ArticleJournal of muscle research and cell motility1997
Stretch activation and isoforms of myosin heavy chain and troponin-T of rat skeletal muscle fibres.
Article in Journal of muscle research and cell motility, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 34 citations in OpenAlex.
- Stretch activation combats force loss from fatigue in fast-contracting mouse skeletal muscle fibers.The Journal of general physiology · 2025Article
- 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 embryonic myosin isoform enables stretch activation and cyclical power in Drosophila jump muscle.Biophysical journal · 2013Article
- Myosin heavy chain composition of the human genioglossus muscle.Journal of speech, language, and hearing research : JSLHR · 2012Article
- 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
- Single skeletal muscle fiber behavior after a quick stretch in young and older men: a possible explanation of the relative preservation of eccentric force in old age.Pflugers Archiv : European journal of physiology · 2006Article
- Interaction between signalling pathways involved in skeletal muscle responses to endurance exercise.Pflugers Archiv : European journal of physiology · 2006Review
- The effect of resection on satellite cell activity in rabbit extraocular muscle.Investigative ophthalmology & visual science · 2006Article
- Functional properties of skinned rabbit skeletal and cardiac muscle preparations containing alpha-cardiac myosin heavy chain.Pflugers Archiv : European journal of physiology · 2004Article
- Functional differences in type-I fibres from two slow skeletal muscles of rabbit.Pflugers Archiv : European journal of physiology · 2003Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recent studies on single mammalian skeletal muscle fibres revealed a correlation between the kinetics of stretch-induced delayed force increase (stretch activation) and the isoforms of the myosin heavy chain. This observation suggests a causal relation between stretch activation and myosin heavy chain. However, the assumption is weakened by the fact that isoforms of other myofibrillar proteins tend to be coexpressed with myosin heavy chain isoforms. The relation between the isoforms of the tropomyosin-binding troponin subunit and myosin heavy chain is unknown. For a variety of reasons, tropomyosin-binding troponin subunit is a possible candidate for being involved in stretch activation. Therefore, we measured stretch activation of single, maximally Ca(2+)-activated skinned rat skeletal muscle fibres and characterized them by their myosin heavy chain composition, as well as by the isoform species of tropomyosin-binding troponin subunit. Four myosin heavy chain isoforms (I, IIa, IId or IIx and IIb) and six tropomyosin-binding troponin subunit isoforms (TnT1s, TnT2s, TnT1f, TnT2f, TnT3f, TnT4f) were distinguished. The following preferential coexpression patterns of the myosin heavy chain and tropomyosin-binding troponin subunit isoforms were observed: MHCI-TnT1s, MHCIIa-TnT3f, MHCIId-TnT1f, and MHCIIb-TnT4f. Stretch activation kinetics was found to be correlated with the myosin heavy chain isoform complement also in fibres not displaying one of the preferential MHC-TnTf isoform coexpression patterns. This corroborates the assumption of a causal relation between myosin heavy chain and stretch activation.
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