ArticleThe Journal of physiology2006
The activity-induced reduction of myofibrillar Ca2+ sensitivity in mouse skeletal muscle is reversed by dithiothreitol.
Article in The Journal of physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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26 citing papers in PubMed, 67 citations in OpenAlex.
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- Incubation with sodium nitrite attenuates fatigue development in intact single mouse fibres at physiologicalThe Journal of physiology · 2019Article
- Mechanical isolation, and measurement of force and myoplasmic free [CaNature protocols · 2017Article
- Diaphragm abnormalities in heart failure and aging: mechanisms and integration of cardiovascular and respiratory pathophysiology.Heart failure reviews · 2017Review
- 0.9% saline is neither normal nor physiological.Journal of Zhejiang University. Science. B · 2016Review
- Beetroot juice supplementation reduces whole body oxygen consumption but does not improve indices of mitochondrial efficiency in human skeletal muscle.The Journal of physiology · 2016Article
- Potential molecular mechanisms underlying muscle fatigue mediated by reactive oxygen and nitrogen species.Frontiers in physiology · 2015Review
- The Measurement of Reversible Redox Dependent Post-translational Modifications and Their Regulation of Mitochondrial and Skeletal Muscle Function.Frontiers in physiology · 2015Review
- The excitation-contraction coupling mechanism in skeletal muscle.Biophysical reviews · 2014Review
- Role of the cytoskeleton in muscle transcriptional responses to altered use.Physiological genomics · 2013Article
- Accessibility of myofilament cysteines and effects on ATPase depend on the activation state during exposure to oxidants.PloS one · 2013Article
- Recent insights into muscle fatigue at the cross-bridge level.Frontiers in physiology · 2012Article
- Antioxidants and Skeletal Muscle Performance: "Common Knowledge" vs. Experimental Evidence.Frontiers in physiology · 2012Article
- Redox Regulation of Nonmuscle Myosin Heavy Chain during Integrin Engagement.Journal of signal transduction · 2012Article
- Chemotherapy-induced weakness and fatigue in skeletal muscle: the role of oxidative stress.Antioxidants & redox signaling · 2011Review
- Redox modulation of diaphragm contractility: Interaction between DHPR and RyR channels.Free radical biology & medicine · 2010Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The aim of this study was to further characterize the reduction of myofibrillar Ca2+ sensitivity in mouse muscle which has been observed after fatigue at 37 degrees C. Muscle bundles and single fibres were isolated from mouse flexor digitorum brevis muscle and studied at 37 degrees C. The single fibres were injected with the Ca2+ indicator indo-1. Muscle fatigue was produced by 0.4 s tetani repeated at 4 s intervals until force had fallen to less than 50% of initial. Excitation-contraction coupling was assessed by measuring the cytosolic calcium concentration ([Ca2+]i) during tetani, and the maximum Ca2+-activated force and the myofibrillar Ca2+ sensitivity were estimated from a series of tetani at different stimulation frequencies. Two main results were found. (i) The reduction of Ca2+ sensitivity only occurred when the muscle was intensely stimulated leading to fatigue. When the muscle was rested for 10 min at 37 degrees C there was no significant change in Ca2+ sensitivity. (ii) If the membrane-permeant thiol-specific reducing agent dithiothreitol (0.5 mm) was applied to the muscle for 2 min following the fatigue protocol, the reduction in Ca2+ sensitivity was reversed. Dithiothreitol had no effect on Ca2+ sensitivity in unfatigued preparations. There was no effect of fatigue or dithiothreitol on tetanic [Ca2+]i or on the maximum Ca2+-activated force. These results suggest that intense activity of skeletal muscle at 37 degrees C causes the production of reactive oxygen species which oxidize a target protein. We propose that critical sulphydryl groups on the target protein(s) are converted to disulphide bonds and this reaction reduces Ca2+ sensitivity.
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