Skip to main content

Transferrin

  • Living reference work entry
  • First Online:
Encyclopedia of Signaling Molecules

Synonyms

Beta-1 metal-binding globulin; PRO1400; PRO1557; PRO2086; Serotransferrin; Siderophilin; TF; TFQTL1; Transferrin

Historical Background

Transferrin is a secreted glycoprotein that transports ferric iron (Fe3+) from extracellular fluids to tissues. It was first documented as “iron-binding component” of human blood plasma back in 1946. The “iron-binding component” was subsequently purified, biochemically characterized, and named transferrin. A similar protein from egg white (ovotransferrin) was previously reported to inhibit bacterial and yeast growth via its iron-binding capacity. A historical account of the early discovery and characterization of transferrin can be found in an excellent review article (Morgan 1981). Functional studies demonstrated that plasma transferrin delivers iron to developing erythroid cells upon binding to cell surface transferrin receptors. The mechanism involves internalization of iron-loaded transferrin within the recipient cell, release of iron...

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Institutional subscriptions

References

  • Bailey S, Evans RW, Garratt RC, Gorinsky B, Hasnain S, Horsburgh C, et al. Molecular structure of serum transferrin at 3.3-A resolution. Biochemistry. 1988;27:5804–12.

    Article  CAS  PubMed  Google Scholar 

  • Barber MF, Elde NC. Nutritional immunity. Escape from bacterial iron piracy through rapid evolution of transferrin. Science. 2014;346:1362–6. doi:10.1126/science.1259329.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Bartnikas TB. Known and potential roles of transferrin in iron biology. Biometals. 2012;25:677–86. doi:10.1007/s10534-012-9520-3.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Bennett MJ, Lebron JA, Bjorkman PJ. Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor. Nature. 2000;403:46–53.

    Article  CAS  PubMed  Google Scholar 

  • Cheng Y, Zak O, Aisen P, Harrison SC, Walz T. Structure of the human transferrin receptor-transferrin complex. Cell. 2004;116:565–76.

    Article  CAS  PubMed  Google Scholar 

  • de Tayrac M, Roth MP, Jouanolle AM, Coppin H, le Gac G, Piperno A, et al. Genome-wide association study identifies TF as a significant modifier gene of iron metabolism in HFE hemochromatosis. J Hepatol. 2015;62:664–72. doi:10.1016/j.jhep.2014.10.017.

    Article  PubMed  Google Scholar 

  • Forni GL, Pinto V, Musso M, Mori M, Girelli D, Caldarelli I, et al. Transferrin-immune complex disease: a potentially overlooked gammopathy mediated by IgM and IgG. Am J Hematol. 2013;88:1045–9. doi:10.1002/ajh.23558.

    Article  CAS  PubMed  Google Scholar 

  • Ganz T. Systemic iron homeostasis. Physiol Rev. 2013;93:1721–41. doi:10.1152/physrev.00008.2013. [pii] 93/4/1721.

    Article  CAS  PubMed  Google Scholar 

  • Gkouvatsos K, Papanikolaou G, Pantopoulos K. Regulation of iron transport and the role of transferrin. Biochim Biophys Acta. 2012;1820:188–202. doi:10.1016/j.bbagen.2011.10.013. [pii] S0304-4165(11)00267-4.

    Article  CAS  PubMed  Google Scholar 

  • Gomme PT, McCann KB, Bertolini J. Transferrin: structure, function and potential therapeutic actions. Drug Discov Today. 2005;10:267–73. doi:10.1016/S1359-6446(04)03333-1.

    Article  CAS  PubMed  Google Scholar 

  • Harris WR. Anion binding properties of the transferrins. Implications for function. Biochim Biophys Acta. 2012;1820:348–61. doi:10.1016/j.bbagen.2011.07.017.

    Article  CAS  PubMed  Google Scholar 

  • Hayashi A, Wada Y, Suzuki T, Shimizu A. Studies on familial hypotransferrinemia: unique clinical course and molecular pathology. Am J Hum Genet. 1993;53:201–13.

    CAS  PubMed  PubMed Central  Google Scholar 

  • Klausner RD, Ashwell G, van Renswoude J, Harford JB, Bridges KR. Binding of apotransferrin to K562 cells: explanation of the transferrin cycle. Proc Natl Acad Sci USA. 1983;80:2263–6.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Lambert LA. Molecular evolution of the transferrin family and associated receptors. Biochim Biophys Acta. 2012;1820:244–55. doi:10.1016/j.bbagen.2011.06.002.

    Article  CAS  PubMed  Google Scholar 

  • MacGillivray RT, Mendez E, Shewale JG, Sinha SK, Lineback-Zins J, Brew K. The primary structure of human serum transferrin. The structures of seven cyanogen bromide fragments and the assembly of the complete structure. J Biol Chem. 1983;258:3543–53.

    CAS  PubMed  Google Scholar 

  • Morgan EH. Transferrin: biochemistry, physiology and clinical significance. Mol Asp Med. 1981;4:1–23.

    Article  Google Scholar 

  • Pantopoulos K. TfR2 links iron metabolism and erythropoiesis. Blood. 2015;125:1055–6. doi:10.1182/blood-2014-12-617571.

    Article  CAS  PubMed  Google Scholar 

  • Vincent JB, Love S. The binding and transport of alternative metals by transferrin. Biochim Biophys Acta. 2012;1820:362–78. doi:10.1016/j.bbagen.2011.07.003.

    Article  CAS  PubMed  Google Scholar 

  • Yang F, Lum JB, McGill JR, Moore CM, Naylor SL, van Bragt PH, et al. Human transferrin: cDNA characterization and chromosomal localization. Proc Natl Acad Sci USA. 1984;81:2752–6.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Zakin MM. Regulation of transferrin gene expression. FASEB J. 1992;6:3253–8.

    CAS  PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Kostas Pantopoulos .

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 2016 Springer Science+Business Media LLC

About this entry

Cite this entry

Papanikolaou, G., Gkouvatsos, K., Pantopoulos, K. (2016). Transferrin. In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-6438-9_101940-1

Download citation

  • DOI: https://doi.org/10.1007/978-1-4614-6438-9_101940-1

  • Received:

  • Accepted:

  • Published:

  • Publisher Name: Springer, New York, NY

  • Print ISBN: 978-1-4614-6438-9

  • Online ISBN: 978-1-4614-6438-9

  • eBook Packages: Springer Reference Biomedicine and Life SciencesReference Module Biomedical and Life Sciences

Publish with us

Policies and ethics