Encyclopedia of Cancer

Living Edition
| Editors: Manfred Schwab

Thioredoxin System

  • Elias S. J. Arnér
  • Arne Holmgren
Living reference work entry
DOI: https://doi.org/10.1007/978-3-642-27841-9_5777-3

Synonyms

Definition

Thioredoxin (Trx) is a small dithiol-disulfide oxidoreductase existing in all living cells. The thioredoxin system is comprised of Trx, NADPH, and thioredoxin reductase (TrxR) and functions as the cells’ major NADPH-dependent protein disulfide reductase. Trx has numerous functions in cell growth such as the electron donor for ribonucleotide reductase, which is essential for DNA synthesis and repair. Reduced Trx is alo central in antioxidant defense, regulation of transcription factors such as p53, or apoptosis inhibition of ASKI. Trx80 is truncated thioredoxin comprising the 80 or 84 N-terminal amino acids of human cytosolic Trx. TrxR is an essential flavoprotein with a catalytic selenocysteine residue, which is a target for many chemotherapeutic drugs. Both Trx and TrxR are upregulated in most but not all forms of cancer.

Characteristics

Trx contains a conserved active site...

Keywords

Protein Disulfide Isomerase Ribonucleotide Reductase Selenium Compound Dehydroascorbic Acid Gold Compound 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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References

  1. Arnér ESJ, Holmgren A (2000) Physiological functions of thioredoxin and thioredoxin reductase. Eur J Biochem 267:6102–6109CrossRefPubMedGoogle Scholar
  2. Arner ESJ, Holmgren A (2006) The thioredoxin system in cancer. Semin Cancer Biol 16:420–426CrossRefPubMedGoogle Scholar
  3. Holmgren A (2006) Selenite in cancer therapy. A commentary on “Selenite induces apoptosis in sarcomatoid malignant mesothelioma cells through oxidative stress”. Free Radiol Biol Med 41:862–865CrossRefGoogle Scholar
  4. Lillig CH, Holmgren A (2007) Thioredoxin and related molecules: from biology to health and disease. Antioxid Redox Signal 9:25–47CrossRefPubMedGoogle Scholar
  5. Rundlöf A-K, Arnér ESJ (2004) Regulation of the mammalian selenoprotein thioredoxin reductase 1 in relation to cellular phenotype, growth and signaling events. Antioxid Redox Signal 6:41–52CrossRefPubMedGoogle Scholar

See Also

  1. (2012) ASK1. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 296. doi:10.1007/978-3-642-16483-5_410Google Scholar
  2. (2012) Dithiol. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 1125. doi:10.1007/978-3-642-16483-5_1651Google Scholar
  3. (2012) P53. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 2747. doi:10.1007/978-3-642-16483-5_4331Google Scholar
  4. (2012) Selenocysteine. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 3359. doi:10.1007/978-3-642-16483-5_5223Google Scholar
  5. (2012) Selenoenzyme. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 3359. doi:10.1007/978-3-642-16483-5_5224Google Scholar
  6. (2012) Thioredoxin. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 3669. doi:10.1007/978-3-642-16483-5_5774Google Scholar
  7. (2012) Thioredoxin Reductase. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 3669. doi:10.1007/978-3-642-16483-5_5776Google Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2014

Authors and Affiliations

  1. 1.Department of Medical Biochemistry and BiophysicsKarolinska InstitutetStockholmSweden