Encyclopedia of Molecular Pharmacology

Living Edition
| Editors: Stefan Offermanns, Walter Rosenthal


  • Tilman GruneEmail author
  • Lars-Oliver Klotz
Living reference work entry
DOI: https://doi.org/10.1007/978-3-030-21573-6_5161-1


Definitions: Oxidants, Antioxidants, Free Radicals, ROS

Antioxidants are molecules characterized by function rather than common structural motifs. Their common feature is the capability of acting “anti”-oxidants in biological systems. Owing to the exposure of tissues to high concentrations of physically dissolved molecular oxygen as well as to nitrogen-containing biomolecules, the oxidants, usually implied as being opposed by antioxidants, are oxygen- and/or nitrogen-derived reactive species generated in biological systems (Fig. 1). There is, of course, a plethora of other biologically relevant reactive species and oxidants, including sulfur-centered radicals or chlorinated species. Referring to all of these using the frequently employed acronym ROS (“reactive oxygen species”), as we will in this entry, is, therefore, strictly speaking, incorrect. It has, however, the advantage that two inconsistencies are being avoided: if the compounds shown in Fig. 1were referred to...
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  1. Augustyniak E, Adam A, Wojdyla K, Rogowska-Wrzesinska A, Willetts R, Korkmaz A, Atalay M, Weber D, Grune T, Borsa C, Gradinaru D, Chand Bollineni R, Fedorova M, Griffiths HR (2015) Validation of protein carbonyl measurement: a multi-Centre study. Redox Biol 4:149–157CrossRefGoogle Scholar
  2. Bosio GN, Breitenbach T, Parisi J, Reigosa M, Blaikie FH, Pedersen BW, Silva EF, Martire DO, Ogilby PR (2013) Antioxidant beta-carotene does not quench singlet oxygen in mammalian cells. J Am Chem Soc 135:272–279CrossRefGoogle Scholar
  3. Breusing N, Grune T (2010) Biomarkers of protein oxidation from a chemical, biological and medical point of view. Exp Gerontol 45:733–737CrossRefGoogle Scholar
  4. Breusing N, Grune T, Andrisic L, Atalay M, Bartosz G, Biasi F, Borovic S, Bravo L, Casals I, Casillas R, Dinischiotu A, Drzewinska J, Faber H, Fauzi NM, Gajewska A, Gambini J, Gradinaru D, Kokkola T, Lojek A, Luczaj W, Margina D, Mascia C, Mateos R, Meinitzer A, Mitjavila MT, Mrakovcic L, Munteanu MC, Podborska M, Poli G, Sicinska P, Skrzydlewska E, Vina J, Wiswedel I, Zarkovic N, Zelzer S, Spickett CM (2010) An inter-laboratory validation of methods of lipid peroxidation measurement in UVA-treated human plasma samples. Free Radic Res 44:1203–1215CrossRefGoogle Scholar
  5. Frijhoff J, Winyard PG, Zarkovic N, Davies SS, Stocker R, Cheng D, Knight AR, Taylor EL, Oettrich J, Ruskovska T, Gasparovic AC, Cuadrado A, Weber D, Poulsen HE, Grune T, Schmidt HH, Ghezzi P (2015) Clinical relevance of biomarkers of oxidative stress. Antioxid Redox Signal 23:1144–1170CrossRefGoogle Scholar
  6. Gille A, Turkistani A, Tsitsipatis D, Hou X, Tauber S, Hamann I, Urban N, Erler K, Steinbrenner H, Klotz LO (2019) Nuclear trapping of inactive FOXO1 by the Nrf2 activator diethyl maleate. Redox Biol 20:19–27CrossRefGoogle Scholar
  7. Grune T, Berger MM (2007) Markers of oxidative stress in ICU clinical settings: present and future. Curr Opin Clin Nutr Metab Care 10:712–717CrossRefGoogle Scholar
  8. Grune T, Reinheckel T, Davies KJ (1997) Degradation of oxidized proteins in mammalian cells. FASEB J 11:526–534CrossRefGoogle Scholar
  9. Guerra B, Issinger OG (2019) Natural Compounds and Derivatives as Ser/Thr Protein Kinase Modulators and Inhibitors. Pharmaceuticals (Basel) 12:pii:E4CrossRefGoogle Scholar
  10. Jung T, Catalgol B, Grune T (2009) The proteasomal system. Mol Asp Med 30:191–296CrossRefGoogle Scholar
  11. Kehrer JP, Klotz LO (2015) Free radicals and related reactive species as mediators of tissue injury and disease: implications for health. Crit Rev Toxicol 45:765–798CrossRefGoogle Scholar
  12. Klotz LO (2015) On the biochemistry of antioxidants: current aspects. In: Roberts SM, Kehrer JP, Klotz LO (eds) Studies on experimental toxicology and pharmacology. Springer International Publishing, Cham, pp 383–396CrossRefGoogle Scholar
  13. Klotz LO, Steinbrenner H (2017) Cellular adaptation to xenobiotics: interplay between xenosensors, reactive oxygen species and FOXO transcription factors. Redox Biol 13:646–654CrossRefGoogle Scholar
  14. Klotz LO, Sanchez-Ramos C, Prieto-Arroyo I, Urbanek P, Steinbrenner H, Monsalve M (2015) Redox regulation of FoxO transcription factors. Redox Biol 6:51–72CrossRefGoogle Scholar
  15. Korovila I, Hugo M, Castro JP, Weber D, Höhn A, Grune T, Jung T (2017) Proteostasis, oxidative stress and aging. Redox Biol 13:550–567CrossRefGoogle Scholar
  16. Powers SK, Ji LL, Kavazis AN, Jackson MJ (2011) Reactive oxygen species: impact on skeletal muscle. Compr Physiol 1:941–969PubMedPubMedCentralGoogle Scholar
  17. Satoh T, Lipton S (2017) Recent advances in understanding NRF2 as a druggable target: development of pro-electrophilic and non-covalent NRF2 activators to overcome systemic side effects of electrophilic drugs like dimethyl fumarate. F1000Res 6:2138CrossRefGoogle Scholar
  18. Schulze-Topphoff U, Varrin-Doyer M, Pekarek K, Spencer CM, Shetty A, Sagan SA, Cree BA, Sobel RA, Wipke BT, Steinman L, Scannevin RH, Zamvil SS (2016) Dimethyl fumarate treatment induces adaptive and innate immune modulation independent of Nrf2. Proc Natl Acad Sci U S A 113:4777–4782CrossRefGoogle Scholar
  19. Siems WG, Brenke R, Sommerburg O, Grune T (1999) Improved antioxidative protection in winter swimmers. QJM 92:193–198CrossRefGoogle Scholar
  20. Sies H (1993) Strategies of antioxidant defense. Eur J Biochem 215:213–219CrossRefGoogle Scholar
  21. Sies H, Berndt C, Jones DP (2017) Oxidative stress. Annu Rev Biochem 86:715–748CrossRefGoogle Scholar
  22. Steinbrenner H, Speckmann B, Klotz LO (2016) Selenoproteins: Antioxidant selenoenzymes and beyond. Arch Biochem Biophys 595:113–119CrossRefGoogle Scholar
  23. Weber D, Milkovic L, Bennett SJ, Griffiths HR, Zarkovic N, Grune T (2013) Measurement of HNE-protein adducts in human plasma and serum by ELISA-comparison of two primary antibodies. Redox Biol 1:226–233CrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg New York 2020

Authors and Affiliations

  1. 1.Molecular ToxicologyGerman Institute of Human Nutrition Potsdam-RehbrueckeNuthetalGermany
  2. 2.Institute of Nutritional Sciences, Nutrigenomics SectionFriedrich-Schiller-Universität JenaJenaGermany