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By G. Winkelmann

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The discrepancy of responses among luminol and cytochrome c emphasizes the importance of the use of different methodologies to detect oxidative burst, in order to avoid erroneous conclusions. Indeed, if only cytochrome c was used the results would indicate, like in other reports Biometals (2010) 23:31–41 (DeCoursey et al. 2003), that zinc decreases O2•production in human neutrophils. The enzymatic complex NADPH oxidase is considered electrogenic because, when activated, transfers electrons from intracellular NADPH to molecular oxygen, producing O2•- in the extracellular or intraphagosomal space (Cross and Segal 2004).

Biol Trace Elem Res 74:97–105 DeCoursey TE, Morgan D, Cherny VV (2003) The voltage dependence of NADPH oxidase reveals why phagocytes need proton channels. Nature 422:531–534 Dekker LV, Leitges M, Altschuler G, Mistry N, McDermott A, Roes J, Segal AW (2000) Protein kinase C-beta contributes to NADPH oxidase activation in neutrophils. Biochem J 347:285–289 Denicola A, Radi R (2005) Peroxynitrite and drug-dependent toxicity. Toxicology 208:273–288 Essin K, Salanova B, Kettritz R, Sausbier M, Luft FC, Kraus D, Bohn E, Autenrieth IB, Peschel A, Ruth P, Gollasch M (2007) Large-conductance calcium-activated potassium channel activity is absent in human and mouse neutrophils and is not required for innate immunity.

Since the studied reactive species are formed downstream of NADPH oxidase activation, and contribute to luminol chemiluminescence, these results, together with those obtained in the cytochrome c assay system, at lower concentrations, allows the conclusion that zinc activates human neutrophils’ oxidative burst in vitro. Zinc had no effect on neutrophils previously stimulated with PMA, which suggests common activating mechanisms. In contrast, when fMLP was used, zinc tendentially increases the signal, suggesting different activating mechanisms.

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