Advertisement

Ascorbate: The Most Effective Antioxidant in Human Blood Plasma

  • Balz Frei
  • Roland Stocker
  • Laura England
  • Bruce N. Ames
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 264)

Abstract

Living is like getting irradiated. This is because we are constantly exposed to oxidants such as Superoxide radicals, hydrogen peroxide, hydroxyl radicals, and singlet oxygen. These reactive oxygen species are generated during normal oxidative metabolism, for example by spontaneous autoxidation of electron transport carriers in mitochondria, or as a result of the action of oxidases.1 One of these oxidases, the NADPH oxidase of polymorphonuclear leukocytes (PMNs) (primarily neutrophils and eosinophils), is pivotal to the body’s defense against pathogenic microorganisms. The immediate product of the stimulus-induced activation of the NADPH oxidase of PMNs is Superoxide anion, whereas subsequent reactions form further oxidants including hydrogen peroxide, hypochlorite, and chloramines.2,3 These oxidants not only kill the invading microorganisms, but also can cause considerable oxidative damage to the host himself. Other sources of oxidants to which we are constantly exposed include our diet, polluted air (particularly from smoking), natural radio active gases,e.g. radon leaching from soils, and some drugs.4,5

Keywords

Lipid Peroxidation NADPH Oxidase Sulfhydryl Group Lipid Hydroperoxide Peroxyl Radical 
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.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    B. Chance, H. Sies, and A. Boveris, Hydroperoxide metabolism in mammalian organs, Physiol. Rev. 59:527 (1979).PubMedGoogle Scholar
  2. 2.
    S. J. Klebanoff, Phagocytic cells: products of oxygen metabolism, in: “Inflammation: Basic Principles and Clinical Correlates,” pp. 391, J. I. Gallin, I. M. Goldstein, and R. Snyderman, eds., Raven Press, New York, (1988).Google Scholar
  3. 3.
    S. J. Weiss, M. B. Lampert, and S. T. Test, Long-lived oxidants generated by human neutrophils: characterization and bioactivity, Science 222:625 (1983).PubMedCrossRefGoogle Scholar
  4. 4.
    B. N. Ames, Dietary carcinogens and anticarcinogens, Science 221:1256 (1983).PubMedCrossRefGoogle Scholar
  5. 5.
    B. N. Ames, R. Magaw, and L. S. Gold, Ranking possible carcinogenic hazards, Science 236:271 (1987).PubMedCrossRefGoogle Scholar
  6. 6.
    H. Esterbauer and K. H. Cheeseman, eds., “Lipid Peroxidation: Part II. Pathological Implications,” Chem. Phys. Lipids 45, Nos. 2–4 (1987).Google Scholar
  7. 7.
    B. Halliwell, Albumin-an important extracellular antioxidant? Biochem. Pharmacol. 37:569 (1988).Google Scholar
  8. 8.
    O. I. Aruoma and B. Halliwell, Superoxide-dependent and ascorbate-dependent formation of hydroxyl radicals from hydrogen peroxide in the presence of iron. Are lactoferrin and transferrin promoters of hydroxyl-radical generation? Biochem. J. 241:273 (1987).PubMedGoogle Scholar
  9. 9.
    J. M. C. Gutteridge, Antioxidant properties of caeruloplasmin towards iron-and copper-dependent oxygen radical formation, FEBS Lett. 157:37 (1983).PubMedCrossRefGoogle Scholar
  10. 10.
    B. Frei, R. Stocker, and B. N. Ames, Antioxidant defenses and lipid peroxidation in human blood plasma, Proc. Natl. Äcad. Sci. USA 85:9748 (1988).PubMedCrossRefGoogle Scholar
  11. 11.
    Y. Yamamoto, M. H. Brodsky, J. C. Baker, and B. N. Ames, Detection and characterization of lipid hydroperoxides at picomole levels by high-performance liquid chromatography, Anal. Biochem. 160:7 (1987).PubMedCrossRefGoogle Scholar
  12. 12.
    B. Frei, Y. Yamamoto, D. Niclas, and B. N. Ames, Evaluation of an isoluminol chemiluminescence assay for the detection of hydroperoxides in human blood plasma, Anal. Biochem. 175:120 (1988).PubMedCrossRefGoogle Scholar
  13. 13.
    R. Stocker, A. N. Glazer, and B. N. Ames, Antioxidant activity of albumin-bound bilirubin, Proc. Natl. Acad. Sci. USA 84:5918 (1987).PubMedCrossRefGoogle Scholar
  14. 14.
    E. Heimerhorst and G. B. Stokes, Microcentrifuge desalting: a rapid, quantitative method for desalting small amounts of protein, Anal. Biochem. 104:130 (1980).Google Scholar
  15. 15.
    B. Halliwell, M. Wasil, and M. Grootveld, Biologically significant scavenging of the myeloperoxidase-derived oxidant hypochlorous acid by ascorbic acid. Implications for antioxidant protection in the inflamed rheumatoid joint, FEBS Lett. 213:15 (1987).PubMedCrossRefGoogle Scholar
  16. 16.
    M. Grootveld, B. Halliwell, and C. P. Moorhouse, Action of uric acid, allopurinol and oxypurinol on the myeloperoxidase-derived oxidant hypochlorous acid, Free Rad. Res. Comms. 4:69 (1987).CrossRefGoogle Scholar
  17. 17.
    R. Stocker, A. Lai, E. Peterhans, and B. N. Ames, Antioxidant properties of bilirubin and biliverdin, in: “Medical, Biochemical and Chemical Aspects of Free Radicals,” E. Niki and T. Yoshikawa, eds., Elsevier, Amsterdam, in press.Google Scholar
  18. 18.
    C. Lentner, “Geigy Scientific Tables,” p. 122, Ciba-Geigy Limited, Basle (1984)Google Scholar
  19. 19.
    G. W. Burton, A. Joyce, and K. U. Ingold, First proof that vitamin E is the major lipid-soluble, chain-breaking antioxidant in human blood plasma, Lancet 2:327 (1982).Google Scholar

Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • Balz Frei
    • 1
  • Roland Stocker
    • 1
  • Laura England
    • 1
  • Bruce N. Ames
    • 1
  1. 1.Department of BiochemistryUniversity of CaliforniaBerkeleyUSA

Personalised recommendations