ArticleJournal of muscle research and cell motility2000
The maximal velocity of vascular smooth muscle shortening is independent of the expression of calponin.
Article in Journal of muscle research and cell motility, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Mechanoregulation and function of calponin and transgelin.Biophysics reviews · 2024Review
- Calponin 1 inhibits agonist-induced ERK activation and decreases calcium sensitization in vascular smooth muscle.Journal of cellular and molecular medicine · 2024Article
- Evolution and function of calponin and transgelin.Frontiers in cell and developmental biology · 2023Review
- Review
- Maximum shortening velocity of lymphatic muscle approaches that of striated muscle.American journal of physiology. Heart and circulatory physiology · 2013Article
- Expression of the fast twitch troponin complex, fTnT, fTnI and fTnC, in vascular smooth muscle.Cell motility and the cytoskeleton · 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
- Article
- Myosin heavy chain isoform expression regulates shortening velocity in smooth muscle: studies using an SMB KO mouse line.Journal of muscle research and cell motility · 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
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
In smooth muscle, the phosphorylation/dephosphorylation of the 20-kDa regulatory light chain of myosin (MLC20) is known to regulate actomyosin interaction and force. However, a thin filament based regulatory system for actomyosin interaction has been suggested to exist in parallel to MLC20 phosphorylation. Calponin is a thin filament associated protein that in vitro inhibits actomyosin interaction, and has been suggested to reduce maximal shortening velocity (vmax). Using antibodies to h1- and h2-calponin, we demonstrated that calponin was present in smooth muscle from Sprague Dawley (SD) rats, while calponin was not detectable in the smooth muscle from Wistar Kyoto (WKY) rats. vmax determined from the force vs. velocity relationship at maximal Ca2+ activation was not different for either the aorta or the portal vein of SD vs. WKY rats. These results suggest that physiological levels of calponin do not contribute to a thin filament-based secondary regulation to inhibit smooth muscle contraction.
Indexed as
Identifiers
What OpenQuestion holds
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.