ArticleThe Journal of physiology2006
Dependence of cross-bridge kinetics on myosin light chain isoforms in rabbit and rat skeletal muscle fibres.
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 17 papers.
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Who cites it
17 citing papers in PubMed, 30 citations in OpenAlex.
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- Developmental, physiologic and phylogenetic perspectives on the expression and regulation of myosin heavy chains in mammalian skeletal muscles.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2023Review
- Transcriptomic analysis the mechanisms of anti-osteoporosis of desert-living Cistanche herb in ovariectomized rats of postmenopausal osteoporosis.Functional & integrative genomics · 2023Article
- The Effects of a Transgelin-2 Agonist Administered at Different Times in a Mouse Model of Airway Hyperresponsiveness.Frontiers in pharmacology · 2022Article
- Single-molecule analysis reveals that regulatory light chains fine-tune skeletal myosin II function.The Journal of biological chemistry · 2020Article
- Increasing myosin light chain 3f (MLC3f) protects against a decline in contractile velocity.PloS one · 2019Article
- Comparative muscle proteomics/phosphoproteomics analysis provides new insight for the biosafety evaluation of fat-1 transgenic cattle.Transgenic research · 2017Article
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- Influence of chronic food deprivation on structure-function relationship of juvenile rat fast muscles.Journal of muscle research and cell motility · 2013Article
- Thermal acclimation in rainbow smelt, Osmerus mordax, leads to faster myotomal muscle contractile properties and improved swimming performance.Biology open · 2013Article
- Variation in the determinants of power of chemically skinned type I rat soleus muscle fibres.Journal of comparative physiology. A, Neuroethology, sensory, neural, and behavioral physiology · 2011Article
- Insights into the kinetics of Ca2+-regulated contraction and relaxation from myofibril studies.Pflugers Archiv : European journal of physiology · 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
- Human genome comparison of paretic and nonparetic vastus lateralis muscle in patients with hemiparetic stroke.Journal of rehabilitation research and development · 2008Article
- Cross-bridge kinetics of fast and slow fibres of cat jaw and limb muscles: correlations with myosin subunit composition.Journal of muscle research and cell motility · 2007Article
- Myosin heavy chain isoform composition and stretch activation kinetics in single fibres of Xenopus laevis iliofibularis muscle.The Journal of physiology · 2006Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cross-bridge kinetics underlying stretch-induced force transients was studied in fibres with different myosin light chain (MLC) isoforms from skeletal muscles of rabbit and rat. The force transients were induced by stepwise stretches (< 0.3% of fibre length) applied on maximally Ca2+-activated skinned fibres. Fast fibre types IIB, IID (or IIX) and IIA and the slow fibre type I containing the myosin heavy chain isoforms MHC-IIb, MHC-IId (or MHC-IIx), MHC-IIa and MHC-I, respectively, were investigated. The MLC isoform content varied within fibre types. Fast fibre types contained the fast regulatory MLC isoform MLC2f and different proportions of the fast alkali MLC isoforms MLC1f and MLC3f. Type I fibres contained the slow regulatory MLC isoform MLC2s and the slow alkali MLC isoform MLC1s. Slow MLC isoforms were also present in several type IIA fibres. The kinetics of force transients differed by a factor of about 30 between fibre types (order from fastest to slowest kinetics: IIB > IID > IIA >> I). The kinetics of the force transients was not dependent on the relative content of MLC1f and MLC3f. Type IIA fibres containing fast and slow MLC isoforms were about 1.2 times slower than type IIA fibres containing only fast MLC isoforms. We conclude that while the cross-bridge kinetics is mainly determined by the MHC isoforms present, it is affected by fast and slow MLC isoforms but not by the relative content of MLC1f and MLC3f. Thus, the physiological role of fast and slow MLC isoforms in type IIA fibres is a fine-tuning of the cross-bridge kinetics.
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