induced by anti-α3 integrin (VLA-3) antibodies. Exp. Cell Res. 211, 133-141
8. Weitzman, J.B., Chen, A., and Hemler, M.E. (1995) Investigation of the role of β1 integrins in cell-cell adhesion. J. Cell Sci. 108, 3635-3644
9. Nakamura, K., Iwamoto, R., and Mekada, E. (1995) Membrane-anchored heparin-binding EGF-like growth factor (HB-EGF) and diphtheria toxin receptor-associated protein (DRAP27)/CD9 form a complex with integrin α3β1 at cell-cell contact sites. J. Cell Biol. 129, 1691-1705
10. Okochi, H., Kato, M., Nashiro, K., Yoshie, O., Miyazono, K., and Furue, M. (1997) Expression of tetra-spans transmembrane family (CD9, CD37, CD53, CD63, CD81 and CD82) in normal and neoplastic human keratinocytes: an association of CD9 with α3β1 integrin. Br. J. Dermatol. 137, 856-863
11. Berditchevski, F., Chang, S., Bodorova, J., and Hemler, M.E. (1997) Generation of monoclonal antibodies to integrin-associated proteins. Evidence that α3β1 complexes with EMMPRIN/ basigin/OX47/M6. J. Biol. Chem. 272, 29174-29180
12. Berditchevski, F., Tolias, K.F., Wong, K., Carpenter, C.L., and Hemler, M.E. (1997) A novel link between integrins, transmembrane-4 superfamily proteins (CD63 and CD81), and phosphatidylinositol 4-kinase. J. Biol. Chem. 272, 2595-2598
13. Yanez-Mo, M., Alfranca, A., Cabanas, C., Marazuela, M., Tejedor, R., Ursa, M.A., and Ashman, L.K., de Landazuri, M.O., and Sanchez-Madrid, F. (1998) Regulation of endothelial cell motility by complexes of tetraspan molecules CD81/TAPA-1 and CD151/PETA-3 with α3β1 integrin localized at endothelial lateral junctions. J. Cell Biol. 141, 791-804
14. Coppolino, M., Migliorini, M., Argraves, W.S., and Dedhar, S. (1995) Identification of a novel form of the α3 integrin subunit: covalent association with transferrin receptor. Biochem. J. 306, 129-134
15. McCormick, J.I. and Johnstone, R.M. (1995) Identification of the integrin α3β1 as a component of a partially purified A-system amino acid transporter from Ehrlich cell plasma membranes. Biochem. J. 311, 743-751
16. Tsuji, T., Yamamoto, F., Miura, Y., Takio, K., Titani, K., Pawar, S., Osawa, T., and Hakomori, S. (1990) Characterization through cDNA cloning of galactoprotein b3 (Gap b3), a cell surface membrane glycoprotein showing enhanced expression on oncogenic transformation. Identification of Gap b3 as a member of the integrin superfamily. J. Biol. Chem. 265, 7016-7021
17. Tsuji, T., Hakomori, S., and Osawa, T. (1991) Identification of human galactoprotein b3, an oncogenic transformation-induced membrane glycoprotein, as VLA-3α subunit: the primary structure of human integrin α3. J. Biochem. 109, 659-665
18. Takada, Y., Murphy, E., Pil, P., Chen, C., Ginsberg, M.H., and Hemler, M.E. (1991) Molecular cloning and expression of the cDNA for α3 subunit of human α3β1 (VLA-3), an integrin receptor for fibronectin, laminin, and collagen. J. Cell Biol. 115, 257-266
19. Takeuchi, K., Hirano, K., Tsuji, T., Osawa, T., and Irimura, T. (1995) cDNA cloning of mouse VLA-3α subunit. J. Cell. Biochem. 57, 371-377
20. Tamura, R.N., Cooper, H.M., Collo, G., and Quaranta, V. (1991) Cell type-specific integrin variants with alternative α chain cytoplasmic domains. Proc. Natl. Acad. Sci. USA 88, 10183-10187
21. de Melker, A.A., Sterk, L.M., Delwel, G.O., Fles, D.L., Daams, H., Weening, J.J., and Sonnenberg, A. (1997) The A and B variants of the α3 integrin subunit: tissue distribution and functional characterization. Lab. Invest. 76, 547-563
22. Dedhar, S., Saulnier, R., Nagle, R., and Overall, C.M. (1993) Specific alterations in the expression of α3β1 and α6β4 integrins in highly invasive and metastatic variants of human prostate carcinoma cells selected by in vitro invasion through reconstituted basement membrane. Clin. Exp. Metastasis 11, 391-400
23. Bartolazzi, A., Cerboni, C., Flamini, G., Bigotti, A., Lauriola, L., and Natali, P.G. (1995) Expression of α3β1 integrin receptor and its ligands in human lung tumors. Int. J. Cancer 64, 248-252
24. Melchiori, A., Mortarini, R., Carlone, S., Marchisio, P.C., Anichini, A., Noonan, D.M., and Albini, A. (1995) The α3β1 integrin is involved in melanoma cell migration and invasion. Exp. Cell Res. 219, 233-242
25. Bartolazzi, A., Cerboni, C., Nicotra, M.R., Mottolese, M., Bigotti, A., and Natali, P.G. (1994) Transformation and tumor progression are frequently associated with expression of the α3/β1 heterodimer in solid tumors. Int. J. Cancer 58, 488-491
26. Van Waes, C., Surh, D.M., Chen, Z., Kirby, M., Rhim, J.S., Brager, R., Sessions, R.B., Poore, J., Wolf, G.T., and Carey, T.E. (1995) Increase in suprabasilar integrin adhesion molecule expression in human epidermal neoplasms accompanies increased proliferation occurring with immortalization and tumor progression. Cancer Res. 55, 5434-5344
27. Nishimura, S., Chung, Y.S., Yashiro, M., Inoue, T., and Sowa, M. (1996) Role of α2β1-and α3β1-integrin in the peritoneal implantation of scirrhous gastric carcinoma. Br. J. Cancer 74, 1406-1412
28. Tawil, N.J., Gowri, V., Djoneidi, M., Nip, J., Carbonetto, S., and Brodt, P. (1996) Integrin α3β1 can promote adhesion and spreading of metastatic breast carcinoma cells on the lymph node stroma. Int. J. Cancer 66, 703-710
29. Lichtner, R.B., Howlett, A.R., Lerch, M., Xuan, J.A., Brink, J., Langton-Webster, B., and Schneider, M.R. (1998) Negative cooperativity between α3β1 and α2β1 integrins in human mammary carcinoma MDA MB 231 cells. Exp. Cell Res. 240, 368-376
30. Adachi, M., Taki, T., Huang, C., Higashiyama, M., Doi, O., Tsuji, T., and Miyake, M. (1998) Reduced integrin α3 expression as a factor of poor prognosis of patients with adenocarcinoma of the lung. J. Clin. Oncol. 16, 1060-1067
31. Feinberg, A.P. and Vogelstein, B. (1983) A technique for radio-labeling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem. 132, 6-13
32. Mount, S.M. (1982) A catalogue of splice junction sequences. Nucleic Acids Res. 10, 459-472
33. Coppolino, M., Leung-Hagesteijn, C., Dedhar, S., and Wilkins, J. (1995) Inducible interaction of integrin α2β1 with calreticulin. Dependence on the activation state of the integrin. J. Biol. Chem. 270, 23132-23138
34. Coppolino, M.G., Woodside, M.J., Demaurex, N., Grinstein, S., St-Arnaud, R., and Dedhar, S. (1997) Calreticulin is essential for integrin-mediated calcium signalling and cell adhesion. Nature 386, 843-847
35. Hogervorst, F., Admiraal, L.G., Niessen, C., Kuikman, I., Janssen, H., Daams, H., and Sonnenberg, A. (1993) Biochemical characterization and tissue distribution of the A and B variants of the integrin α6 subunit. J. Cell Biol. 121, 179-191
36. Ziober, B.L., Vu, M.P., Waleh, N., Crawford, J., Lin, C.S., and Kramer, R.H. (1993) Alternative extracellular and cytoplasmic domains of the integrin α7 subunit are differentially expressed during development. J. Biol. Chem. 268, 26773-26783
37. Thorsteinsdottir, S., Roelen, B.A., Freund, E., Gaspar, A.C., Sonnenberg, A., and Mummery, C.L. (1995) Expression patterns of laminin receptor splice variants α6Aβ1 and α6Bβ1 suggest different roles in mouse development. Dev. Dyn. 204, 240-258
38. Heidenreich, R., Eisman, R., Surrey, S., Delgrosso, K., Bennett, J.S., Schwartz, E., and Poncz, M. (1990) Organization of the gene for platelet glycoprotein IIb. Biochemistry 29, 1232-1244
39. Corbi, A.L., Garcia-Aguilar, J., and Springer, T.A. (1990) Genomic structure of an integrin α subunit, the leukocyte p150, 95 molecule [published erratum appears in J. Biol Chem. 265, 12750-12751, 1990]. J. Biol. Chem. 265, 2782-2788
40. Fleming, J.C., Pahl, H.L., Gonzalez, D.A., Smith, T.F., and Tenen, D.G. (1993) Structural analysis of the CD11b gene and phylogenetic analysis of the α-integrin gene family demonstrate remarkable conservation of genomic organization and suggest early diversification during evolution. J. Immunol. 150, 480-490
41. Pulkkinen, L., Kimonis, V.E., Xu, Y., Spanou, E.N., McLean, W.H., and Uitto, J. (1997) Homozygous α6 integrin mutation in junctional epidermolysis bullosa with congenital duodenal atresia. Hum. Mol. Genet. 6, 669-674
42. Jones, S.D., van der Flier, A., and Sonnenberg, A. (1998) Genomic organization of the human α3 integrin subunit gene. Biochem. Biophys. Res. Commun. 248, 896-898