Abstract
Since the early 1970’s, interest in fibronectin has increased steadily, and there is now a massive literature on the structure and functional attributes of this complex molecule (see reviews 1–3)o Although its absence or depletion from the surface of transformed cells first brought fibronectin to the attention of those interested in tumour formation and invasion,the fact that it has significant roles to play in the adhesion and migration of normal cells has widened the field to include connective tissue, developmental biology and more recently molecular biology. Fibronectin is now the most studied of all connective tissue components and two major attributes make this glycoprotein of particular interest. Firstly, the glycoprotein has the capacity to bind other connective tissue components and cell surfaces through a series of domains joined by more flexible regions1 (Fig. l). The implication of this is that fibronectin is ideally suited for a role in mediating cell attachment (whether eukaryotic or prokar- yotic) to collagenous extracellular matrices. Secondly, the molecule is widespread in vivo, deposited in connective tissues and basement membranes and present in a soluble form in many body fluids including plasma, cerebrospinal and amniotic fluids.1–3
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References
K.M. Yamada, Cell surface interactions with extracellular materials, Ann. Rev. Biochem 52:761 (1983).
D.F. Mosher, Physiology of fibronectin, Ann. Rev. Med. 35:561 (1984).
R.O. Hynes, Fibronectin and its relation to cellular structure and behavior, in. “Cell Biology of Extracellular Matrix”, E.D. Hay, ed., Plenum Press, New York (1981).
A. Vaheri and D.F. Mosher, High molecular weight cell surface- associated glycoprotein (fibronectin) lost in malignant transformation, Biochim. Biophys. Acta 516:1 (1978).
R.O. Hynes and K.M. Yamada, Fibronectins: Multi-functional modular glycoproteins, J. Cell Biol. 95:369 (1982).
E. Engvall, E. Ruoslahti, and E.J. Miller, Affinity of fibronectin to collagens of different genetic types and to fibrinogen, J. Exp. Med. 147:1584 (1978).
F. Jilek and Hc Hormann, Cold-insoluble globulin (fibronectin) IV. Affinity to soluble collagen of various types, Hoppe- Seylerls Z. Physiol. Chem. 359:247 (1978).
L.I. Gold, B. Frangione, and E. Pearlstein, Biochemical and immunological characterization of three binding sites on human plasma fibronectin with different affinities for heparin, Biochemistry 22:4113 (1983).
I.V. Ali and R.O. Hynes, Effects of LETS glycoprotein on cell motility, Cell 14:439 (1978).
J.R. Couchman, D.A. Rees, M.R. Green, and C.G. Smith, Fibronectin has a dual role in locomotion and anchorage of primary chick fibroblasts and can promote entry into the division cycle, J. Cell Biol. 93:402 (1982).
G. Froman, L. Switalski, A. Faris, T. Wadstrom, and M. Hook, Binding of E© coli to fibronectin - A mechanism of tissue adherence, J. Biol. Chem. In Press (1985).
S.K. Akiyama and M.D. Johnson, Fibronectin in evolution: Presence in invertebrates and isolation from Microciona prolifera, Comp. Biochem. Physiol. B. 76:687 (1983).
J.E. Schwarzbauer, J.W. Tamkun, I.R. Lemischka, and R.O, Hynes, Three different fibronectin mRNAs arise by alternative splicing within the coding region, Cell 35:421 (1983).
A.R. Kornblihtt, K. Vibe-Pedersen, and F.E. Baralle, Human fibronectin: molecular cloning evidence for two mRNA species differing by an internal segment coding for a structural domain, EMBO J. 3:221 (1984).
J.W. Tamkun, J.E. Schwarzbauer, and R.O. Hynes, A single rat fibronectin gene generates three different mRNAs by alternative splicing of a complex exon, Proc. Natl. Acad. Sci. U.S.A. 81:5140 (1984).
K. Sekiguchi and S. Hakomori, Functional domain structure of fibronectin, Proc. Natl. Acad. Sci. U.S.A. 77:2661 (1980).
J.R. Couchman, M. Hook, D.A. Rees, and R. Timpl, Adhesion, growth and matrix production by fibroblasts on laminin substrates, J. Cell Biol, 96:177 (1983).
D.M. Scott, J.C. Murray, and M.J. Barnes, Investigation of the attachment of bovine corneal endothelial cells to coll- agens and other components of the subendothelium, Exp. Cell Res, 144:472 (1983).
M. Hook, K. Rubin, A. Oldberg, B. Obrink, and A. Vaheri, Cold-insoluble globulin mediates the adhesion of rat liver cells to plastic petri dishes, Biochem. Biophys. Res. Commun. 79:726 (1977).
R.A. Badley, J.R. Couchman, and D.A. Rees, Comparison of the cell cytoskeleton in migratory and stationary chick fibroblasts, J. Muscle Res. Cell Motility 1:5 (1980).
J.R. Couchman, M. Lenn, and D.A. Rees, Coupling of cytoskeleton functions for fibroblast locomotion, Eur. J. Cell Biol. In Press (1985).
R.J. Beyth and L.A. Culp, Complementary adhesive responses of human skin fibroblasts to the cell-binding domain of fibronectin and the heparan sulfate-binding protein, platelet factor-4, Exp. Cell Res. 155:537 (1984).
J.E. Doran, A.R. Mansberger, and A.C. Pease, Cold-insoluble globulin-enhanced phagocytosis of gelatinized targets by macrophage monolayers: A model system, J. Retic. Soc. 27:471 (1980).
F.A. Blumenstock, T.M. Saba, P. Weber, and R. Laffin, Biochemical and immunological characterization of human opsonic «2 SB glycoprotein: Its identity with cold- insoluble globulin, J. Biol. Chem. 253:4287 (1978).
F. Jilek and H. Hormann, Cold-insoluble globulin. III. Cyanogen bromide and plasminolysis fragments containing a label introduced by transamidation, Hoppe-Seyler’s Z. Physiol. Chem. 358:1165 (1977).
A.B. Robbins, J.E. Doran, A.C. Reese, A.R. Mansberger, Cold-insoluble globulin levels in operative trauma: serum depletion, wound sequestration and biological activity: an experimental and clinical study, Am. Surg. 46:663 (1980).
R.A.F. Clark, H.J. Winn, H.F. Dvorak, and R.P. Colvin, Fibronectin beneath reepithelializing epidermis in vivo; sources and significance, J. Invest. Dermatol. 80:265 (1983).
R.A.F. Clark, P. DellaPelle, E. Manseau, J.M. Lanigan, H.F. Dvorak, and R.Bo Colvin, Blood vessel fibronectin increases in conjunction with endothelial cell proliferation and capillary ingrowth during wound healing, J. Invest. Dermatol. 79:269 (1982).
J.R. Couchman, W.T. Gibson, Do Thorn, A.C. Weaver, D.A. Rees, and W.E. Parish, Fibronectin distribution in epithelial and associated tissues of the rat. Arch. Dermatol. Res, 266:295 (1979).
W.T. Gibson, J.R. Couchman, and A.C. Weaver, Fibronectin distribution during the development of fetal rat skin, J. Invest, Dermatol, 8l:480 (1983).
D.R. Critchley, M.A. England, J. Wakely, and R.O. Hynes, Distribution of fibronectin in the ectoderm of gastrul- ating embryos, Nature, Lond. 280:498 (1979)«.
B.W. Mayer, E.D. Hay, and R.O. Hynes, Immunocytochemical localization of fibronectin in embryonic chick trunk and area vasculosa, Dev. Biol, 82:267 (l98l).
J. Heasman, R.O. Hynes, A.P. Swan, V, Thomas, and C.C. Wylie, Primordial germ cells of Xenopus embryos: the role of fibronectin in their adhesion during migration, Cell 27: 437 (1981).
J.C. Boucaut, T. Darnibere, H. Boulebache, and J.P. Thiery, Prevention of gastrulation but not neuralation by antibodies to fibronectin in amphibian embryos, Nature, Lond. 307:364 (1984).
J.P. Thiery, J.-L. Duband, A. Delouvee, G. Tucker, H. Aoyama, T.J. Poole, and K.M. Yamada© Ontogeny of the peripheral nervous system, J. Embryol. exp. Morphol. 82:35 (1984).
G.A. Dunn, Contact guidance of cultured tissue cells: a survey of potentially relevant properties of the substratum, in “Cell Behaviour”, R. Bellairs, A.S.G. Curtis, G.A. Dunn, eds., Cambridge University Press, Cambridge (1982).
D.C. Turner, J. Lawton, P. Dollenmeier, R. Ehrismann, and M. Chiquet, Guidance of myogenic cell migration by oriented deposits of fibronectin, Dev. Biol. 95: 497(1983).
A. Baron-Von Evercooren, H.K. Kleinman, S. Ohno, P. Marangos, I.P. Schwartz, and M.E. Dubois-Dalcq, Nerve growth factor, laminin and fibronectin promote neurite outgrowth in human fetal sensory ganglion cultures, J. Neurosci. Res. 8:179 (1982).
R.O. Hynes and A.T. Destree, Relationships between fibronectin (LETS protein) and actin, Cell 15:875 (1977).
V.-P. Lehto, T. Vartio, and I. Virtanen, Fibronectin remains in the cytoskeletal preparations of cultured human fibroblasts, Cell Biol. Int. Rep. 5:417 (1981).
J.D. Aplin, R.C. Hughes, C.L. Jaffe, and N. Sharon, Reversible cross-linking of cellular components of adherent fibroblasts to fibronectin and lectin-coated substrata, Exp. Cell Res. 134:488 (1981).
H.K. Kleinman, G.R. Martin, and P.HC Fishman, Ganglioside inhibition of fibronectin-mediated cell adhesion to collagen, Proc. Natl. Acad. Sci. U.S.A. 76:3367 (1979).
P.J. Brown and R.L. Juliano, Admodulin: A cell surface glycoprotein specifically involved in fibronectin-mediated adhesion, J. Cell Biol. 99:16la (1984).
T. Hasegawa, E. Hasegawa, W.-T. Chen, and K.M. Yamada, Characterization of a membrane glycoprotein complex implicated in cell adhesion to fibronectin, J. Cell Biol. 99:165a (1984).
R.C. Hughes, S.D.J. Pena, J. Clark, and R.R. Dourmashkin, Molecular requirements for the adhesion and spreading of hamster fibroblasts, Exp. Cell Res. 121:307 (1979).
L. Kjellen, I. Pettersson, and M. Hook, Cell-surface heparan sulfate: an intercalated membrane proteoglycan, Proc. Nat. Acad. Sci. U.S.A. 78:5371 (1981).
A.C. Rapraeger and M. Bernfield, Heparan sulfate proteoglycans from mouse mammary epithelial cells, J. Biol. Chem. 258: 3632 (1983).
L.S. Fransson, I. Carlstedt, L. Coster, and A. Malmstrom, Structure and function of cell-surface associated proteo- heparan sulphate, Eur. J. Cell Biol. 1:18 (1983).
A. Woods, M. Hook, L. Kjellen, C.G. Smith, and D.A. Rees, Relationship of heparan sulfate proteoglycans to the cytoskeleton and extracellular matrix of cultured fibroblasts, J. Cell Biol. 99:1743 (1984).
A. Woods, J.R. Couchman, M. Hook, and So Johansson, Adhesion and cytoskeletal organisation of fibroblasts in response to fibronectin peptides. In Preparation.
M.D. Pierschbacher and E. Ruoslahti, Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule, Nature, Lond. 309:30 (1984).
S. Johansson, Demonstration of high affinity fibronectin-receptors on rat hepatocytes in suspension, J. Biol. Chem. In Press (1985).
A. Garcia-Pardo, E. Pearlstein, and B. Frangione, Primary structure of human plasma fibronectin. The 29,000-dalton NHterminal domain, J. Biol. Chem. 258:12670 (1983).
K. Sekiguchi, S. Hakomori, M. Funahashi, I. Matsumoto, and N. Seno, Binding of fibronectin and its proteolytic fragments to glycosaminoglycans, J. Biol. Chem. 258:14359 (1983).
R. Timpl, H. Rohde, P.Go Robey, S.I. Rennard, J.M. Foidart, and G.R. Martin, Laminin - A glycoprotein from basement membranes, J. Biol. Chem. 254:9933 (1979).
D. Edgar, R. Timpl, and H. Thoenen, The heparin-binding domain of laminin is responsible for its effects on neurite outgrowth and neuronal survival, EMBO J. 3:1463 (1984).
R. Timpl, S. Johansson, V. van Delden, I. Oberbaumer, and M. Hook, Characterization of protease-resistant fragments of laminin mediating attachment and spreading of rat hepatocytes, J. Biol. Chem. 258:8922 (1983).
J. Jilek and H. Hormann, Fibronectin (cold-insoluble globulin). VI. Influence of heparin and hyaluronic acid on the binding of native collagen, Hoppe-Seyler’s Z. Physiol. Chem. 360:597 (1979).
M.H. Ginsberg, R.G. Painter, J. Forsyth, C. Birdwell, and E.F. Plow, Thrombin increases expression of fibronectin antigen on the platelet surface, Proc. Natl. Acad. Sci. U.S.A. 77:1049 (1980).
W.T. Gibson, J.R. Couchman, R.A. Badley, H.J. Saunders, and C.G. Smith, Fibronectin in cultured rat keratinocytes: distribution, synthesis, and relationship to cytoskeletal proteins, Eur. J. Cell Biol. 30:205 (1983).
D.J. Donaldson and J.T. Mahan, Fibrinogen and fibronectin as substrates for epidermal cell migration during wound closure, J. Cell Sci. 62:117 (1983).
J.R. Couchman and S. Blencowe, Adhesion and cell surface relationships during fibroblast and epithelial migration in vitro, in “Cell Traffic in the Developing and Adult Organism”, G. Haemmerli and P. Strauli, eds., Karger, Basel. In Press (1985).
A.E. Postlethwaite, J. Keski-Oja, G. Balian, and A.H. Kang, Induction of fibroblast chemotaxis by fibronectin. Localization of the chemotactic region to a 140,000- molecular weight non-gelatin-binding fragment, J. Exp. Med. 15:194 (1981).
H.E.J. Seppa, K.M. Yamada, S.T. Seppa, M.H. Silver, H.K. Kleinman, and E. Schiffman, The cell binding fragment of fibronectin is chemotactic for fibroblasts, Cell Biol. Int. Rep. 5:813 (1981).
M.B. Furie and D.B. Rifkin, Proteolytically derived fragments of human plasma fibronectin and their localization within the intact molecule, J. Biol. Chem. 255:3134 (1980).
I.I. Singer, D.W. Kawka, D.M. Kazazis, and R.A.F. Clark, In vivo co-distribution of fibronectin and actin fibers in granulation tissue: immunofluorescence and electron microscope studies of the fibronexus at the myofibroblast surface, J. Cell Biol. 98:2091 (1984).
M. Kurkinen, A. Vaheri, P.J. Roberts, and S. Steinman, Sequential appearance of fibronectin and collagen in experimental granulation tissue, Lab. Invest. 43:47 (1980).
M.W. Lark and L.A. Culp, Multiple classes of heparan sulfate proteoglycans from fibroblast substratum adhesion sites, J. Biol. Chem. 259:6773 (1984).
M. Hook, L. Kjellen, S. Johansson, and J. Robinson, Cell surface glycosaminoglycans, Ann. Rev. Biochem. 53:847 (1984).
A. Woods, J«R. Couchman, and M. Hook, Heparan sulfate proteoglycans of rat embryo fibroblastSo A hydrophobic form may link cytoskeleton and matrix components, J. Biol. Chem. Submitted.
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© 1986 Plenum Press, New York
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Couchman, J.R., Woods, A. (1986). Fibronectin: Role in Cell Surface Interactions. In: Crawford, N., Taylor, D.E.M. (eds) Interaction of Cells with Natural and Foreign Surfaces. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-2229-0_3
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