ArticleJournal of comparative physiology. B, Biochemical, systemic, and environmental physiology2009
Twitchin of mollusc smooth muscles can induce "catch"-like properties in human skeletal muscle: support for the assumption that the "catch" state involves twitchin linkages between myofilaments.
Article in Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- The unique biology of catch muscles: insights into structure, function, and robotics innovations.Frontiers in bioengineering and biotechnology · 2025Review
- Passive force enhancement in striated muscle.Journal of applied physiology (Bethesda, Md. : 1985) · 2019Review
- Why are muscles strong, and why do they require little energy in eccentric action?Journal of sport and health science · 2018Article
- Cytoskeletal protein kinases: titin and its relations in mechanosensing.Pflugers Archiv : European journal of physiology · 2011Review
- The highly efficient holding function of the mollusc 'catch' muscle is not based on decelerated myosin head cross-bridge cycles.Proceedings. Biological sciences · 2010Article
- Mechanism of catch force: tethering of thick and thin filaments by twitchin.Journal of biomedicine & biotechnology · 2010Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Molluscan catch muscles can maintain tension with low or even no energy utilization, and therefore, they represent ideal models for studying energy-saving holding states. For many decades it was assumed that catch is due to a simple slowing of the force-generating myosin head cross-bridge cycles. However, recently evidences increased suggesting that catch is rather caused by passive structures linking the myofilaments in a phosphorylation-dependent manner. One possible linkage structure is the titin-like thick filament protein twitchin, which could form bridges to the thin filaments. Twitchin is known to regulate the catch state depending on its phosphorylation state. Here, we found that twitchin induces a catch-like stiffness in skinned human skeletal muscle fibres, when these fibres are exposed to this protein. Subsequent phosphorylation of twitchin reduces the stiffness. These findings support the assumption that catch of molluscan smooth muscle involves twitchin linkages between thick and thin filaments.
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Registered trials
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