Evidence map›Paper›PMID 12380682›Full record

ArticleCell stress & chaperones2002

Distribution, phosphorylation, and activities of Hsp25 in heat-stressed H9c2 myoblasts: a functional link to cytoprotection.

Anton L Bryantsev, Svetlana A Loktionova, Olga P Ilyinskaya, Eduard M Tararak, Harm H Kampinga, Alexander E Kabakov

Open access · greenAbstract read
In one paragraph

Article in Cell stress & chaperones, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

28 citing papers in PubMed, 66 citations in OpenAlex.

  1. Small heat shock proteins and biomolecular condensates.Cellular and molecular life sciences : CMLS · 2026
    Review
  2. Review
  3. Review
  4. The protective role of HSP27 in ocular diseases.Molecular biology reports · 2022
    Review
  5. Review
  6. Review
  7. Review
  8. Review
  9. Untying the knot: protein quality control in inherited cardiomyopathies.Pflugers Archiv : European journal of physiology · 2019
    Review
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  11. Article
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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

6 authors at 1 institution in 1 country.

Anton L BryantsevMolecular and Cellular Cardiology Lab, Institute of Experimental Cardiology, Cardiology Research Centre, Moscow, Russia. cardiocell@cardio.ru
Svetlana A Loktionova
Olga P Ilyinskaya
Eduard M Tararak
Harm H Kampinga
Alexander E Kabakov
Institute of Experimental Cardiology · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The behavior of the endogenous heat shock protein 25 (Hsp25) in heat-stressed rat H9c2 myoblasts was studied. After mild or severe heating, this protein became less extractable with Triton X-100 and displayed characteristic immunofluorescence patterns, namely (1) granules in the nucleus, and (2) association with F-actin bundles in the cytoplasm. The intranuclear granulation of Hsp25 and its association with F-actin were sensitive to drugs affecting Hsp25 phosphorylation (cantharidin, sodium orthovanadate, SB203580, SB202190). Isoform analysis of Hsp25 translocated to the nucleus-free cytoskeletal fraction revealed only mono- and biphosphorylated Hsp25 and no unphosphorylated Hsp25. Transfected luciferase with initial localization in the nucleosol became colocalized with the Hsp25-containing granules after a heat shock treatment that denatured the enzyme in the cells. The association of Hsp25 with actin filaments after a mild heat stress conferred protection from subsequent F-actin-damaging treatments with cytochalasins (D and B) or severe heat stress. We hypothesize that (1) the binding of heat-denatured nucleosolic proteins to the Hsp25 contained in specific granular structures may serve for the subsequent chaperoning or degradation of the bound proteins, and (2) the actin cytoskeleton is stabilized by the direct targeting of phosphorylated Hsp25 to microfilament bundles.

Indexed as

Heat-Shock ProteinsHot TemperatureAnimalsCell NucleusCell SurvivalCytoskeletonHSP27 Heat-Shock ProteinsImidazolesMitogen-Activated Protein KinasesMyoblastsNeoplasm Proteinsp38 Mitogen-Activated Protein KinasesPhosphorylationPyridinesRatsHeat-Shock ProteinsHSP27 Heat-Shock ProteinsHspb1 protein, ratImidazolesMitogen-Activated Protein KinasesNeoplasm Proteinsp38 Mitogen-Activated Protein KinasesPyridinesSB 203580

Identifiers

PMID12380682
PMCPMC514812
OpenAlexW2109186390

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.