ArticleJournal of muscle research and cell motility2004
Myosin light chain isoform expression among single mammalian skeletal muscle fibers: species variations.
Article in Journal of muscle research and cell motility, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 45 citations in OpenAlex.
- The Acute, Short-, and Long-Term Effects of Endurance Exercise on Skeletal Muscle Transcriptome Profiles.International journal of molecular sciences · 2024Article
- Myosin essential light chain 1sa decelerates actin and thin filament gliding on β-myosin molecules.The Journal of general physiology · 2022Article
- Thick Filament Protein Network, Functions, and Disease Association.Comprehensive Physiology · 2018Review
- Nucleotide and protein sequences for dog masticatory tropomyosin identify a novel Tpm4 gene product.Journal of muscle research and cell motility · 2015Article
- Heterogeneous activation of a slow myosin gene in proliferating myoblasts and differentiated single myofibers.Developmental biology · 2015Article
- Myosin phosphorylation and force potentiation in skeletal muscle: evidence from animal models.Journal of muscle research and cell motility · 2013Review
- Complex tropomyosin and troponin T isoform expression patterns in orbital and global fibers of adult dog and rat extraocular muscles.Journal of muscle research and cell motility · 2013Article
- An Always Correlated gene expression landscape for ovine skeletal muscle, lessons learnt from comparison with an "equivalent" bovine landscape.BMC research notes · 2012Article
- Inferring the transcriptional landscape of bovine skeletal muscle by integrating co-expression networks.PloS one · 2009Article
- Masticatory (;superfast') myosin heavy chain and embryonic/atrial myosin light chain 1 in rodent jaw-closing muscles.The Journal of experimental biology · 2009Article
- Induction of muscle weakness by local inflammation: an experimental animal model.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2009Article
- Altered fast- and slow-twitch muscle fibre characteristics in female mice with a (S248F) knock-in mutation of the brain neuronal nicotinic acetylcholine receptor.Journal of muscle research and cell motility · 2009Article
- Influence of fast and slow alkali myosin light chain isoforms on the kinetics of stretch-induced force transients of fast-twitch type IIA fibres of rat.Pflugers Archiv : European journal of physiology · 2008Article
- Differential expression of sarcolipin protein during muscle development and cardiac pathophysiology.Journal of molecular and cellular cardiology · 2007Article
- Subcellular proteomics of mice gastrocnemius and soleus muscles.Analytical biochemistry · 2007Article
- Dependence of cross-bridge kinetics on myosin light chain isoforms in rabbit and rat skeletal muscle fibres.The Journal of physiology · 2006Article
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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
Extensive heterogeneity in myosin heavy chain and light chain (MLC) isoform expression in skeletal muscle has been well documented in several mammalian species. The initial objective of this study was to determine the extent of heterogeneity in myosin isoform expression among single fibers in limb muscles of dogs, a species for which relatively little has been reported. Fibers were isolated from muscles that have different functions with respect to limb extension and limb flexion and were analyzed on SDS gels, with respect to myosin isoform composition. The results of this part of the study indicate that there are at least four distinct fiber types in dog limb and diaphragm muscles, on the basis of MLC isoform expression: conventional fast (expressing fast-type isoforms of MLC1 (MLC1F) and MLC2 (MLC2F), plus MLC3), conventional slow (expressing slow-type MLC1 (MLC1S) and MLC2 (MLC2S)), hybrid (expressing MLC1S, MLC1F, MLC2S, MLC2F and MLC3) and a second slow fiber type, designated as S1F. S1F fibers express MLC1F, along with MLC1S and MLC2S and relatively low levels of MLC3. The fraction of slow fibers that are S1F fibers varies among dog limb muscles, being greater in limb extensors than flexors. Furthermore, the mean level of MLC1F in S1F fibers is greater in extensors than flexors (mean levels range from approximately 3% to 50% of total MLC1). The study was, therefore, extended to include six additional species, spanning a broad range in adult body size to more thoroughly characterize heterogeneity in MLC isoform expression among mammals. The results indicate that there are distinct patterns in MLC isoform expression among fast and slow fibers among different species. Specifically, large-size mammals have two distinct types of slow fibers, based upon MLC isoform composition (conventional and S1F fibers), whereas small mammals exhibit variations in MLC isoforms between different types of fast fibers, including a fast fiber type that expresses MLC1S (designated as F1S fibers). S1F fibers were absent in rodent muscles and F1S fibers were not found in large mammals. We conclude that extensive variation exists in MLC isoform expression in mammalian skeletal muscle fibers, yet there are distinct patterns among different species and among muscles within an individual species.
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