Abstract
Fibronectin, laminin, and other recently characterized noncollagenous extra-cellular proteins play important roles in many cell surface interactions. For example, fibronectin helps to mediate cell adhesion, embryonic cell migration, and wound healing, while laminin can promote processes as diverse as axonal outgrowth, maintenance of the polarized, differentiated phenotype of epithelial cells on a basement membrane, and metastasis. Each of these glycoproteins can participate in a variety of functions by using different specialized domains or peptide recognition sequences for binding to specific cell surface receptors, or to collagens, proteoglycans, or other extracellular molecules. In the decade since the first edition of this book, there has been remarkable progress in our understanding of the structures, domain organization, and biological roles of these multifunctional cell interactive proteins.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Akiyama, S. K., and Yamada, K. M., 1985, Synthetic peptides competitively inhibit both direct binding to fibroblasts and functional biological assays for the purified cell-binding domain of fibronectin, J. Biol. Chem. 260:10402–10405.
Akiyama, S. K., Hasegawa, E., Hasegawa, T., and Yamada, K. M., 1985, The interactions of fibronectin fragments with fibroblastic cells, J. Biol. Chem. 260:13256–13260.
Asch, A. S., and Nachman, R. L., 1989, Thrombospondin: Phenomenology to function, Prog. Hemost. Thromb. 9:157–176.
Aumailley, M., Wiedemann, H., Mann, K., and Timpl, R., 1989, Binding of nidogen and the lami-nin-nidogen complex to basement membrane collagen type IV, Eur. J. Biochem. 184:241–248.
Aumailley, M., Gerl, M., Sonnenberg, A., Deutzmann, R., and Timpl, R., 1990, Identification of the Arg-Gly-Asp sequence in laminin A chain as a latent cell-binding site being exposed in frag-ment P1, FEBS Lett. 262:82–86.
Bale, M. D., Wohlfahrt, L. A., Mosher, D. F., Tomasini, B., and Sutton, R. C., 1989, Identification of vitronectin as a major plasma protein absorbed on polymer surfaces of different copolymer composition, Blood 74:2698–2706.
Barnes, D. W., Foley, T. P., Shaffer, M. C., and Silnutzer, J. E., 1984, Human serum spreading factor: Relationship to somatomedin B, J. Clin. Endocrinol. Metab. 59:1019–1021.
Baron, M., Norman, D., Willis, A., and Campbell, I. D., 1990, Structure of the fibronectin type 1 module, Nature 345:642–646.
Beck, K., Hunter, I., and Engel, J., 1990, Structure and function of laminin. Anatomy of a multidomain glycoprotein, FASEB J. 4:148–160.
Benecky, M. J., Kolvenbach, C. G., Wine, R. W., DiOrio, J. P., and Mosesson, M. W., 1990, Human plasma fibronectin structure probed by steady-state fluorescence polarization: Evidence for a rigid oblate structure, Biochemistry 29:3082–3091.
Boucaut, J.-C., Darribére, T., Poole, T. J., Aoyama, H., Yamada, K. M., and Thiery, J. P., 1984, Biologically active synthetic peptides as probes of embyonic development: A competitive peptide inhibitor of fibronectin function inhibits gastrulation in amphibian embryos and neural crest cell migration in avian embryos, J. Cell Biol. 99:1822–1830.
Bourdon, M. A., and Ruoslahti, E., 1989, Tenascin mediates cell attachment through an RGDdependent receptor, J. Cell Biol. 108:1149–1155.
Burridge, K., Fath, K., Kelly, T., Nuckolls, G., and Turner, C., 1988, Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton, Annu. Rev. Cell Biol. 4:487–525.
Carsons, S. E. (ed.), 1989, Fibronectin in Health and Disease, CRC Press, Boca Raton.
Chakravarti, S., Tam, M. F., and Chung, A. E., 1990, The basement membrane glycoprotein entactin promotes cell attachment and binds calcium ions, J. Biol. Chem. 265:10597–10603.
Chiquet-Ehrismann, R., 1990, What distinguished tenascin from fibronectin? FASEB J. 4:2598–2604.
Chiquet-Ehrismann, R., Kalla, P., Pearson, C. A., Beck, K., and Chiquet, M., 1988, Tenascin interferes with fibronectin action, Cell 53:383–390.
Dahlbäck, K., Löfberg, H., Alumets, J., and Dahlbäck, B., 1989, Immunohistochemical demonstration of age-related deposition of vitronectin (S-protein of complement) and terminal complement complex on dermal elastic fibers, J. Invest. Dermatol. 92:727–733.
Dardik, R., and Lahav, J., 1989, Multiple domains are involved in the interaction of endothelial cell thrombospondin with fibronectin, Eur. J. Biochem. 185:581–588.
Darribére, T., Guida, K., Larjava, H., Johnson, K. E., Yamada, K. M., Thiery, J. P., and Boucaut, J.-C., 1990, In vivo analyses of integrin beta 1 subunit function in fibronectin matrix assembly, J. Cell Biol. 110:1813–1823.
Dean, D. C., McQuillan, J. J., and Weintraub, S., 1990, Serum stimulation of fibronectin gene expression appears to result from rapid serum-induced binding of nuclear proteins to a cAMP response element, J. Biol. Chem. 265:3522–3527.
Dejana, E., Colella, S., Conforti, G., Abbadini, M., Gaboli, M., and Marchisio, P. C., 1988, Fibronectin and vitronectin regulate the organization of their respective Arg-Gly-Asp adhesion receptors in cultured human endothelial cells, J. Cell Biol. 107:1215–1223.
Deutzmann, R., Aumailley, M., Wiedemann, H., Pysny, W., Timpl, R., and Edgar, D., 1990, Cell adhesion, spreading and neurite stimulation by laminin fragment E8 depends on maintenance of secondary and tertiary structure in its rod and globular domain, Eur. J. Biochem. 191:513–522.
Dillner, L., Dickerson, K., Manthorpe, M., Ruoslahti, E., and Engvall, E., 1988, The neurite-promoting domain of human laminin promotes attachment and induces characteristic morphology in non-neuronal cells, Exp. Cell Res. 177:186–198.
Donoviel, D. B., Framson, P., Eldridge, C. F., Cooke, M., Kobayashi, S., and Bornstein, P., 1988, Structural analysis and expression of the human thrombospondin gene promoter, J. Biol. Chem. 263:18590–18593.
D’Souza, S. E., Ginsberg, M. H., Burke, T. A., and Plow, E. F., 1990, The ligand binding site of the platelet integrin receptor GPIIb-IIIa is proximal to the second calcium binding domain of its alpha subunit, J. Biol. Chem. 265:3440–3446.
Dufour, S., Duband, J.-L., Humphries, M. J., Obara, M., Yamada, K. M., and Thiery, J. P., 1988a, Attachment, spreading and locomotion of avian neural crest cells are mediated by multiple adhesion sites on fibronectin molecules, EMBO J. 7:2661–2671.
Dufour, S., Duband, J.-L., Kornblihtt, A. R., and Thiery, J. P., 1988b, The role of fibronectins in embryonic cell migrations, Trends Genet. 4:198–203.
Durkin, M. E., Chakravarti, S., Bartos, B. B., Liu, S. H., Friedman, R. L., and Chung, A. E., 1988, Amino acid sequence and domain structure of entactin. Homology with epidermal growth factor precursor and low density lipoprotein receptor, J. Cell Biol. 107:2749–2756.
Ehrig, K., Leivo, I., Argraves, W. S., Ruoslahti, E., and Engvall, E., 1990, Merosin, a tissue-specific basement membrane protein, is a laminin-like protein, Proc. Natl. Acad. Sci. USA. 87:3264–3268.
Ehrismann, R., Roth, D. E., Eppenberger, H. M., and Turner, D. C., 1982, Arrangement of attachment-promoting, self-association, and heparin-binding sites in horse serum fibronectin, J. Biol. Chem. 257:7381–7387.
Enenstein, J., and Furcht, L. T., 1988, Epithelial and neural localization and heparin binding of the cell-substratum adhesion molecule, epinectin, J. Invest. Dermatol. 91:34–38.
Erickson, H. P., and Bourdon, M. A., 1989, Tenascin: An extracellular matrix protein prominent in specialized embryonic tissues and tumors, Annu. Rev. Cell Biol. 5:71–92.
Fava, R. A., and McClure, D. B., 1987, Fibronectin-associated transforming growth factor, J. Cell. Physiol. 131:184–189.
Fogerty, F. J., Akiyama, S. K., Yamada, K. M., and Mosher, D. F., 1990, Inhibition of binding of fibronectin to matrix assembly sites by anti-integrin (a41) antibodies, J. Cell Biol. 111:699–708.
Fox, G., Parry, N. R., Barnett, P. V., McGinn, B., Rowlands, D. J., and Brown, F., 1989, The cell attachment site on foot-and-mouth disease virus includes the amino acid sequence RGD (arginine-glycine-aspartic acid), J. Gen. Virol. 70:625–637.
Frazier, W. A., 1987, Thrombospondin: A modular adhesive glycoprotein of platelets and nucleated cells, J. Cell Biol. 105:625–632.
Friedlander, D. R., Hoffman, S., and Edelman, G. M., 1988, Functional mapping of cytotactin: Proteolytic fragments active in cell—substrate adhesion, J. Cell Biol. 107:2329–2340.
Gehlsen, K. R., Dickerson, K., Argraves, W. S., Engvall, E., and Ruoslahti, E., 1989, Subunit structure of a laminin-binding integrin and localization of its binding site on laminin, J. Biol. Chem. 264:19034–19038.
Ginsberg, M. H., Loftus, J. C., and Plow, E. F., 1988, Cytoadhesins, integrins, and platelets, Thromb. Haemost. 59:1–6.
Graf., J., Iwamoto, Y., Sasaki, M., Martin, G. R., Kleinman, H. K., Robey, F. A., and Yamada, Y., 1987, Identification of an amino acid sequence in laminin mediating cell attachment, chemotaxis, and receptor binding, Cell 48:989–996.
Grant, D. S., Tashiro, K., Segui-Real, B., Yamada, Y., Martin, G. R., and Kleinman, H. K., 1989, Two different laminin domains mediate the differentiation of human endothelial cells into capillary-like structures in vitro, Cell 58:933–943.
Grinnell, F., and Phan, T. V., 1983, Deposition of fibronectin on material surfaces exposed to plasma: Quantitative and biological studies, J. Cell. Physiol. 116:289–296.
Guan, J. L., Trevithick, J. E., and Hynes, R. 0., 1990, Retroviral expression of alternatively spliced forms of rat fibronectin, J. Cell Biol. 110:833–847.
Hall, D. E., Reichardt, L. F., Crowley, E., Holley, B., Moezzi, H., Sonnenberg, A., and Damsky, C. H., 1990, The α1/β1 and α6/β1 integrin heterodimers mediate cell attachment to distinct sites on laminin, J. Cell Biol. 110:2175–2184.
Hayashi, M., and Yamada, K. M., 1982, Divalent cation modulation of fibronectin binding to heparin and to DNA, J. Biol. Chem. 257:5263–5267.
Heinegárd, D., and Oldberg, A., 1989, Structure and biology of cartilage and bone matrix non-collagenous macromolecules, FASEB J. 3:2042–2051.
Hershberger, R. P., and Culp, L. A., 1990, Cell-type-specific expression of alternatively spliced human fibronectin IIICS mRNAs, Mol. Cell. Biol., 10:662–671.
Hirano, H., Yamada, Y., Sullivan, M., de Crombrugghe, B., Pastan, I., and Yamada, K. M., 1983, Isolation of genomic DNA clones spanning the entire fibronectin gene, Proc. Natl. Acad. Sci. USA 80:46–50.
Hoffman, S., Crossin, K. L., and Edelman, G. M., 1988, Molecular forms, binding functions, and developmental expression patterns of cytotactin and cytotactin-binding proteoglycan, an interactive pair of extracellular matrix molecules, J. Cell Biol. 106:519–532.
Hoffman, S., Crossin, K. L., Jones, F. S., Friedlander, D. R., and Edelman, G. M., 1990, Cytotactin and cytotactin-binding proteoglycan. An interactive pair of extracellular matrix proteins, Ann. N.Y. Acad. Sci. 580:288–301.
Humphries, M. J., Akiyama, S. K., Komoriya, A., Olden, K., and Yamada, K. M., 1986, Identification of an alternatively spliced site in human plasma fibronectin that mediates cell type-specific adhesion, J. Cell Biol. 103:2637–2647.
Humphries, M. J., Komoriya, A., Akiyama, S. K., Olden, K., and Yamada, K. M., 1987, Identification of two distinct regions of the type III connecting segment of human plasma fibronectin that promote cell type-specific adhesion, J. Biol. Chem. 262:6886–6892.
Humphries, M. J., Akiyama, S. K., Komoriya, A., Olden, K., and Yamada, K. M., 1988, Neurite extension of chicken peripheral nervous system neurons on fibronectin: Relative importance of specific adhesion sites in the central cell-binding domain and the alternatively spliced type III connecting segment, J. Cell Biol. 106:1289–1297.
Hunter, D. D., Porter, B. E., Bulock, J. W., Adams, S. P., Merlie, J. P., and Sanes, J. R., 1989, Primary sequence of a motor neuron-selective adhesive site in the synaptic basal lamina protein slaminin, Cell 59:905–913.
Hynes, R. O., 1990, Fibronectins, Springer-Verlag, Berlin.
Ingham, K. C., Landwehr, R., and Engel, J., 1985, Interaction of fibronectin with Clq and collagen. Effects of ionic strength and denaturation of the collagenous component, Eur. J. Biochem, 148:219–224.
Ingham, K. C., Brew, S. A., and Migliorini, M. M., 1989, Further localization of the gelatin-binding determinants within fibronectin. Active fragments devoid of type II homologous repeat modules, J. Biol. Chem. 264:16977–16980.
Izumi, M., Shimo-Oka, T., Morishita, N., Ii, I., and Hayashi, M., 1988, Identification of the collagen-binding domain of vitronectin using monoclonal antibodies, Cell Struct. Funct. 13:217–225.
Izzard, C. S., Radinsky, R., and Culp, L. A., 1986, Substratum contacts and cytoskeletal reorganization of BALB/c 3T3 cells on a cell-binding fragment and heparin-binding fragments of plasma fibronectin, Exp. Cell Res. 165:320–336.
Jenne, D., and Stanley, K. K., 1985, Molecular cloning of S-protein, a link between complement, coagulation and cell—substrate adhesion, EMBO J. 4:3153–3157.
Jenne, D., and Stanley, K. K., 1987, Nucleotide sequence and organization of the human S-protein gene: Repeating peptide motifs in the “pexin” family and a model for their evolution, Biochemistry 26:6735–6742.
Jones, F. S., Hoffman, S., Cunningham, B. A., and Edelman, G. M., 1989, A detailed structural model of cytotactin: Protein homologies, alternative RNA splicing, and binding regions, Proc. Natl. Acad. Sci. USA 86:1905–1909.
Kaesberg, P. R., Ershler, W. B., Esko, J D, and Mosher, D. F., 1989, Chinese hamster ovary cell adhesion to human platelet thrombospondin is dependent on cell surface heparan sulfate proteoglycan, J. Clin. Invest. 83:994–1001.
Kanemoto, T., Reich, R., Royce, L., Greatorex, D., Adler, S. H., Shiraishi, N., Martin, G. R., Yamada, Y., and Kleinman, H. K., 1990, Identification of an amino acid sequence from the laminin A chain that stimulates metastasis and collagenase IV production,Proc. Natl. Acad. Sci. USA 87:2279–2283.
Ketis, N. V., Lawler, J., Hoover, R. L., and Karnovsky, M. J., 1988, Effects of heat shock on the expression of thrombospondin by endothelial cells in culture, J. Cell Biol. 106:893–904.
Keynes, R., and Cook, G., 1990, Cell—cell repulsion: Clues from the growth cone? Cell 62: 609–610.
Kleinman, H. K., and Weeks, B. S., 1991, The neural cell response to laminin: Active sites, recep-tors, and intracellular signals, Comments Develop. Neurobiol. in press.
Kleinman, H. K., Graf, J., Iwamoto, Y., Sasaki, M., Schasteen, C. S., Yamada, Y., Martin, G. R., and Robey, F. A., 1989, Identification of a second active site in laminin for promotion of cell adhesion and migration and inhibition of in vivo melanoma lung colonization, Arch. Biochem. Biophys. 272:39–45.
Knox, P., 1984, Kinetics of cell spreading in the presence of different concentrations of serum or fibronectin-depleted serum, J. Cell Sci. 71:51–59.
Komoriya, A., Green, L. J., Mervic, M., Yamada, S. S., Yamada, K. M., and Humphries, M. J., 1991, The minimal essential sequence for a major cell type-specific adhesion site (CS1) within the alternatively spliced IIICS domain of fibronectin is Leu-Asp-Val, J. Biol. Chem. 266: 15075–15079.
Kornblihtt, A. R., Umezawa, K., Vibe-Pedersen, K., and Baralle, F. E., 1985, Primary structure of human fibronectin: Differential splicing may generate at least 10 polypeptides from a single gene, EMBO J. 4:1755–1759.
Kouzi-Koliakos, K., Koliakos, G. G., Tsilibary, E. C., Furcht, L. T., and Charonis, A. S., 1989, Mapping of three major heparin-binding sites on laminin and identification of a novel heparin-binding site on the B1 chain, J. Biol. Chem. 264:17971–17978.
Kubota, K., Katayama, S., Matsuda, M., and Hayashi, M., 1988, Three types of vitronectin in human blood, Cell Struct. Funct. 13:123–128.
Lahav, J., 1988, Thrombospondin inhibits adhesion of endothelial cells, Exp. Cell Res. 177: 199–204.
Laherty, C. D., Gierman, T. M., and Dixit, V. M., 1989, Characterization of the promoter region of the human thrombospondin gene. DNA sequences within the first intron increase transcription, J. Biol. Chem. 264:11222–11227.
Lane, T. F., and Sage, E. H. 1990, Functional mapping of SPARC: Peptides from two distinct Ca+ +binding sites modulate cell shape, J. Cell Biol. 111:3065–3076.
Lash, J. W., Linask, K. K., and Yamada, K. M., 1987, Synthetic peptides that mimic the adhesive recognition signal of fibronectin: Differential effects on cell—cell and cell—substratum adhesion in embryonic chick cells, Dev. Biol. 123:411–420.
Lawler, J., 1986, The structural and functional properties of thrombospondin, Blood 67:1197–1209.
Lawler, J., and Hynes, R. O., 1989, An integrin receptor on normal and thrombasthenic platelets that binds thrombospondin, Blood 74:2022–2027.
Lawler, J., Weinstein, R., and Hynes, R. O., 1988, Cell attachment to thrombospondin: The role of ARG-GLY-ASP, calcium, and integrin receptors, J. Cell Biol. 107:2351–2361.
Liesi, P., Narvanen, A., Soos, J., Sariola, H., and Snounou, G., 1989, Identification of a neurite outgrowth-promoting domain of laminin using synthetic peptides, FEBS Lett. 244:141–148.
Lightner, V. A., and Erickson, H. P., 1990, Binding of hexabrachion (tenascin) to the extracellular matrix and substratum and its effect on cell adhesion, J. Cell Sci. 95:263–277.
Loftus, J. C., O’Toole, T. E., Plow, E. F., Glass, A., Frelinger, A. L., and Ginsberg, M. H., 1990, A 133 integrin mutation abolishes ligand binding and alters divalent cation dependent conformation, Science 249:915–918.
Long, M. W., and Dixit, V. M., 1990, Thrombospondin functions as a cytoadhesion molecule for human hematopoietic progenitor cells, Blood 75:2311–2318.
Lotz, M. M., Burdsal, C. A., Erickson, H. P., and McClay, D. R., 1989, Cell adhesion to fibronectin and tenascin: Quantitative measurements of initial binding and subsequent strengthening response, J. Cell Biol. 109:1795–1805.
Lyons-Giordano, B., Brinker, J. M., and Kefalides, N. A., 1989, Heparin increases mRNA levels of thrombospondin but not fibronectin in human vascular smooth muscle cells, Biochem. Biophys. Res. Commun. 162:1100–1104.
Mackie, E. J., Halfter, W., and Liverani, D., 1988, Induction of tenascin in healing wounds, J. Cell Biol. 107:2757–2767.
Majack, R. A., Goodman, L V., and Dixit, V. M., 1988, Cell surface thrombospondin is functionally essential for vascular smooth muscle cell proliferation, J. Cell Biol. 106:415–422.
Mann, K., Deutzmann, R., Aumailley, M., Timpl, R., Raimondi, L., Yamada, Y., Pan, T. C., Conway, D., and Chu, M. L., 1989, Amino acid sequence of mouse nidogen, a multidomain basement membrane protein with binding activity for laminin, collagen IV and cells,EMBO J.8:65–72.
Martin, G. R., Timpl, R., and Kühn, K., 1988, Basement membrane proteins: Molecular structure and function, Adv. Prot. Chem. 39:1–50.
McCarthy, J. B., Chelberg, M. K., Mickelson, D. J., and Furcht, L. T, 1988, Localization and chemical synthesis of fibronectin peptides with melanoma adhesion and heparin binding activities, Biochemistry 27:1380–1388.
McCarthy, J. B., Skubitz, A. P., Qi, Z., Yi, X. Y., Mickelson, D. J., Klein, D. J., and Furcht, L. T., 1990, RGD-independent cell adhesion to the carboxy-terminal heparin-binding fragment of fibronectin involves heparin-dependent and -independent activities, J. Cell Biol. 110:777–787.
McDonald, J. A., 1988, Extracellular matrix assembly, Annu. Rev. Cell Biol. 4:183–207.
McDonald, J. A., Quade, B. J., Broekelmann, T. J., LaChance, R., Forsman, K., Hasegawa, E., and Akiyama, S., 1987, Fibronectin’s cell-adhesive domain and an amino-terminal matrix assembly domain participate in its assembly into fibroblast pericellular matrix, J. Biol. Chem. 262:2957–2967.
McKeown-Longo, P. J., and Mosher, D. F., 1985, Interaction of the 70,000-mol-wt amino fragment of fibronectin with the matrix-assembly receptor of fibroblasts, J. Cell Biol. 100:364–374.
Mecham, R. P., Hinek, A., Griffin, G. L., Senior, R. M., and Liotta, L. A., 1989, The elastin receptor shows structural and functional similarities to the 67-kDa tumor cell laminin receptor, J. Biol. Chem. 264:1665 2–166 5 7.
Moos, M., Tacke, R., Scherer, H., Teplow, D., Früh, K., and Schachner, M., 1988, Neural adhesion molecule L1 as a member of the immunoglobulin superfamily with binding domains similar to fibronectin, Nature 334:701–703.
Mosher, D. F. (ed.,), 1989, Fibronectin, Academic Press, New York.
Mosher, D. F., 1990, Physiology of thrombospondin, Annu. Rev. Med. 41:85–97.
Mould, A. P., Komoriya, A., Yamada, K. M., and Humphries, M. J., 1991, Affinity chromatographic isolation of the melanoma adhesion receptor for the IIICS region of fibronectin and its identification as the integrin α4β1, J. Biol. Chem. 265:4020–4024.
Murphy-Ullrich, J. E., and Höök, M., 1989, Thrombospondin modulates focal adhesions in endothelial cells, J. Cell Biol. 109:1309–1319.
Musial, J., Niewiarowski, S., Rucinski, B., Stewart, G. J., Cook, J. J., Williams, J. A., and Edmunds, L. H., 1990, Inhibition of platelet adhesion to surfaces of extracorporeal circuits by disintegrins. RGD-containing peptides from viper venoms, Circulation 82:261–273.
Nagai, T., Yamakama, N., Aota, S., Yamada, S. S., Akiyama, S. K., Olden, K., and Yamada, K. M., 1991, 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. in press.
Nojima, Y., Humphries, M. J., Mould, A. P., Komoriya, A., Yamada, K. M., Schlossman, S. F., and Morimoto, C., 1990, VLA-4 mediates CD3-dependent CD4 + T cell activation via the CS1 alternatively spliced domain of fibronectin, J. Exp. Med. 172:1185–1192.
Obara, M., Kang, M. S., and Yamada, K. M., 1988, Site-directed mutagenesis of the cell-binding domain of human fibronectin: Separable, synergistic sites mediate adhesive function, Cell 53:649–657.
Olden, K., Pratt, R. M., and Yamada, K. M., 1979, Role of carbohydrate in biological function of the adhesive glycoprotein fibronectin, Proc. Natl. Acad. Sci. USA 76:3343–3347.
O’Shea, K. S., and Dixit, V. M., 1988, Unique distribution of the extracellular matrix component thrombospondin in the developing mouse embryo, J. Cell Biol. 107:2737–2748.
Owens, R. J., and Baralle, F. E., 1986, Mapping the collagen-binding site of human fibronectin by expression in Escherichia coli, EMBO J. 5:2825–2830.
Oyama, F., Murata, Y., Suganuma, N., Kimura, T, Titani, K., and Sekiguchi, K., 1989, Patterns of alternative splicing of fibronectin pre-mRNA in human adult and fetal tissues, Biochemistry 28:1428–1434.
Panayotou, G., End, P., Aumailley, M., Timpl, R., and Engel, J., 1989, Domains of laminin with growth-factor activity, Cell 56:93–101.
Patel, R. S., Odermatt, E., Schwarzbauer, J. E., and Hynes, R. O., 1987, Organization of the fibronec-tin gene provides evidence for exon shuffling during evolution, EMBO J. 6:2565–2572.
Pearson, C. A., Pearson, D., Shibahara, S., Hofsteenge, J., and Chiquet-Ehrismann, R., 1988, Ten-ascin: cDNA cloning and induction by TGF-beta, EMBO J. 7:2977–2982.
Penttinen, R. P., Kobayashi, S., and Bornstein, P., 1988, Transforming growth factor beta increases mRNA for matrix proteins both in the presence and in the absence of changes in mRNA stability, Proc. Natl. Acad. Sci. USA 85:1105–1108.
Pesciotta-Peters, D. M., Portz, L. M., Fullenwider, J., and Mosher, D. F., 1990, Co-assembly of plasma and cellular fibronectins into fibrils in human fibroblast cultures, J. Cell Biol. 111:249–256.
Pierschbacher, M. D., and Ruoslahti, E., 1984, Cell attachment activity of fibronectin can be dupli-cated by small synthetic fragments of the molecule, Nature 309:30–33.
Pierschbacher, M. D., and Ruoslahti, E., 1987, Influence of stereochemistry of the sequence agr-glyasp-xaa on binding specificity in cell adhesion, J. Biol. Chem. 262:17294–17298.
Preissner, K. T., and Müller-Berghaus, G., 1987, Neutralization and binding of heparin by S protein/vitronectin in the inhibition of factor Xa by antithrombin III. Involvement of an inducible heparin-binding domain of S protein/vitronectin, J. Biol. Chem. 262:12247–12253.
Prochownik, E. V., O’Rourke, K., and Dixit, V. M., 1989, Expression and analysis of COOH-terminal deletions of the human thrombospondin molecule, J. Cell Biol. 109:843–852.
Reiman, D., Tuomanen, E., Falkow, S., Golenbock, D. T., Saukkonen, K., and Wright, S. D., 1990, Recognition of a bacterial adhesion by an integrin: Macrophage CR3 (alpha M beta 2, CD11b/CD18) binds filamentous hemagglutinin of Bordetella pertussis, Cell 61:1375–1382.
Riou, J. F., Shi, D. L., Chiquet, M., and Boucaut, J.-C., 1990, Exogenous tenascin inhibits mesodermal cell migration during amphibian gastrulation, Dev. Biol. 137:305–317.
Roberts, D. D., and Ginsburg, V., 1988, Sulfated glycolipids and cell adhesion, Arch. Biochem. Biophys. 267:405–415.
Sakai, L. Y., Keene, D. R., and Engvall, E., 1986, Fibrillin, a new 350-kD glycoprotein is a component of extracellular microfibrils, J. Cell Biol. 103:2499–2509.
Sasaki, M., Kleinman, H. K., Huber, H., Deutzmann, R., and Yamada, Y., 1988, Laminin, a multidomain protein. The A chain has a unique globular domain and homology with the basement membrane proteoglycan and the laminin B chains, J. Biol. Chem. 263:16536–16544.
Silverstein, R. L., Asch, A. S., and Nachman, R. L., 1989, Glycoprotein IV mediates thrombospondin-dependent platelet—monocyte and platelet—U937 cell adhesion, J. Clin. Invest. 84:546–552.
Singer, I. I., Kawka, D. W., Scott, S., Mumford, R. A., and Lark, M. W., 1987, The fibronectin cell attachment sequence Arg-Gly-Asp-Ser promotes focal contact formation during early fibroblast attachment and spreading, J. Cell Biol. 104:573–584.
Singer, I. I., Scott, S., Kawka, D. W., Kazazis, D. M., Gailit, J., and Ruoslahti, E., 1988, Cell surface distribution of fibronectin and vitronectin receptors depends on substrate composition and extracellular matrix accumulation, J. Cell Biol. 106:2171–2182.
Sjoberg, B., Eriksson, M., Osterlund, E., Pap, S., and Osterlund, K., 1989, Solution structure of human plasma fibronectin as a function of NaC1 concentration determined by small-angle X-ray scattering, Eur. Biophys. J. 17:5–11.
Skubitz, A. P. N., McCarthy, J. B., Zhao, Q, Yi, X., and Furcht, L. T., 1990, Definition of a sequence, RYVVLPR, within laminin peptide F-9 that mediates metastatic fibrosarcoma cell adhesion and spreading, Cancer Res. 50:7612–7622.
Spiegel, S., Yamada, K. M., Hom, B. E., Moss, J., and Fishman, P. H., 1986, Fibrillar organization of fibronectin is expressed coordinately with cell surface gangliosides in a variant murine fibroblast, J. Cell Biol. 102:1898–1906.
Spring, J., Beck, K., and Chiquet-Ehrismann, R., 1989, Two contrary functions of tenascin: Dissection of the active sites by recombinant tenascin fragments, Cell 59:325–334.
Suzuki, S., Oldberg, A., Hayman, E. G., Pierschbacher, M. D., and Ruoslahti, E., 1985, Complete amino acid sequence of human vitronectin deduced from cDNA. Similarity of cell attachment sites in vitronectin and fibronectin, EMBO J. 4:2519–2524.
Tashiro, K., Sephel, G. C., Weeks, B., Sasaki, M., Martin, G. R., Kleinman, H. K., and Yamada, Y., 1989, A synthetic peptide containing the IKVAV sequence from the A chain of laminin mediates cell attachment, migration, and neurite outgrowth, J. Biol. Chem. 264:16174–16182.
Taylor, H. C., Lightner, V. A., Beyer, W. F., McCaslin, D., Briscoe, G., and Erickson, H. P., 1989, Biochemical and structural studies of tenascin/hexabrachion proteins, J. Cell. Biochem. 41:7190.
Thompson, L. K., Horowitz, P. M., Bentley, K. L., Thomas, D. D., Alderete, J. F., and Klebe, R. J., 1986, Localization of the ganglioside-binding site of fibronectin, J. Biol. Chem. 261:5209–5214.
Timpl, R., 1989, Structure and biological activity of basement membrane proteins, Eur. J. Biochem. 180:487–502.
Tomasini, B. R., and Mosher, D. F., 1991, Vitronectin, Prog. Hemost. Thromb. 10:269–305.
Varani, J., Nickoloff, B. J., Riser, B. L., Mitra, R. S., O’Rourke, K., and Dixit, V. M., 1988, Thrombo-spondin-induced adhesion of human keratinocytes, J. Clin. Invest. 81:1537–1544.
Vartio, T., Laitinen, L., Närvänen, O., Cutolo, M., Thornell, L. E., Zardi, L., and Virtanen, I., 1987, Differential expression of the ED sequence-containing form of cellular fibronectin in embryon-ic and adult human tissues, J. Cell Sci. 88:419–430.
Vischer P., Völker, W., Schmidt, A., and Sinclair, N., 1988, Association of thrombospondin of endothelial cells with other matrix proteins and cell attachment sites and migration tracks, Eur. J. Cell Biol. 47:36–46.
Wolff, C., and Lai, C. S., 1989, Fluorescence energy transfer detects changes in fibronectin structure upon surface binding, Arch. Biochem. Biophys. 268:536–545.
Woods, A., Couchman, J. R., Johansson, S., and Höök, M., 1986, Adhesion and cytoskeletal organisation of fibroblasts in response to fibronectin fragments, EMBO J. 5:665–670.
Yamada, K. M., 1989, Fibronectin structure, functions and receptors, Curr. Opinion Cell Biol. 1:956–963.
Yamada, K. M., and Kennedy, D. W., 1984, Dualistic nature of adhesive protein function: Fibronectin and its biologically active peptide fragments can autoinhibit fibronectin function, J. Cell Biol. 99:29–36.
Yamagata, M., Yamada, K. M., Yoneda, M., Suzuki, S., and Kimata, K., 1986, Chondroitin sulfate proteoglycan (PG-M-like proteoglycan) is involved in the binding of hyaluronic acid to cellular fibronectin, J. Biol. Chem. 261:13526–13535.
Yatohgo, T., Izumi, M., Kashiwagi, H., and Hayashi, M., 1988, Novel purification of vitronectin from human plasma by heparin affinity chromatography, Cell Struct. Funct. 13:281–292.
Yurchenco, P. D., Cheng, Y. S., and Schittny, J. C., 1990, Heparin modulation of laminin polymeriza-tion, J. Biol. Chem. 265:3981–3991.
Zhu, B. C., and Laine, R. A., 1985, Polylactosamine glycosylation on human fetal placental fibronectin weakens the binding affinity of fibronectin to gelatin, J. Biol. Chem. 260:4041–4045.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1991 Springer Science+Business Media New York
About this chapter
Cite this chapter
Yamada, K.M. (1991). Fibronectin and Other Cell Interactive Glycoproteins. In: Hay, E.D. (eds) Cell Biology of Extracellular Matrix. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3770-0_5
Download citation
DOI: https://doi.org/10.1007/978-1-4615-3770-0_5
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-6680-5
Online ISBN: 978-1-4615-3770-0
eBook Packages: Springer Book Archive