ArticleThe Journal of physiology2003
Temperature dependence of NADPH oxidase in human eosinophils.
Article in The Journal of physiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 49 citations in OpenAlex.
- Thermostable enzyme isoforms, continuously producing monocomponent superoxide radicals, from human postoperative serous fluids: isolation and properties.BMC cancer · 2025Article
- Temperature Dependent Activity of the Voltage-Gated Proton Channel.Advances in experimental medicine and biology · 2024Review
- Voltage-Gated Proton Channels in the Tree of Life.Biomolecules · 2023Review
- Reactive Oxygen Species in the Reproductive System: Sources and Physiological Roles.Advances in experimental medicine and biology · 2022Article
- VDAC Gating Thermodynamics, but Not Gating Kinetics, Are Virtually Temperature Independent.Biophysical journal · 2020Article
- Mechanistic computational modeling of the kinetics and regulation of NADPH oxidase 2 assembly and activation facilitating superoxide production.Free radical research · 2020Article
- A thermodynamically-constrained mathematical model for the kinetics and regulation of NADPH oxidase 2 complex-mediated electron transfer and superoxide production.Free radical biology & medicine · 2019Article
- Korean Red Ginseng (Journal of ginseng research · 2019Article
- Molecular and functional characterization of the voltage-gated proton channel in zebrafish neutrophils.Physiological reports · 2017Article
- The intimate and controversial relationship between voltage-gated proton channels and the phagocyte NADPH oxidase.Immunological reviews · 2016Review
- 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
- Insight into oxidative stress in varicocele-associated male infertility: part 1.Nature reviews. Urology · 2012Review
- Strong glucose dependence of electron current in human monocytes.American journal of physiology. Cell physiology · 2012Article
- Identification of Thr29 as a critical phosphorylation site that activates the human proton channel Hvcn1 in leukocytes.The Journal of biological chemistry · 2010Article
- Voltage-gated proton channels find their dream job managing the respiratory burst in phagocytes.Physiology (Bethesda, Md.) · 2010Review
- Temperature dependence of proton permeation through a voltage-gated proton channel.The Journal of general physiology · 2009Article
- Charge compensation for NADPH oxidase activity in microglia in rat brain slices does not involve a proton current.The European journal of neuroscience · 2008Article
- A pH-stabilizing role of voltage-gated proton channels in IgE-mediated activation of human basophils.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Role of Nox2 in elimination of microorganisms.Seminars in immunopathology · 2008Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The phagocyte NADPH oxidase helps kill pathogens by producing superoxide anion, O2-. This enzyme is electrogenic because it translocates electrons across the membrane, generating an electron current, Ie. Using the permeabilized patch voltage-clamp technique, we studied the temperature dependence of Ie in human eosinophils stimulated by phorbol myristate acetate (PMA) from room temperature to >37 degrees C. For comparison, NADPH oxidase activity was assessed by cytochrome c reduction. The intrinsic temperature dependence of the assembled, functioning NADPH oxidase complex measured during rapid temperature increases to 37 degrees C was surprisingly weak: the Arrhenius activation energy Ea was only 14 kcal mol(-1) (Q10, 2.2). In contrast, steady-state NADPH oxidase activity was strongly temperature dependent at 20-30 degrees C, with Ea 25.1 kcal mol(-1) (Q10, 4.2). The maximum Ie measured at 34 degrees C was -30.5 pA. Above 30 degrees C, the temperature dependence of both Ie and O2- production was less pronounced. Above 37 degrees C, Ie was inhibited reversibly. After rapid temperature increases, a secondary increase in Ie ensued, suggesting that high temperature promotes assembly of additional NADPH oxidase complexes. Evidently, about twice as many NADPH oxidase complexes are active near 37 degrees C than at 20 degrees C. Thus, the higher Q10 of steady-state Ie reflects both increased activity of each NADPH oxidase complex and preferential assembly of NADPH oxidase complexes at high temperature. In summary, NADPH oxidase activity in intact human eosinophils is maximal precisely at 37 degrees C.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.