ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2008
Sarcoplasmic reticulum calcium uptake and speed of relaxation are depressed in nebulin-free skeletal muscle.
Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 62 citations in OpenAlex.
- Defective excitation-contraction coupling and mitochondrial respiration precede mitochondrial CaNature communications · 2023Article
- Peripheral and respiratory muscle impairment during murine acute lung injury.Physiological reports · 2022Article
- Is Upregulation of Sarcolipin Beneficial or Detrimental to Muscle Function?Frontiers in physiology · 2021Article
- Triggering typical nemaline myopathy with compound heterozygous nebulin mutations reveals myofilament structural changes as pathomechanism.Nature communications · 2020Article
- Nebulin: big protein with big responsibilities.Journal of muscle research and cell motility · 2020Review
- Expressing a Z-disk nebulin fragment in nebulin-deficient mouse muscle: effects on muscle structure and function.Skeletal muscle · 2020Article
- Nebulin and titin modulate cross-bridge cycling and length-dependent calcium sensitivity.The Journal of general physiology · 2019Article
- Reducing sarcolipin expression mitigates Duchenne muscular dystrophy and associated cardiomyopathy in mice.Nature communications · 2017Article
- Overview of the Muscle Cytoskeleton.Comprehensive Physiology · 2017Review
- Sarcolipin deletion exacerbates soleus muscle atrophy and weakness in phospholamban overexpressing mice.PloS one · 2017Article
- The effects of accumulated muscle fatigue on the mechanomyographic waveform: implications for injury prediction.European journal of applied physiology · 2016Article
- Diaphragm assessment in mice overexpressing phospholamban in slow-twitch type I muscle fibers.Brain and behavior · 2016Article
- Nebulin, a multi-functional giant.The Journal of experimental biology · 2016Review
- Phospholamban overexpression in mice causes a centronuclear myopathy-like phenotype.Disease models & mechanisms · 2015Article
- Effects of aging, exercise, and disease on force transfer in skeletal muscle.American journal of physiology. Endocrinology and metabolism · 2015Review
- The effects of sarcolipin over-expression in mouse skeletal muscle on metabolic activity.Archives of biochemistry and biophysics · 2015Article
- Pathophysiological concepts in the congenital myopathies: blurring the boundaries, sharpening the focus.Brain : a journal of neurology · 2015Review
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- The nebulin SH3 domain is dispensable for normal skeletal muscle structure but is required for effective active load bearing in mouse.Journal of cell science · 2013Article
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Authors and funding
9 authors at 5 institutions in 3 countries.
Funding
Abstract
Previous work suggested that altered Ca(2+) homeostasis might contribute to dysfunction of nebulin-free muscle, as gene expression analysis revealed that the sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA)-inhibitor sarcolipin (SLN) is up-regulated >70-fold in nebulin knockout mice, and here we tested this proposal. We investigated SLN protein expression in nebulin-free and wild-type skeletal muscle, as well as expression of other Ca(2+)-handling proteins. Ca(2+) uptake capacity was determined in isolated sarcoplasmic reticulum vesicles and in intact myofibers by measuring Ca(2+) transients. Muscle contractile performance was determined in skinned muscle activated with exogenous Ca(2+), as well as in electrically stimulated intact muscle. We found profound up-regulation of SLN protein in nebulin-free skeletal muscle, whereas expression of other Ca(2+)-handling proteins was not (calsequestrin and phospholamban) or was minimally (SERCA) affected. Speed of Ca(2+) uptake was >3-fold decreased in sarcoplasmic reticulum vesicles isolated from nebulin-free muscle as well as in nebulin-free intact myofibers. Ca(2+)-activated stress in skinned muscle and stress produced by intact nebulin-free muscle were reduced to a similar extent compared with wild type. Half-relaxation time was significantly longer in nebulin-free compared with wild-type muscle. Thus, the present study demonstrates for the first time that nebulin might also be involved in physiological Ca(2+) handling of the SR-myofibrillar system.
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