ArticleJournal of muscle research and cell motility2018
Acidosis affects muscle contraction by slowing the rates myosin attaches to and detaches from actin.
Article in Journal of muscle research and cell motility, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.
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Who cites it
18 citing papers in PubMed, 1 synthesis or guideline pooled it, 38 citations in OpenAlex.
- Extracellular Buffering Supplements to Improve Exercise Capacity and Performance: A Comprehensive Systematic Review and Meta-analysis.Sports medicine (Auckland, N.Z.) · 2022Pooled it
- Trial
- The effect of multi-ingredient intra- versus extra-cellular buffering supplementation combined with branched-chain amino acids and creatine on exercise-induced ammonia blood concentration and aerobic capacity in taekwondo athletes.Journal of the International Society of Sports Nutrition · 2021Trial
- Phosphate and acidosis cause fibre type-specific changes to cellular and molecular contractile mechanics at 37°C in skeletal muscle from older adults.Experimental physiology · 2026Article
- Reduced Muscular Carnosine in Proximal Myotonic Myopathy-A PilotAnnals of clinical and translational neurology · 2026Article
- A primer on the methods of skeletal and cardiac muscle mechanics using permeabilized preparations.The Journal of general physiology · 2026Review
- Optimal neuromuscular performance requires motor neuron phosphagen kinases.The Journal of physiology · 2026Article
- Cross-bridge model-based quantification of muscle metabolite alterations leading to fatigue during all-out knee extension exercise.Frontiers in physiology · 2026Article
- A human skeletal muscle cross-bridge model to characterize the role of metabolite accumulation in muscle fatigue.Experimental physiology · 2025Article
- Theoretical treatment of tension transients in muscle following sudden changes in orthophosphate concentration: implications for energy transduction.Journal of muscle research and cell motility · 2025Article
- Skeletal Muscle Fatigue in Rats Is More Consistently Related to Increased Inorganic Phosphate Concentration Than Acidosis.Acta physiologica (Oxford, England) · 2025Article
- Lactic acidosis: implications for human exercise performance.European journal of applied physiology · 2025Review
- Characterizing the concentration and load dependence of phosphate binding to rabbit fast skeletal actomyosin.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Myosin-binding protein C regulates the sarcomere lattice and stabilizes the OFF states of myosin heads.Nature communications · 2024Article
- Myosin-binding protein C forms C-links and stabilizes OFF states of myosin.bioRxiv : the preprint server for biology · 2023Article
- The Poly-E motif in Titin's PEVK region undergoes pH dependent conformational changes.Biochemistry and biophysics reports · 2020Article
- Bioenergetic basis for the increased fatigability with ageing.The Journal of physiology · 2019Article
- Bioenergetic basis of skeletal muscle fatigue.Current opinion in physiology · 2019Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The loss of muscle force and power during fatigue from intense contractile activity is associated with, and likely caused by, elevated levels of phosphate ([Formula: see text]) and hydrogen ions (decreased pH). To understand how these deficits in muscle performance occur at the molecular level, we used direct measurements of mini-ensembles of myosin generating force in the laser trap assay at pH 7.4 and 6.5. The data are consistent with a mechanochemical model in which a decrease in pH reduces myosin's detachment from actin (by slowing ADP release), increases non-productive myosin binding (by detached myosin rebinding without a powerstroke), and reduces myosin's attachment to actin (by slowing the weak-to-strong binding transition). Additional support of this mechanism is found by incorporating it into a branched pathway model for the effects of [Formula: see text] on myosin's interaction with actin. Including pH-dependence in one additional parameter (acceleration of [Formula: see text]-induced detachment), the model reproduces experimental measurements at high and low pH, and variable [Formula: see text], from the single molecule to large ensemble levels. Furthermore, when scaled up, the model predicts force-velocity relationships that are consistent with muscle fiber measurements. The model suggests that reducing pH has two opposing effects, a decrease in attachment favoring a decrease in muscle force and a decrease in detachment favoring an increase in muscle force. Depending on experimental details, the addition of [Formula: see text] can strengthen one or the other effect, resulting in either synergistic or antagonistic effects. This detailed molecular description suggests a molecular basis for contractile failure during muscle fatigue.
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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.