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Research Article Free access | 10.1172/JCI117162

Activation of H+ conductance in neutrophils requires assembly of components of the respiratory burst oxidase but not its redox function.

A Nanda, J T Curnutte, and S Grinstein

Division of Cell Biology, Hospital for Sick Children, Toronto, Canada.

Find articles by Nanda, A. in: PubMed | Google Scholar

Division of Cell Biology, Hospital for Sick Children, Toronto, Canada.

Find articles by Curnutte, J. in: PubMed | Google Scholar

Division of Cell Biology, Hospital for Sick Children, Toronto, Canada.

Find articles by Grinstein, S. in: PubMed | Google Scholar

Published April 1, 1994 - More info

Published in Volume 93, Issue 4 on April 1, 1994
J Clin Invest. 1994;93(4):1770–1775. https://doi.org/10.1172/JCI117162.
© 1994 The American Society for Clinical Investigation
Published April 1, 1994 - Version history
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Abstract

In phagocytes, superoxide generation by the NADPH oxidase is accompanied by metabolic acid production. Cytoplasmic acidification during this metabolic burst is prevented by a combination of H+ extrusion mechanisms, including a unique H+ conductance. NADPH oxidase is deficient in chronic granulomatous disease (CGD) patients. The burst of acid production is absent in CGD patients lacking the 47-kD (p47-phox) or the 91-kD (gp91-phox) subunits of the oxidase. Activation of the H+ conductance is also defective in these patients suggesting that (a) the oxidase itself undertakes H+ translocation or (b) oxidase assembly is required to stimulate a separate H+ conducting entity. To discern between these possibilities, three rare forms of CGD were studied. In neutrophils expressing nonfunctional cytochrome b, the conductance was activated to near-normal levels, implying that functional oxidase is not required to activate H+ extrusion. CGD cells expressing diminished amounts of cytochrome displayed H+ conductance approaching normal levels, suggesting that the oxidase itself does not translocate H+. Finally, the conductance was only partially inhibited in patients lacking the 67-kD subunit, indicating that this component is not essential for stimulation of H+ transport. We propose that normal assembly of the oxidase subunits is required for optimal activation of a closely associated but distinct H+ conducting entity.

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