1: Invest Clin. 2007 Jun;48(2):249-62.


[Fibronectin. Structure and functions associated to hemostasis. Review]

[Article in Spanish]

Lucena S, Arocha Piñango CL, Guerrero B.

Laboratorio de Fisiopatología, Centro de Medicina Experimental, Instituto Venezolano de Investigaciones Científicas (IVIC), Caracas, Venezuela.

Fibronectin is an adhesive glycoprotein present in a soluble form in plasma and in an insoluble form in the extracellular matrix of many tissues. The human plasma level of this protein is about 300 +/- 100 microg/mL. It is synthesized and secreted by a wide variety of cells, consequently is one of the components of greater distribution in the body that participates in the biochemical reactions of diverse physiological and pathological processes. Due to the presence of multifunctional domains in its structure, fibronectin interacts with diverse components of the coagulation and fibrinolysis. It may bind to collagen, fibrinogen, fibrin, heparin, factor XIII and platelets, among others, regulating processes of importance in hemostasis such as: platelet adhesion and aggregation, tissue remodelling during wound healing, and activation of fibrinolysis by the plasminogen activators.

Publication Types:
English Abstract
Review

PMID: 17598647 [PubMed - indexed for MEDLINE]

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2: Arterioscler Thromb Vasc Biol. 1998 Sep;18(9):1363-70.


Fibronectin: structure, assembly, and cardiovascular implications.

Magnusson MK, Mosher DF.

Department of Medicine, University of Wisconsin-Madison, 53706, USA.

Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 9743223 [PubMed - indexed for MEDLINE]

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3: Virchows Arch. 1996 Dec;429(6):311-22.


Molecular variants of fibronectin and laminin: structure, physiological occurrence and histopathological aspects.

Kosmehl H, Berndt A, Katenkamp D.

Institute of Pathology, Friedrich Schiller University, Jena, Germany.

This review deals with biological and pathological aspects of various isoforms of the matrix molecules fibronectin and laminin. They are generated by different molecular mechanisms: ED-A+ and ED-B+ fibronectin by alternative splicing of pre mRNA, de novo-glycosylated fibronectin by alternative post-translational O-linked glycosylation of the IIICS region, and the laminin isoforms by exchange of single chains of the heterotrimeric molecule. In contrast to the "common" fibronectin, the distribution of ED-B+ and de novo-glycosylated fibronectin is restricted to embryonic tissues; they subsequently reappear in granulation tissue, in fibrosing processes and in tumour stroma. The expression of these so-called oncofetal fibronectins is stimulated by growth factors (TGF beta). The association of the ED-B+ fibronectin with proliferative activity and newly formed vessels identifies this fibronectin variant as a marker of cellular activity in the process of fibrosis and as a suitable agent for the evaluation of tumour angioneogenesis. Initial results suggest a correlation between the amount of ED-B+ and de novo-glycosylated fibronectin in tumour stroma and the behaviour of carcinomas with regard to their invasiveness and propensity for metastatic dissemination. The current nomenclature of the laminin molecule family is presented. The laminin chain constitution of basement membranes switches from embryonic or proliferatively active to adult terminally differentiated tissues [disappearance of the laminin beta 2 (s) chain] and depends on the tissue type. The discrepancy between the loss of basement membranes (multiple basement membrane defects) in carcinomas and the recently reported increased laminin chain synthesis in these tumours may be explained by abundant laminin chain deposition outside the basement membrane in the carcinoma invasion front, possibly associated with enhanced adhesion of budding tumour cells.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 8982375 [PubMed - indexed for MEDLINE]

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4: Matrix Biol. 1996 Nov;15(5):313-20; discussion 321.


Structure and function of fibronectin modules.

Potts JR, Campbell ID.

Department of Biochemistry, University of Oxford, UK.

Fibronectin is an important component of the extracellular matrix and is involved in a diverse range of physiological processes. It is a mosaic protein composed almost entirely of three types of module, F1, F2 and F3. Although the structures of single F1, F2 and F3 modules have been available for a number of years, in many cases the key to understanding the structure-function relationships in fibronectin and other proteins containing these modules lies in studies of module pairs and larger domains. This review focuses on recent advances in the understanding of the structure and function of fibronectin modules.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 8981327 [PubMed - indexed for MEDLINE]

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5: Curr Opin Cell Biol. 1994 Oct;6(5):648-55.


Fibronectin structure and assembly.

Potts JR, Campbell ID.

Department of Biochemistry, University of Oxford, UK.

Significant progress has been made recently in the determination of the structure and assembly of the important matrix protein fibronectin, a molecule mainly constructed from three modular units denoted Fn1, Fn2 and Fn3. Atomic resolution structures are now available for all three single modules, for Fn1 and Fn3 module pairs, and for the disulphide-linked join between fibronectin monomers. Combined with results from new binding and mutation studies, the new structural information is leading to a clearer view of structure/function relationships in intact fibronectin.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 7833045 [PubMed - indexed for MEDLINE]

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6: Indian J Biochem Biophys. 1990 Apr;27(2):63-8.


Structure and properties of fibronectin.

Khan MY.

Department of Biochemistry, School of Life Sciences, North-Eastern Hill University, Shillong.

Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Review

PMID: 2191916 [PubMed - indexed for MEDLINE]

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7: Australas J Dermatol. 1990;31(1):47-56.


Fibronectin: structure, function and significance in wound healing.

Brotchie H, Wakefield D.

Department of Immunopathology, Prince Henry Hospital, Little Bay, NSW.

Several recent reports suggest a therapeutic role for topical application of autologous fibronectin in promoting healing of chronic skin and corneal ulcers. Fibronectin assists in wound healing by contributing to haemostasis, assisting in control of infection and debridement of wounds, and promoting re-epithelialisation, granulation tissue and ultimately a connective tissue of adequate tensile strength to repair the skin defect. The potential for fibronectin to be a therapeutic adjunct demands a close understanding of its structural and functional properties, and such knowledge, particularly emerging from research reported in the last five years, is reviewed.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 2073208 [PubMed - indexed for MEDLINE]

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8: Vestn Dermatol Venerol. 1989;(4):31-4.


[Connective tissue fibronectin: its structure, synthesis and metabolism]

[Article in Russian]

Kovalev VM, Krivenko ZF.

Publication Types:
Review

PMID: 2669410 [PubMed - indexed for MEDLINE]

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9: J Parodontol. 1987 Nov;6(4):297-309.


[Fibronectin, structure and properties: current concepts]

[Article in French]

Martin G, Bene MC, Faure G, Ambrosini P, Jully JM.

Publication Types:
English Abstract
Review

PMID: 3330131 [PubMed - indexed for MEDLINE]

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10: Rev Infect Dis. 1987 Jul-Aug;9 Suppl 4:S317-21.


Fibronectin: a brief overview of its structure, function, and physiology.

Proctor RA.

Department of Medicine, University of Wisconsin, Madison.

Fibronectin is a large glycoprotein that is composed of blocks of three types of repeating, homologous peptide sequences. Several of the homologous blocks form functional domains that are organized in a linear array on two nearly identical subunit arms. Specific domains allow fibronectin to promote cell-to-cell adhesion, cell-to-basement-membrane attachment, clot stabilization, embryogenesis, nerve regeneration, fibroblast migration, macrophage function, and pathogen (virus, fungus, bacteria, and protozoa) binding to mammalian cells and extracellular matrix. Thus, this complex and multifunctional protein is involved in the pathogenesis of infections from the initiation of the infection through the final stages of wound healing.

Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 3326130 [PubMed - indexed for MEDLINE]

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11: Vutr Boles. 1987;26(5):12-5.


[Fibronectin--its clinical importance, chemical structure and biological interactions]

[Article in Bulgarian]

Ivanov V, Chernev K, Shipkov T.

Publication Types:
Review

PMID: 3324485 [PubMed - indexed for MEDLINE]

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12: Ryumachi. 1985 Nov;25(5):381-93.


[Fibronectin--functions, structure, immunological aspects and relation to collagen disease]

[Article in Japanese]

Watanabe Y, Nishikawa J.

Publication Types:
Review

PMID: 3914090 [PubMed - indexed for MEDLINE]

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13: Tanpakushitsu Kakusan Koso. 1983 Mar;28(3):169-81.


[Structure of fibronectin molecule and gene]

[Article in Japanese]

Hayashi M, Hirano H.

Publication Types:
Review

PMID: 6342049 [PubMed - indexed for MEDLINE]

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14: Coll Relat Res. 1981;1(1):95-128.


Fibronectin: current concepts of its structure and functions.

Ruoslahti E, Engvall E, Hayman EG.

Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 7049547 [PubMed - indexed for MEDLINE]

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15: J Supramol Struct Cell Biochem. 1981;16(4):345-8.


The structure of fibronectin and its role in cellular adhesion.

Akiyama SK, Yamada KM, Hayashi M.

Fibronectin is a large, adhesive glycoprotein which is found in a number of locations, most notably on cell surfaces, in extracellular matrixes, and in blood. Fibronectin had been detected in all vertebrates tested and in many invertebrates. Its presence in sponges is significant because this suggests that fibronectin may have appeared very early in evolution, possibly with the most primitive multicellular organisms. Cellular and plasma fibronectins have many striking similarities. However, the locations of the polypeptide chain differences between these two proteins indicate that plasma fibronectin cannot be derived from cellular fibronectin by means of simple post-translational proteolysis. Instead, these different types of fibronectin may be products of different genes or of differentially spliced messenger RNA molecules. Amniotic fluid fibronectin is possibly a third form of the protein. Cellular and plasma fibronectins are composed of at least six protease-resistant domains which contain specific binding sites for actin, gelatin, heparin, Staphylococcus aureus, transglutaminase, fibrin, DNA, and a cell surface receptor. The relative locations of these domains have been mapped in the primary structure of fibronectin. The cell surface receptor for fibronectin has not been positively identified, but may be a glycoprotein, a glycolipid, or a complex of the two. Although cell-substratum adhesion is mediated by fibronectin, the locations of the areas of closest approach of the cell to the substratum (the adhesion plaques) and fibronectin are not coincident under conditions of active cell growth. Under conditions of cell growth arrest in low serum concentrations, some fibronectin may become localized at the adhesion plaques. Models describing the domain structure of fibronectin and the molecular organization of the adhesion plaque area are presented.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 6273596 [PubMed - indexed for MEDLINE]

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16: Blood. 1980 Aug;56(2):145-58.


The structure and biologic activities of plasma fibronectin.

Mosesson MW, Amrani DL.

Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 6994838 [PubMed - indexed for MEDLINE]

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17: Mol Cell Biochem. 1980 Feb 8;29(2):103-28.


Fibronectin: a review of its structure and biological activity.

Pearlstein E, Gold LI, Garcia-Pardo A.

Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 6988694 [PubMed - indexed for MEDLINE]