ArticleThe Journal of general physiology2003
Interactions between electron and proton currents in excised patches from human eosinophils.
Article in The Journal of general physiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 27 citations in OpenAlex.
- Temperature Dependent Activity of the Voltage-Gated Proton Channel.Advances in experimental medicine and biology · 2024Review
- Regulation of Neutrophil Functions by Hv1/VSOP Voltage-Gated Proton Channels.International journal of molecular sciences · 2021Review
- Molecular mechanisms of coupling to voltage sensors in voltage-evoked cellular signals.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2019Review
- Complement C5a Alters the Membrane Potential of Neutrophils during Hemorrhagic Shock.Mediators of inflammation · 2018Article
- Voltage-Gated Proton Channels as Novel Drug Targets: From NADPH Oxidase Regulation to Sperm Biology.Antioxidants & redox signaling · 2015Review
- Analysis of electrophysiological properties and responses of neutrophils.Methods in molecular biology (Clifton, N.J.) · 2014Article
- Physiological roles of voltage-gated proton channels in leukocytes.The Journal of physiology · 2010Review
- Molecular and functional characterization of Hv1 proton channel in human granulocytes.PloS one · 2010Article
- Neutrophil functions and autoimmune arthritis in the absence of p190RhoGAP: generation and analysis of a novel null mutation in mice.Journal of immunology (Baltimore, Md. : 1950) · 2010Article
- Voltage-gated proton channels find their dream job managing the respiratory burst in phagocytes.Physiology (Bethesda, Md.) · 2010Review
- VSOP/Hv1 proton channels sustain calcium entry, neutrophil migration, and superoxide production by limiting cell depolarization and acidification.The Journal of experimental medicine · 2010Article
- Voltage-gated proton channels: what's next?The Journal of physiology · 2008Review
- Sustained activation of proton channels and NADPH oxidase in human eosinophils and murine granulocytes requires PKC but not cPLA2 alpha activity.The Journal of physiology · 2007Article
- Role of nucleotides and phosphoinositides in the stability of electron and proton currents associated with the phagocytic NADPH oxidase.The Biochemical journal · 2006Article
- Consequences of the electrogenic function of the phagocytic NADPH oxidase.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2005Review
- Electron and proton transport by NADPH oxidases.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2005Review
- The pH dependence of NADPH oxidase in human eosinophils.The Journal of physiology · 2005Article
- Voltage- and NADPH-dependence of electron currents generated by the phagocytic NADPH oxidase.The Biochemical journal · 2005Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The NADPH-oxidase is a plasma membrane enzyme complex that enables phagocytes to generate superoxide in order to kill invading pathogens, a critical step in the host defense against infections. The oxidase transfers electrons from cytosolic NADPH to extracellular oxygen, a process that requires concomitant H+ extrusion through depolarization-activated H+ channels. Whether H+ fluxes are mediated by the oxidase itself is controversial, but there is a general agreement that the oxidase and H+ channel are intimately connected. Oxidase activation evokes profound changes in whole-cell H+ current (IH), causing an approximately -40-mV shift in the activation threshold that leads to the appearance of inward IH. To further explore the relationship between the oxidase and proton channel, we performed voltage-clamp experiments on inside-out patches from both resting and phorbol-12-myristate-13-acetate (PMA)-activated human eosinophils. Proton currents from resting cells displayed slow voltage-dependent activation, long-term stability, and were blocked by micromolar internal [Zn2+]. IH from PMA-treated cells activated faster and at lower voltages, enabling sustained H+ influx, but ran down within minutes, regaining the current properties of nonactivated cells. Bath application of NADPH to patches excised from PMA-treated cells evoked electron currents (Ie), which also ran down within minutes and were blocked by diphenylene iodonium (DPI). Run-down of both IH and Ie was delayed, and sometimes prevented, by cytosolic ATP and GTP-gamma-S. A good correlation was observed between the amplitude of Ie and both inward and outward IH when a stable driving force for e- was imposed. Combined application of NADPH and DPI reduced the inward IH amplitude, even in the absence of concomitant oxidase activity. The strict correlation between Ie and IH amplitudes and the sensitivity of IH to oxidase-specific agents suggest that the proton channel is either part of the oxidase complex or linked by a membrane-limited mediator.
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