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Fibronectin

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Encyclopedia of Signaling Molecules
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Synonyms

Cell spreading factor; Cell surface protein; Cold-insoluble globulin; Galactoprotein A; Humoral recognition factor; Large external transformation sensitive protein (LETS); Migration stimulating factor; Opsonic alpha-2 surface binding glycoprotein; Surface glycoprotein antigen

Historical Background

Fibronectin is a large glycoprotein found in plasma (plasma fibronectin) and the extracellular matrix (cellular fibronectin). The former type was initially named cold-insoluble globulin (Morrison et al. 1948). In the 1970s, several laboratories independently characterized cellular fibronectin, naming it surface glycoprotein antigen (Vaheri and Ruoslahti 1974), large external transformation sensitive protein (LETS) (Hynes and Bye 1974), and cell surface protein (Yamada and Weston 1974), among others. When the common identity of these proteins was recognized, the name fibronectin (from the Latin fibra, meaning “fiber” and nectere meaning “to bind”) was adopted.

Fibronectin is composed...

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References

  • Adams JC, Chiquet-Ehrismann R, Tucker RP. The evolution of tenascins and fibronectin. Cell Adhes Migr. 2015;9:22–33. doi:10.4161/19336918.2014.970030.

    Article  CAS  Google Scholar 

  • ffrench-Constant C, Hynes RO. Alternative splicing of fibronectin is temporally and spatially regulated in the chicken embryo. Development. 1989;106:375–88.

    CAS  PubMed  Google Scholar 

  • ffrench-Constant C, Van de Water L, Dvorak HF, Hynes RO. Reappearance of an embryonic pattern of fibronectin splicing during wound healing in the adult rat. J Cell Biol. 1989;109:903–14.

    Article  CAS  PubMed  Google Scholar 

  • George EL, Georges-Labouesse EN, Patel-King RS, Rayburn H, Hynes RO. Defects in mesoderm, neural tube and vascular development in mouse embryos lacking fibronectin. Development. 1993;119:1079–91.

    CAS  PubMed  Google Scholar 

  • Henderson B, Nair S, Pallas J, Williams MA. Fibronectin: a multidomain host adhesin targeted by bacterial fibronectin-binding proteins. FEMS Microbiol Rev. 2011;35:147–200. doi:10.1111/j.1574-6976.2010.00243.x.

    Article  CAS  PubMed  Google Scholar 

  • Hynes RO, Bye JM. Density and cell cycle dependence of cell surface proteins in hamster fibroblasts. Cell. 1974;3:113–20.

    Article  CAS  PubMed  Google Scholar 

  • Insua-Rodríguez J, Oskarsson T. The extracellular matrix in breast cancer. Adv Drug Deliv Rev. 2016;97:41–55. doi:10.1016/j.addr.2015.12.017.

    Article  PubMed  Google Scholar 

  • Leonova EI, Galzitskaya OV. Structure and functions of syndecans in vertebrates. Biochemistry (Mosc). 2013;78:1071–85. doi:10.1134/S0006297913100015.

    Article  CAS  Google Scholar 

  • Mackie EJ, Tucker RP, Halfter W, Chiquet-Ehrismann R, Epperlein HH. The distribution of tenascin coincides with pathways of neural crest cell migration. Development. 1988;102:237–50.

    CAS  PubMed  Google Scholar 

  • Martino MM, Hubbell JA. The 12th-14th type III repeats of fibronectin function as a highly promiscuous growth factor-binding domain. FASEB J. 2010;24:4711–21. doi:10.1096/fj.09-151282.

    Article  CAS  PubMed  Google Scholar 

  • Maurer LM, Ma W, Mosher DF. Dynamic structure of plasma fibronectin. Crit Rev Biochem Mol Biol. 2015;51:213–27. doi:10.1080/10409238.2016.1184224.

    Article  PubMed  Google Scholar 

  • Morrison PR, Edsall JT, Miller SG. Preparation and properties of serum and plasma proteins; the separation of purified fibrinogen from fraction I of human plasma. J Am Chem Soc. 1948;70:3103–8.

    Article  CAS  PubMed  Google Scholar 

  • Muro AF, Chauhan AK, Gajovic S, Iaconcig A, Porro F, Stanta G, Baralle FE. Regulated splicing of the fibronectin EDA exon is essential for proper skin wound healing and normal lifespan. J Cell Biol. 2003;162:149–60.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Ozbek S, Balasubramanian PG, Chiquet-Ehrismann R, Tucker RP, Adams JC. The evolution of extracellular matrix. Mol Biol Cell. 2010;21:4300–5. doi:10.1091/mbc.E10-03-0251.

    Article  PubMed  PubMed Central  Google Scholar 

  • Petersen TE, Thøgersen HC, Skorstengaard K, Vibe-Pedersen K, Sahl P, Sottrup-Jensen L, Magnusson S. Partial primary structure of bovine plasma fibronectin: three types of internal homology. Proc Natl Acad Sci U S A. 1983;80:137–41.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Pierschbacher MD, Ruoslahti E. Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature. 1984;309:30–3.

    Article  CAS  PubMed  Google Scholar 

  • Pytela R, Pierschbacher MD, Ruoslahti E. Identification and isolation of a 140 kd cell surface glycoprotein with properties expected of a fibronectin receptor. Cell. 1985;40:191–8.

    Article  CAS  PubMed  Google Scholar 

  • Qian P, Zuo Z, Wu Z, Meng X, Li G, Wu Z, et al. Pivotal role of reduced let-7g expression in breast cancer invasion and metastasis. Cancer Res. 2011;71:6463–74. doi:10.1158/0008-5472.CAN-11-1322.

    Article  CAS  PubMed  Google Scholar 

  • Schwarzbauer JE, DeSimone DW. Fibronectins, their fibrillogenesis, and in vivo functions. Cold Spring Harb Perspect Biol. 2011;3(7). doi:10.1101/cshperspect.a005041.

    Google Scholar 

  • Tamkun JW, DeSimone DW, Fonda D, Patel RS, Buck C, Horwitz AF, Hynes RO. Structure of integrin, a glycoprotein involved in the transmembrane linkage between fibronectin and actin. Cell. 1986;46:271–82.

    Article  CAS  PubMed  Google Scholar 

  • Vaheri A, Ruoslahti E. Disappearance of a major cell-type specific surface glycoprotein antigen (SF) after transformation of fibroblasts by Rous sarcoma virus. Int J Cancer. 1974;13:579–86.

    Article  CAS  PubMed  Google Scholar 

  • Vega ME, Schwarzbauer JE. Collaboration of fibronectin matrix with other extracellular signals in morphogenesis and differentiation. Curr Opin Cell Biol. 2016;42:1–6. doi:10.1016/j.ceb.2016.03.014.

    Article  CAS  PubMed  Google Scholar 

  • Yamada KM, Weston JA. Isolation of a major cell surface glycoprotein from fibroblasts. Proc Natl Acad Sci U S A. 1974;71:3492–6.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

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Correspondence to Richard P. Tucker .

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Tucker, R.P. (2016). Fibronectin. In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-6438-9_101621-1

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  • DOI: https://doi.org/10.1007/978-1-4614-6438-9_101621-1

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