Superoxide Dismutases and the Oxidative Burst in Human Blood Polymorphonuclear Leukocytes

  • Martine Torres
  • Jacques Hakim
  • R. E. Basford
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 141)


Both cyanide (CN)-sensitive and CN-resistant superoxide dismutases (SOD) have been identified in human polymorphonuclear leukocytes (PMN), and located in the cytosol and granules of these cells 1–4. These enzymes catalyse the dismutation of superoxide anion (\( {{O}^{-}}_{{\dot{2}}} \)) to hydrogen peroxide (H2O2), and are thus thought to be protective in PMN against the highly reactive \( {{O}^{-}}_{{\dot{2}}} \), as they are in other tissues and cells of aerobic organisms2,4–6 However, the functional activity of PMN, i.e. their microbial killing activity, depends largely on the ability of PMN to generate \( {{O}^{-}}_{{\dot{2}}} \) during their stimulated oxidative burst7(OB).Moreover, the OB of the PMN not only kills the ingested bacteria, but is also a suicidal event for the PMN, suggesting that the SOD might lose their activity during the OB. On the other hand it is well known that SOD activity inhibits O2-uptake, NAD(P)H oxidation, and \( {{O}^{-}}_{{\dot{2}}} \) formation by isolated subcellular fractions from PMN8–10.


Oxidative Burst7 Subcellular Fraction Chronic Granulomatous Disease NADH Oxidation NADPH Oxidation 


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Copyright information

© Plenum Press, New York 1982

Authors and Affiliations

  • Martine Torres
    • 1
  • Jacques Hakim
    • 1
  • R. E. Basford
  1. 1.Laboratoire d’Immunologie et d’Hématologie — CHU Xavier BichatUniversité Paris VIIParis Cedex 18France

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