ArticlePflugers Archiv : European journal of physiology2008
Oxidation of multiple methionine residues impairs rapid sodium channel inactivation.
Article in Pflugers Archiv : European journal of physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 83 citations in OpenAlex.
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- Pyrethroid resistance in Aedes aegypti: genetic mechanisms worldwide, and recommendations for effective vector control.Parasites & vectors · 2025Review
- A Possible Role of Tetrodotoxin-Sensitive NaInternational journal of molecular sciences · 2024Article
- The Intricate Balance between Life and Death: ROS, Cathepsins, and Their Interplay in Cell Death and Autophagy.International journal of molecular sciences · 2024Review
- The inotropic and arrhythmogenic effects of acutely increased late IFrontiers in cardiovascular medicine · 2024Article
- Transient and Sustained Ganglion Cell Light Responses Are Differentially Modulated by Intrinsically Produced Reactive Oxygen Species Acting upon Specific Voltage-Gated NaThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2023Article
- When the Gates Swing Open Only: Arrhythmia Mutations That Target the Fast Inactivation Gate of NaCells · 2022Review
- The Potential of a Protein Model Synthesized Absent of Methionine.Molecules (Basel, Switzerland) · 2022Review
- Article
- Genomic and Non-Genomic Regulatory Mechanisms of the Cardiac Sodium Channel in Cardiac Arrhythmias.International journal of molecular sciences · 2022Review
- Attenuating persistent sodium current-induced atrial myopathy and fibrillation by preventing mitochondrial oxidative stress.JCI insight · 2021Article
- Profiling Dopamine-Induced Oxidized Proteoforms of β-synuclein by Top-Down Mass Spectrometry.Antioxidants (Basel, Switzerland) · 2021Article
- NGF-Induced Nav1.7 Upregulation Contributes to Chronic Post-surgical Pain by Activating SGK1-Dependent Nedd4-2 Phosphorylation.Molecular neurobiology · 2021Article
- Oxidation of methionine residues activates the high-threshold heat-sensitive ion channel TRPV2.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Oxygen-sensitive interneurons exhibit increased activity and GABA release during ROS scavenging in the cerebral cortex of the western painted turtle.Journal of neurophysiology · 2019Article
- Circadian redox rhythms in the regulation of neuronal excitability.Free radical biology & medicine · 2018Review
- Arrhythmogenic Mechanisms in Heart Failure: Linking β-Adrenergic Stimulation, Stretch, and Calcium.Frontiers in physiology · 2018Review
- Non-photonic sensing of membrane-delimited reactive species with a NaScientific reports · 2017Article
- Critical illness polyneuropathy in ICU patients is related to reduced motor nerve excitability caused by reduced sodium permeability.Intensive care medicine experimental · 2016Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Reactive oxygen species (ROS) readily oxidize the sulfur-containing amino acids cysteine and methionine (Met). The impact of Met oxidation on the fast inactivation of the skeletal muscle sodium channel Na(V)1.4 expressed in mammalian cells was studied by applying the Met-preferring oxidant chloramine-T or by irradiating the ROS-producing dye Lucifer Yellow in the patch pipettes. Both interventions dramatically slowed down inactivation of the sodium channels. Replacement of Met in the Ile-Phe-Met inactivation motif with Leu (M1305L) strongly attenuated the oxidizing effect on inactivation but did not eliminate it completely. Mutagenesis of Met1470 in the putative receptor of the inactivation lid also markedly diminished the oxidation sensitivity of the channel, while that of other conserved Met residues in intracellular linkers connecting the membrane-spanning segments (442, 1139, 1154, 1316, 1469) were of minor importance. The results of mutagenesis, assays of other Na(V) channel isoforms (Na(V)1.2, Na(V)1.5, Na(V)1.7), and the kinetics of the oxidation-induced removal of inactivation collectively indicate that multiple Met residues need to be oxidized to completely impair inactivation. This arrangement using multiple Met residues confers a finely graded oxidative modulation of Na(V) channels and allows organisms to adapt to a variety of oxidative stress conditions, such as ischemic reperfusion.
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