ArticleJournal of muscle research and cell motility1990
The action of brevin, an F-actin severing protein, on the mechanical properties and ATPase activity of skinned smooth muscle.
Article in Journal of muscle research and cell motility, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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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
8 citing papers in PubMed, 14 citations in OpenAlex.
- Molecular characterization of severin from Clonorchis sinensis excretory/secretory products and its potential anti-apoptotic role in hepatocarcinoma PLC cells.PLoS neglected tropical diseases · 2013Article
- F-actin stabilization increases tension cost during contraction of permeabilized airway smooth muscle in dogs.The Journal of physiology · 1999Article
- Hypoxia and smooth muscle function: key regulatory events during metabolic stress.The Journal of physiology · 1998Review
- Involvement of the cytoskeleton in calcium-dependent stress relaxation of rat aortic smooth muscle.Journal of muscle research and cell motility · 1998Article
- Distribution of gelsolin in mouse ovary.Cell and tissue research · 1994Article
- X-ray diffraction study on mammalian visceral smooth muscles in resting and activated states.Journal of muscle research and cell motility · 1993Article
- Relaxant effect of phalloidin on Triton-skinned microvascular and other smooth muscle preparations.Journal of muscle research and cell motility · 1992Article
- Complex stiffness of smooth muscle cytoplasm in the presence of Ca-activated brevin.Journal of muscle research and cell motility · 1991Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Brevin is a protein which regulates the actin gel-sol transformation: it severs F-actin filaments into shorter ones. This action is Ca-dependent and is prevented by tropomyosin. We tested the effect of brevin on isometric contractions of skinned smooth muscle (taenia coli) and noted a dramatic loss of tension that possibly reflects some F-actin fragmentation. This effect is tentatively attributed to a partial loss of tropomyosin in the skinning procedure. We also studied the effect of brevin on unloaded shortenings of skinned preparations: thin bundles and enzymatically dissociated cells. We observed a marked increase of the velocity of shortening in the presence of brevin. This effect cannot be attributed to an increased ATPase activity as the latter is slightly reduced in the presence of brevin. We interpret this result as reflecting a decrease in internal resistance to movement, possibly by solation of an actin-filamin domain.
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