Encyclopedia of Cancer

Living Edition
| Editors: Manfred Schwab

Reductases

Living reference work entry
DOI: https://doi.org/10.1007/978-3-642-27841-9_5007-2

Synonyms

Definition

Carbonyl reduction of aldehydes, ketones, and quinones to their corresponding hydroxy derivatives plays an important role in the phase I metabolism of many endogenous (biogenic aldehydes, steroids, prostaglandins, reactive lipid peroxidation products) and xenobiotic (pharmacologic drugs, carcinogens, toxicants) compounds (Xenobiotics).

Characteristics

From the pharmacologist’s point of view, carbonyl reduction is of significance in various inactivation processes of drugs bearing a carbonyl group. The carbinols formed may retain therapeutic potency, thus prolonging the pharmacodynamic effect of the parent drug, or, in some instances, a compound gains activity through carbonyl reduction. From the toxicologist’s point of view, carbonyl reduction plays an important role in the toxification of drugs such as daunorubicin and doxorubicin (Adriamycin), whereas numerous reports corroborate the concept...

Keywords

Aldose Reductase Glycyrrhetinic Acid Carbonyl Reductase Smokeless Tobacco User Carbonyl Reduction 
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. Hoffmann F, Maser E (2007) Carbonyl reductases and pluripotent hydroxysteroid dehydrogenases of the short-chain dehydrogenase/reductase superfamily. Drug Metab Rev 39:87–144CrossRefPubMedGoogle Scholar
  2. Jin Y, Penning TM (2007) Aldo-keto reductases and bioactivation/detoxication. Annu Rev Pharmacol Toxicol 47:263–292CrossRefPubMedGoogle Scholar
  3. Maser E (2004) Significance of reductases in the detoxification of the tobacco-specific carcinogen NNK. Trends Pharmacol Sci 25:235–237CrossRefPubMedGoogle Scholar
  4. Oppermann U (2007) Carbonyl reductases: the complex relationships of mammalian carbonyl- and quinone-reducing enzymes and their role in physiology. Annu Rev Pharmacol Toxicol 47:293–322CrossRefPubMedGoogle Scholar
  5. Plebuch M, Soldan M, Hungerer C, Koch L, Maser E (2007) Increased resistance of tumor cells to daunorubicin after transfection of cDNAs coding for anthracycline inactivating enzymes. Cancer Lett 255:49–56CrossRefPubMedGoogle Scholar
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Copyright information

© Springer-Verlag Berlin Heidelberg 2014

Authors and Affiliations

  1. 1.Institute of Toxicology and Pharmacology for Natural ScientistsUniversity Medical SchoolKielGermany