ArticlePflugers Archiv : European journal of physiology1994
Effects of exogenously applied calponin on Ca(2+)-regulated force in skinned smooth muscle of the rabbit mesenteric artery.
Article in Pflugers Archiv : European journal of physiology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 51 citations in OpenAlex.
- A rapid degradation of calponin 2 is required for cytokinesis.American journal of physiology. Cell physiology · 2021Article
- Calponin control of cerebrovascular reactivity: therapeutic implications in brain trauma.Journal of cellular and molecular medicine · 2009Review
- Proteome alteration induced by hTERT transfection of human fibroblast cells.Proteome science · 2008Article
- Effects of h1-calponin ablation on the contractile properties of bladder versus vascular smooth muscle in mice lacking SM-B myosin.The Journal of physiology · 2006Article
- Calponin (CaP) as a latch-bridge protein--a new concept in regulation of contractility in smooth muscles.Journal of muscle research and cell motility · 2004Review
- Contractile properties and proteins of smooth muscles of a calponin knockout mouse.The Journal of physiology · 2000Article
- A role for serine-175 in modulating the molecular conformation of calponin.The Biochemical journal · 2000Article
- Actin and the smooth muscle regulatory proteins: a structural perspective.Journal of muscle research and cell motility · 2000Review
- Calponin interaction with alpha-actinin-actin: evidence for a structural role for calponin.Biophysical journal · 1999Article
- h1- and h2-calponins are not essential for norepinephrine- or sodium fluoride-induced contraction of rat aortic smooth muscle.Journal of muscle research and cell motility · 1998Article
- Clostridium difficile toxin B inhibits carbachol-induced force and myosin light chain phosphorylation in guinea-pig smooth muscle: role of Rho proteins.The Journal of physiology · 1998Article
- Slow cycling of unphosphorylated myosin is inhibited by calponin, thus keeping smooth muscle relaxed.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Inhibition by calponin of isometric force in demembranated vascular smooth muscle strips: the critical role of serine-175.The Biochemical journal · 1996Article
- Effect of KC399, a newly synthesized K+ channel opener, on acetylcholine-induced electrical and mechanical activities in rabbit tracheal smooth muscle.British journal of pharmacology · 1995Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To help elucidate the physiological role of calponin (a thin-filament-linked regulatory protein) in smooth muscle contraction, the effects of its exogenous application were investigated on actin-activated MgAT-Pase activity in crude actomyosin from chicken gizzard, and on contraction induced by Ca(2+)-dependent and -independent means in arterial smooth muscle strips skinned by saponin or beta-escin. Calponin concentration dependently inhibited actin-activated MgATPase activity with a proportional increase in its binding to actomyosin and also attenuated Ca(2+)-induced contractions, in the presence or absence of calmodulin, in skinned arterial strips. Calponin, when phosphorylated by protein kinase C, reduced both its ability to bind to actomyosin and its inhibitory action on actomyosin MgATPase. The phosphorylated calponin also had no effect on the maximum Ca(2+)-induced contraction in skinned smooth muscle, suggesting that these actions of calponin are not nonspecific. Calponin attenuated the Ca(2+)-independent contraction observed in myosin light chain thio-phosphorylated strips, or on application of trypsin-treated myosin light chain kinase. However, calponin had no effect on maintained rigor contraction. These results suggest that in vascular smooth muscle, calponin may play a physiological role in the inhibition of Ca(2+)-regulated force, possibly through a direct action on active actin-myosin interactions.
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