ArticleThe Journal of experimental medicine1999
A novel H(+) conductance in eosinophils: unique characteristics and absence in chronic granulomatous disease.
Article in The Journal of experimental medicine, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
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Who cites it
67 citing papers in PubMed.
- Hv1 channel in immune cells and pharmacology.Pharmacological research · 2025Review
- The formation and function of the neutrophil phagosome.Immunological reviews · 2023Review
- Role of voltage-gated proton channel (Hv1) in cancer biology.Frontiers in pharmacology · 2023Review
- Intracellular pH regulation: characterization and functional investigation of HBMC molecular and cell biology · 2021Article
- Voltage-gated proton channels exist in the plasma membrane of human oocytes.Human reproduction (Oxford, England) · 2019Article
- Voltage and pH sensing by the voltage-gated proton channel, HJournal of the Royal Society, Interface · 2018Review
- Complement C5a Alters the Membrane Potential of Neutrophils during Hemorrhagic Shock.Mediators of inflammation · 2018Article
- Extracellular phosphates enhance activities of voltage-gated proton channels and production of reactive oxygen species in murine osteoclast-like cells.Pflugers Archiv : European journal of physiology · 2017Article
- The intimate and controversial relationship between voltage-gated proton channels and the phagocyte NADPH oxidase.Immunological reviews · 2016Review
- Insights into the structure and function of HV1 from a meta-analysis of mutation studies.The Journal of general physiology · 2016Review
- Proton channels and renal hypertensive injury: a key piece of the Dahl salt-sensitive rat puzzle?American journal of physiology. Regulatory, integrative and comparative physiology · 2016Review
- Effects of unsaturated fatty acids on the kinetics of voltage-gated proton channels heterologously expressed in cultured cells.The Journal of physiology · 2016Article
- Voltage-Gated Proton Channels as Novel Drug Targets: From NADPH Oxidase Regulation to Sperm Biology.Antioxidants & redox signaling · 2015Review
- The Voltage-Gated Proton Channel: A Riddle, Wrapped in a Mystery, inside an Enigma.Biochemistry · 2015Review
- Enhanced activation of an amino-terminally truncated isoform of the voltage-gated proton channel HVCN1 enriched in malignant B cells.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Expression of the voltage-sensing phosphatase gene in the chick embryonic tissues and in the adult cerebellum.Communicative & integrative biology · 2014Article
- Regulation of immune responses by proton channels.Immunology · 2014Review
- Philosophy of voltage-gated proton channels.Journal of the Royal Society, Interface · 2014Review
- Analysis of electrophysiological properties and responses of neutrophils.Methods in molecular biology (Clifton, N.J.) · 2014Article
- Voltage-gated proton channels: molecular biology, physiology, and pathophysiology of the H(V) family.Physiological reviews · 2013Review
7 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
7 authors.
Funding
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Abstract
Efficient mechanisms of H(+) ion extrusion are crucial for normal NADPH oxidase function. However, whether the NADPH oxidase-in analogy with mitochondrial cytochromes-has an inherent H(+) channel activity remains uncertain: electrophysiological studies did not find altered H(+) currents in cells from patients with chronic granulomatous disease (CGD), challenging earlier reports in intact cells. In this study, we describe the presence of two different types of H(+) currents in human eosinophils. The "classical" H(+) current had properties similar to previously described H(+) conductances and was present in CGD cells. In contrast, the "novel" type of H(+) current had not been described previously and displayed unique properties: (a) it was absent in cells from gp91- or p47-deficient CGD patients; (b) it was only observed under experimental conditions that allowed NADPH oxidase activation; (c) because of its low threshold of voltage activation, it allowed proton influx and cytosolic acidification; (d) it activated faster and deactivated with slower and distinct kinetics than the classical H(+) currents; and (e) it was approximately 20-fold more sensitive to Zn(2+) and was blocked by the histidine-reactive agent, diethylpyrocarbonate (DEPC). In summary, our results demonstrate that the NADPH oxidase or a closely associated protein provides a novel type of H(+) conductance during phagocyte activation. The unique properties of this conductance suggest that its physiological function is not restricted to H(+) extrusion and repolarization, but might include depolarization, pH-dependent signal termination, and determination of the phagosomal pH set point.
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