Evidence map›Paper›PMID 8645154›Full record

ArticleThe Biochemical journal1996

Modulation of gelsolin-induced actin-filament severing by caldesmon and tropomyosin and the effect of these proteins on the actin activation of myosin Mg(2+)-ATPase activity.

R Dabrowska, H Hinssen, B Gałazkiewicz, E Nowak

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.7field-weighted citation impact, top 33% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. New insights into the regulation of the actin cytoskeleton by tropomyosin.International review of cell and molecular biology · 2010
    Review
  6. Smooth muscle signalling pathways in health and disease.Journal of cellular and molecular medicine · 2008
    Review
  7. Review
  8. Caldesmon and the regulation of cytoskeletal functions.Advances in experimental medicine and biology · 2008
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 3 institutions in 3 countries.

R DabrowskaDepartment of Muscle Biochemistry, Nencki Institute of Experimental Biology, Warsaw, Poland.
H Hinssen
B Gałazkiewicz
E Nowak
Instytut Biologii Doświadczalnej im. Marcelego Nenckiego · PLAustrian Academy of Sciences · ATBielefeld University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have investigated the cumulative effects of three smooth-muscle actin-binding proteins, gelsolin, caldesmon and tropomyosin, on actin activation of myosin Mg(2+)-ATPase activity under low-ionic-strength conditions. A combination of tropomyosin (at a stoicheiometric ratio to actin) and gelsolin (at a molar ratio to actin of up to 1:100) showed essentially additive stimulatory effects that were counteracted by caldesmon. Suppression of the gelsolin-induced activation of the ATPase by caldesmon was higher in the presence of tropomyosin although it was not complete even at stoicheiometric amounts of both proteins to actin. Since activation of actin-activated ATPase activity of myosin by gelsolin is related to its severing action, it is concluded that caldesmon and tropomyosin cannot fully protect actin filaments against the severing activity of gelsolin. Direct analysis of the actin-severing activity of gelsolin by a fluorimetric assay using pyrene-labelled actin confirmed this conclusion. Tropomyosin and caldesmon in saturating amounts relative to actin inhibited the activity of gelsolin by between 21 and 40% and 25 and 48% respectively, depending on the molar ratio of gelsolin to actin. The inhibitory effect was increased with a combination of both (up to 67%) although it was evident that even under these conditions the actin filaments were not fully protected from being severed by gelsolin. These findings were corroborated by electron-microscopic investigation of actin filaments with or without tropomyosin and caldesmon after the addition of gelsolin.

Indexed as

ActinsAnimalsCa(2+) Mg(2+)-ATPaseCalmodulin-Binding ProteinsChickensEnzyme ActivationGelsolinIn Vitro TechniquesMicroscopy, ElectronMyosinsRabbitsSwineTropomyosinActinsCa(2+) Mg(2+)-ATPaseCalmodulin-Binding ProteinsGelsolinMyosinsTropomyosin

Identifiers

PMID8645154
PMCPMC1217271
OpenAlexW13830274

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.