Evidence map›Paper›PMID 2834402›Full record

ArticleThe Journal of cell biology1988

Localization and mobility of gelsolin in cells.

J A Cooper, D J Loftus, C Frieden, J Bryan, E L Elson

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

16 citing papers in PubMed, 61 citations in OpenAlex.

  1. Regulation of Mitochondrial Function by the Actin Cytoskeleton.Frontiers in cell and developmental biology · 2021
    Review
  2. Article
  3. Quantification of fibre polymerization through Fourier space image analysis.Proceedings. Mathematical, physical, and engineering sciences · 2011
    Article
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  8. An actin-associated protein present in the microtubule organizing center and the growth cones of PC-12 cells.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1992
    Article
  9. Article
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  12. Article
  13. Review
  14. Article
  15. Isolation and characterization of gelsolin from cultured BHK cells.Journal of muscle research and cell motility · 1989
    Article
  16. 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

5 authors at 1 institution in 1 country.

J A CooperDepartment of Biological Chemistry, Washington University School of Medicine, St. Louis Missouri 63110.
D J Loftus
C Frieden
J Bryan
E L Elson
Washington University in St. Louis · US

Funding

CHEMISTRY AND LOCALIZATION OF ACTIN GELLING PROTEINSR01GM026091 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI BRYAN, JOSEPH · 1985 to 1998
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BIOPHYSICAL STUDIES OF CELL DEFORMABILITYR01GM027160 · NIGMS · WASHINGTON UNIVERSITY · PI ELSON, ELLIOT L. · 1985 to 1986
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NIGMS NIH HHS GM 13332NIGMS NIH HHS GM 26091NIGMS NIH HHS GM 27160
6 · The paper itself

Abstract

To investigate the physiologic role of gelsolin in cells, we have studied the location and mobility of gelsolin in a mouse fibroblast cell line (C3H). Gelsolin was localized by immunofluorescence of fixed and permeabilized cells and by fluorescent analog cytochemistry of living cells and cells that were fixed and/or permeabilized. Overall, the images show that in living cells gelsolin has a diffuse cytoplasmic distribution, but in fixed cells a minor fraction is associated with regions of the cell that are rich in actin filaments. The latter fraction is more prominent after permeabilization of the fixed cells because some diffuse gelsolin is not fixed and is therefore lost during permeabilization, confirmed by immunoblots. To determine quantitatively whether gelsolin is bound to actin filaments in living cells, we measured the mobility of microinjected fluorescent gelsolin by fluorescence photobleaching recovery. Gelsolin is fully mobile with a diffusion coefficient similar to that of control proteins. As a positive control, fluorescent phalloidin, which binds actin filaments, is totally immobile. These results are supported by immunoblots on cells permeabilized with detergent. All the endogenous gelsolin is extracted, and the half-time for the extraction is approximately 5 s, which is about the rate predicted for diffusion. Therefore, gelsolin is not tightly bound to actin filaments in cells. The most likely interpretation of the difference between living and fixed cells is that fixation traps a fraction of gelsolin that is associated with actin filaments in short-lived complexes.

Indexed as

AnimalsBlood PlateletsCalcium-Binding ProteinsCell LineCytoplasmCytoskeletonFixativesFluorescent Antibody TechniqueGelsolinHistocytochemistryImmunoassayMicrofilament ProteinsMicroinjectionsSoftwareCalcium-Binding ProteinsFixativesGelsolinMicrofilament Proteins

Identifiers

PMID2834402
PMCPMC2115018
OpenAlexW2016924776

What OpenQuestion holds

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LicenceCC BY-NC-SA
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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.