Function and Receptor Specificity of a Minimal 20 Kilodalton Cell Adhesive Fragment of Fibronectin

References

• Akiyama S. K., Hasegawa E., Hasegawa T., Yamada K. M. The interaction of fibronectin fragments with fibroblastic cells. J. Biol. Chem. 1985; 260: 13256–13260
   PubMed Web of Science ®Google Scholar
• Akiyama S. K., Nagata K., Yamada K. M. Cell surface receptors for extracellular matrix proteins. Biochim. Biophys. Acta 1990; 1031: 91–109
   PubMed Web of Science ®Google Scholar
• Akiyama S. K., Yamada K. M. Comparisons of evolutionarily distinct fibronectins: Evidence for the origin of plasma and fibroblast cellular fibronectins from a single gene. J. Cell. Biochem. 1985a; 27: 97–107
   PubMed Web of Science ®Google Scholar
• Akiyama S. K., Yamada K. M. Synthetic peptides competitively inhibit both direct binding to fibroblasts and functional biological assays for the purified cell-binding domain of fibronectin. J. Biol. Chem. 1985b; 260: 10402–10405
   PubMed Web of Science ®Google Scholar
• Akiyama S. K., Yamada S. S., Yamada K. M. Characterization of a 140-kD avian cell surface antigen as a fibronectin-binding molecule. J. Cell Biol. 1986; 102: 442–448
   PubMed Web of Science ®Google Scholar
• Akiyama S. K., Yamada S. S., Chen W.-T., Yamada K. M. Analysis of fibronectin receptor function with monoclonal antibodies: Roles in cell adhesion, migration, matrix assembly, and cytoskeletal organization. J. Cell Biol. 1989; 109: 863–875
   PubMed Web of Science ®Google Scholar
• Albelda S. M., Buck C. A. Integrins and other cell adhesion molecules. FASEB J. 1990; 4: 2868–2880
   PubMed Web of Science ®Google Scholar
• Aota S., Nagai T., Yamada K. M. Characterization of regions of fibronectin besides the argmme-glyrine-aspartic acid sequence required for adhesive function of the cell-binding domain using site-directed mutagenesis. J. Biol. Chem. 1991; 266: 15938–15943
   PubMed Web of Science ®Google Scholar
• Borsi L., Castellani P., Balza E., Siri A., Pellecchia C., De Scalzi F., Zardi L. Large scale procedure for the purification of fibronectin domains. Anal. Biochem. 1986; 155: 335–345
   PubMed Web of Science ®Google Scholar
• Bowditch R. D., Halloran C. E., Aota S., Obara M., Plow E. F., Yamada K. M., Ginsberg M. H. Integrin αIIb,β3 (platelet GP IIb-IIIa) recognizes multiple sites in fibronectin. J. Biol. Chem. 1991; 266: 23323–23328
   PubMed Web of Science ®Google Scholar
• Busk M., Pytela R., Sheppard D. Characterization of the integrin alpha v beta 6 as a fibronectin-binding protein. J. Biol. Chem. 1992; 267: 5790–5796
   PubMed Web of Science ®Google Scholar
• Carson S. E. Fibronectin in Health and Disease. CRC Press, Boca Raton, FL 1990; 297
   Google Scholar
• Charo I. F., Nannizzi L., Smith J. W., Cheresh D. A. The vitronectin receptor αvβ3 binds fibronectin and acts in concert with α5β1 in promoting cellular attachment and spreading on fibronectin. J. Cell Biol. 1990; 111: 2795–2800
   PubMed Web of Science ®Google Scholar
• Chaudhary V. K., Queen C., Junghans R. P., Waldmann T. A., FitzGerald D. J., Pastan I. A recombinant immunotoxin consisting of two antibody variable domains fused to Pseudomonas exotoxin. Nature 1989; 339: 394–397
   PubMed Web of Science ®Google Scholar
• Elices M. J., Urry L. A., Hemler 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
• Ginsberg M. H., Loftus J. C., Plow E. F. Cytoadhesions, integrins, and platelets. Thromb. Hemostas. 1988; 59: 1–6
   PubMed Web of Science ®Google Scholar
• Guan J.-L., Hynes R. O. Lymphoid cells recognize an alternatively-spliced segment of fibronectin via the receptor α4β1. Cell 1990; 60: 53–61
   PubMed Web of Science ®Google Scholar
• Hemler M. E. VLA proteins in the integrin family: Structures, functions, and their role on leukocytes. Annu. Rev. Immunol. 1990; 8: 365–400
   PubMed Web of Science ®Google Scholar
• Hynes R. O. Fibronectins. Springer-Verlag, NY 1990; 546
   Google Scholar
• Hynes R. O. Integrins: Versatility, modulation, and signaling in cell adhesion. Cell 1992; 69: 11–25
   PubMed Web of Science ®Google Scholar
• Hautanen A., Gailit J., Mann D. M., Ruoslahti E. Effects of modifications of the RGD sequence and its context on recognition by the fibronectin receptor. J. Biol. Chem. 1989; 264: 1437–1442
   PubMed Web of Science ®Google Scholar
• Juliano R. L. Membrane receptors for extracellular matrix macromolecules: relationship to cell adhesion and tumor metastasis. Biochim. Biophys. Acta 1987; 907: 261–278
   PubMed Web of Science ®Google Scholar
• Katayama M., Hino F., Odate Y., Goto S., Kimizuka F., Kato I., Titani K., Sekiguchi K. Isolation and characterization of two monoclonal antibodies that recognize remote epitopes on the cell-binding domain of human fibronectin. Exp. Cell Res. 1989; 185: 229–236
   PubMed Web of Science ®Google Scholar
• Kimizuka E., Ohdate Y., Kawase Y., Shimojo T., Taguchi Y., Hashino K., Goto S., Hashi H., Kato I., Sekiguchi K., Titani K. Role of type III homology repeats in cell adhesive function within the cell-binding domain of fibronectin. J. Biol. Chem. 1991; 266: 3045–3051
   PubMed Web of Science ®Google Scholar
• Humphries M. J., Komoriya A., Akiyama S. K., Olden K., Yamada K. M. Identification of two distinct regions of the type III connecting segment of human plasma fibronectin that promote cell type-specific adhesion. J. Biol. Chem. 1987; 262: 6886–6892
   PubMed Web of Science ®Google Scholar
• Kornblihtt A. R., Umezawa K., Vibe-Pedersen K., Baralle F. E. Primary structure of human fibronectin: differential splicing may generate at least ten polypeptides from a single gene. EMBO J. 1985; 4: 1755–1759
   PubMed Web of Science ®Google Scholar
• Larjava H., Peltonen J., Akiyama S. K., Yamada S. S., Gralnick H. R., Uitto J., Yamada K. M. Novel function for β1 integrins in keratinocyte cell-cell interactions. J. Cell Biol. 1990; 110: 803–815
   PubMed Web of Science ®Google Scholar
• Lewandowska K., Kaetzel C. S., Zardi L., Culp L. A. Binding characteristics of complementary fibronectin fragments on artificial substrata. FEBS Lett. 1988; 237: 35–39
   PubMed Web of Science ®Google Scholar
• Receptors for Extracellular Matrix, J. A. McDonald, R. P. Mecham. Academic Press, NY 1991; 330
   Google Scholar
• Miekka S. I., Ingham K. C., Menache D. Rapid methods for isolation of human plasma fibronetin. Thromb. Res. 1982; 27: 1–14
   PubMed Web of Science ®Google Scholar
• Mosher D. F. Fibronectin. Academic Press, NY 1989; 474
   Google Scholar
• Nagai T., Yamakawa N., Aota S., Yamada S. S., Akiyama S. K., Olden K., Yamada K. M. Monoclonal antibody characterization of two distant sites required for function of the central cell-binding domain of fibronectin in cell adhesion, cell migration, and matrix assembly. J Cell Biol. 1991; 114: 1295–1305
   PubMed Web of Science ®Google Scholar
• Nowlin D. M., Gorscan F., Moscinski M., Chiang S.-L., Lobl T. J., Cardarelli P. M. A novel cyclic pentapeptide inhibits α4β1 and α5β1 integrin-mediated cell adhesion. J. Biol. Chem. 1993; 268: 20352–20359
   PubMed Web of Science ®Google Scholar
• Obara M., Kang M. S., Yamada K. M. Site-directed mutagenesis of the cell-binding domain of fibronectin: Separable, synergistic sites mediate adhesive function. Cell 1988; 53: 649–657
   PubMed Web of Science ®Google Scholar
• Pasqualini R., Bodorova J., Ye S., Hemler M. E. A study of the structure, function, and distribution of β5 integrins using novel anti-β5 monoclonal antibodies. J. Cell Sci. 1993; 105: 1873–1884
   Web of Science ®Google Scholar
• Pierschbacher M. D., Ruoslahti E. Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion. J. Biol. Chem. 1987; 262: 17294–17298
   PubMed Web of Science ®Google Scholar
• Pierschbacher M. D., Ruoslahti E. Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature 1984; 309: 30–33
   PubMed Web of Science ®Google Scholar
• Pierschbacher M. D., Hayman E. G., Ruoslahti E. Location of the cell-attachment site in fibronectin with monoclonal antibodies and proteolytic fragments of the molecule. Cell 1981; 26: 259–267
   PubMed Web of Science ®Google Scholar
• Pierschbacher M. D., Ruoslahti E., Sundelin J., Lind P., Peterson P. A. The cell attachment domain of fibronectin. Determination of the primary structure. J. Biol. Chem. 1982; 257: 9593–9597
   PubMed Web of Science ®Google Scholar
• Pytela R., Pierschbacher M. D., Ruoslahti E. A125/115-kDa cell surface receptor specific for vitronectin interacts with the arginine-glycine-aspartic acid adhesion sequence derived from fibronectin. Proc. Natl. Acad. Sci. USA 1985a; 82: 5766–5770
   PubMed Web of Science ®Google Scholar
• Pytela R., Pierschbacher M. D., Ruoslahti E. Identification and isolation of a 140 kd cell surface glycoprotein with properties expected of a fibronectin receptor. Cell 1985b; 40: 191–198
   PubMed Web of Science ®Google Scholar
• Ruoslahti E. Integrins. J. Clin. Invest. 1991; 87: 1–5
   PubMed Web of Science ®Google Scholar
• Saiki R. K., Gelfand D. H., Stoffel S., Scharf S. J., Higuchi R., Horn C. T., Mullis K. B., Erlich H. A. Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase. Science 1988; 239: 487–491
   PubMed Web of Science ®Google Scholar
• Studier F. W., Moffatt B. A. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 1986; 189: 113–130
   PubMed Web of Science ®Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• Varani J., Orr W., Ward P. A. A comparison of the migration patterns of normal and malignant cells in two assay systems. Am. J. Pathol. 1978; 90: 159–171
   PubMed Web of Science ®Google Scholar
• Vogel B. E., Tarone G., Giancotti F. G., Gailit J., Ruoslahti E. A novel fibronectin receptor with an unexpected sub-unit composition (αvβ1). J. Biol. Chem. 1990; 265: 5934–5937
   PubMed Web of Science ®Google Scholar
• Vogel B. E., Lee S.-J., Hildebrand A., Craig W., Pierschbacher M. D., Wong-Staal F., Ruoslahti E. A novel integrin specificity exemplified by binding of the (αvβ5 integrin to the basic domain of the HIV Tat protein and vitronectin. J. Cell Biol. 1993; 121: 461–468
   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
• Yamada K. M., Kennedy D. W. Dualistic nature of adhesive protein function: fibronectin and its biologically active peptide fragments can autoinhibit fibronectin function. J. Cell Biol. 1984; 99: 29–36
   PubMed Web of Science ®Google Scholar
• Yamada K. M., Kennedy D. W., Yamada S. S., Gralnick H., Chen W.-T., Akiyama S. K. Monoclonal antibody and synthetic peptide inhibitors of human tumor cell migration. Cancer Res. 1990; 50: 4485–4496
   PubMed Web of Science ®Google Scholar
• Zardi L., Carnemolla B., Balza E., Borsi L., Castellani P., Rocca M., Siri A. Elution of fibronectin proteolytic fragments from a hydroxyapatite chromatography column. A simple procedure for the purification of fibronectin domains. Eur. J. Biochem. 1985; 146: 571–579
   PubMedGoogle Scholar