ArticleThe Journal of physiology2009
Redox modulation of global phosphatase activity and protein phosphorylation in intact skeletal muscle.
Article in The Journal of physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
48 citing papers in PubMed, 81 citations in OpenAlex.
- FGF2 supports NANOG expression via pyruvate dehydrogenase-dependent histone acetylation under low oxygen conditions.Frontiers in cell and developmental biology · 2025Article
- Renal FGF23 signaling depends on redox protein Memo1 and promotes orthovanadate-sensitive protein phosphotyrosyl phosphatase activity.Journal of cell communication and signaling · 2023Article
- Chronic Kidney Disease is Associated With Attenuated Plasma Metabolome Response to Oral Glucose Tolerance Testing.Journal of renal nutrition : the official journal of the Council on Renal Nutrition of the National Kidney Foundation · 2023Article
- Cardiovasomobility: an integrative understanding of how disuse impacts cardiovascular and skeletal muscle health.Journal of applied physiology (Bethesda, Md. : 1985) · 2022Review
- Article
- Exercise Cuts Both Ways with ROS in Remodifying Innate and Adaptive Responses: Rewiring the Redox Mechanism of the Immune System during Exercise.Antioxidants (Basel, Switzerland) · 2021Review
- Review
- Reactive oxygen species in exercise and insulin resistance: Working towards personalized antioxidant treatment.Redox biology · 2021Review
- Age-Related Alterations at Neuromuscular Junction: Role of Oxidative Stress and Epigenetic Modifications.Cells · 2021Review
- Exercise-Stimulated ROS Sensitive Signaling Pathways in Skeletal Muscle.Antioxidants (Basel, Switzerland) · 2021Review
- The Role of Hydrogen Peroxide and Peroxiredoxins throughout the Cell Cycle.Antioxidants (Basel, Switzerland) · 2020Review
- Global redox proteome and phosphoproteome analysis reveals redox switch in Akt.Nature communications · 2019Article
- Cardiac ischemia-reperfusion injury induces ROS-dependent loss of PKA regulatory subunit RIα.American journal of physiology. Heart and circulatory physiology · 2019Article
- Exercise-Induced Mitohormesis for the Maintenance of Skeletal Muscle and Healthspan Extension.Sports (Basel, Switzerland) · 2019Review
- The reduced activity of PP-1α under redox stress condition is a consequence of GSH-mediated transient disulfide formation.Scientific reports · 2018Article
- Oxidative Stress, Intrauterine Growth Restriction, and Developmental Programming of Type 2 Diabetes.Physiology (Bethesda, Md.) · 2018Review
- Chronic Kidney Disease-Induced Insulin Resistance: Current State of the Field.Current diabetes reports · 2018Review
- Redox homeostasis and age-related deficits in neuromuscular integrity and function.Journal of cachexia, sarcopenia and muscle · 2017Review
- Targeting the NO/superoxide ratio in adipose tissue: relevance to obesity and diabetes management.British journal of pharmacology · 2017Review
- Exercise and Glycemic Control: Focus on Redox Homeostasis and Redox-Sensitive Protein Signaling.Frontiers in endocrinology · 2017Review
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
Abstract
Skeletal muscles produce transient reactive oxygen species (ROS) in response to intense stimulation, disuse atrophy, heat stress, hypoxia, osmotic stress, stretch and cell receptor activation. The physiological significance is not well understood. Protein phosphatases (PPases) are known to be highly sensitive to oxidants and could contribute to many different signalling responses in muscle. We tested whether broad categories of PPases are inhibited by levels of acute oxidant exposure that do not result in loss of contractile function or gross oxidative stress. We also tested if this exposure results in elevated levels of global protein phosphorylation. Rat diaphragm muscles were treated with either 2,3-dimethoxy-1-naphthoquinone (DMNQ; 1, 10, 100 microm; a mitochondrial O(2)(.-)/H2O2 generator) or exogenous H2O2 (5, 50, 500 microm) for 30 min. Supernatants were assayed for serine/threonine PPase (Ser/Thr-PPase) or protein tyrosine PPase (PTP) activities. With the exception of 500 microm H2O2, no other oxidant exposures significantly elevated protein carbonyl formation, nor did they alter the magnitude of twitch force. DMNQ significantly decreased all categories of PPase activity at 10 and 100 microm and reduced PTP at 1 microm. Similar reductions in Ser/Thr-PPase activity were seen in response to 50 and 500 microm H2O2 and PTP at 500 microm H2O2. ROS treatments resulted a dose-dependent increase in the phosphorylation states of many proteins. The data are consistent with the concept that PPases, within intact skeletal muscles, are highly sensitive to acute changes in ROS activity and that localized ROS play a critical role in lowering the barriers for effective phosphorylation events to occur in muscle cells, thus increasing the probability for cell signalling responses to proceed.
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What OpenQuestion holds
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.