ArticlePflugers Archiv : European journal of physiology1991
Correlation between isoform composition of the 17 kDa myosin light chain and maximal shortening velocity in smooth muscle.
Article in Pflugers Archiv : European journal of physiology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 122 citations in OpenAlex.
- Pharmacological and mechanical properties of isolated pig coronary veins.Frontiers in physiology · 2023Article
- Influence of layer separation on the determination of stomach smooth muscle properties.Pflugers Archiv : European journal of physiology · 2021Article
- Signaling and metabolic properties of fast and slow smooth muscle types from mice.Pflugers Archiv : European journal of physiology · 2018Article
- The expression and functional activities of smooth muscle myosin and non-muscle myosin isoforms in rat prostate.Journal of cellular and molecular medicine · 2018Article
- Mechanisms of Vascular Smooth Muscle Contraction and the Basis for Pharmacologic Treatment of Smooth Muscle Disorders.Pharmacological reviews · 2016Review
- Smooth muscle contractile diversity in the control of regional circulations.American journal of physiology. Heart and circulatory physiology · 2014Review
- Transforming growth factor-beta (TGF- β) signaling in paravertebral muscles in juvenile and adolescent idiopathic scoliosis.BioMed research international · 2014Article
- Thick filament length and isoform composition determine self-organized contractile units in actomyosin bundles.Biophysical journal · 2013Article
- Smooth muscle myosin expression, isoform composition, and functional activities in rat corpus cavernosum altered by the streptozotocin-induced type 1 diabetes.American journal of physiology. Endocrinology and metabolism · 2012Article
- A multi-scale approach to airway hyperresponsiveness: from molecule to organ.Frontiers in physiology · 2012Article
- Article
- Vascular smooth muscle phenotypic diversity and function.Physiological genomics · 2010Review
- Affinity for MgADP and force of unbinding from actin of myosin purified from tonic and phasic smooth muscle.American journal of physiology. Cell physiology · 2008Article
- Smooth muscle myosin: regulation and properties.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2004Review
- Myosin regulatory light chain phosphorylation and strain modulate adenosine diphosphate release from smooth muscle Myosin.Biophysical journal · 2004Article
- The smooth muscle myosin seven amino acid heavy chain insert's kinetic role in the crossbridge cycle for mouse bladder.The Journal of physiology · 2003Article
- The kinetic properties of smooth muscle: how a little extra weight makes myosin faster.Journal of muscle research and cell motility · 2003Review
- Smooth, slow and smart muscle motors.Journal of muscle research and cell motility · 2003Review
- Decreased shortening velocity and altered myosin isoforms in guinea-pig hypertrophic intestinal smooth muscle.The Journal of physiology · 2002Article
- Effects of thyroxine on myosin isoform expression and mechanical properties in guinea-pig smooth muscle.The Journal of physiology · 2002Article
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2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The relation between the isoform distribution of the myosin 17 kDa essential light chain (LC17) and the mechanical properties of smooth muscle was investigated. The relative content of the basic (LC17b) and acidic (LC17a) isoelectric variants of the 17 kDa myosin light chain was determined in different mammalian smooth muscle tissues. The relative content of LC17b varied between muscles: rabbit rectococcygeus 0%, rabbit trachea 5%, guinea-pig taenia coli 21%, rat uterus 38%, rabbit aorta 56% and rat aorta 60%. The rate of tension development was determined following photolysis of caged-adenosine triphosphate (ATP) in skinned fibres activated with thiophosphorylation of the regulatory light chains. The half-time for force development was 0.67 s in rabbit rectococcygeus, 1.6 s in rabbit trachea, 1.13 s in guinea-pig taenia coli and 1.38 s in rabbit aorta. The maximal shortening velocity (Vmax) was determined with the isotonic quick release technique in skinned fibre preparations activated with thiophosphorylation. Vmax was 0.25 muscle lengths per second (ML/s) in rabbit rectococcygeus, 0.24 ML/s in rabbit trachea, 0.17 ML/s in guinea-pig taenia coli, 0.11 ML/s in rat uterus and 0.03 ML/s in rabbit aorta. The range of variation in Vmax between muscles was larger than in the half-time for force development. The inverse relationship between Vmax and the relative content of LC17b in the investigated muscles suggests that the type of essential myosin light chain influences the Vmax in smooth muscle.
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