ArticleJournal of muscle research and cell motility1998
Temperature sensitivity of force and shortening velocity in maximally activated skinned smooth muscle.
Article in Journal of muscle research and cell motility, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed.
- Signaling and metabolic properties of fast and slow smooth muscle types from mice.Pflugers Archiv : European journal of physiology · 2018Article
- What do we learn by studying the temperature effect on isometric tension and tension transients in mammalian striated muscle fibres?Journal of muscle research and cell motility · 2003Review
- Temperature effect on isometric tension is mediated by regulatory proteins tropomyosin and troponin in bovine myocardium.The Journal of physiology · 2002Article
- On the mechanisms whereby temperature affects excitation-contraction coupling in smooth muscle.The Journal of general physiology · 2002Article
- Kinetics of contraction in depolarized smooth muscle from guinea-pig taenia coli after photodestruction of nifedipine.The Journal of physiology · 1999Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have studied the temperature dependence of isometric force, rate of force development and maximal shortening velocity (Vmax) in skinned guinea-pig taenia coli smooth muscle. To eliminate the influence of temperature on activation mechanisms, maximally thiophosphorylated preparations were used. Isometric force in the range 2-35 degrees C was maximal at 22 degrees C with a decrease of 25% at 2 degrees C and 10% at 35 degrees C. Rate of tension development from rigor after photolytic release of ATP increased four-fold between 5 degrees C and 30 degrees C. Vmax increased with a Q10 of about 2 (1.6, range 5-15 degrees C, and 2.2, range 22-30 degrees C). The temperature dependence of the rate of tension development indicates rate-limitation by transitions into force-generating states or by the hydrolysis reaction. The temperature dependence of Vmax reflects effects of temperature on reactions (e.g. the ADP-release) associated with cross-bridge detachment. The small temperature dependence of steady-state force in smooth compared with skeletal muscle suggests differences in the cross-bridge reactions controlling the number of attached force-generating states in the two muscle types.
Indexed as
Identifiers
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.