Evidence map›Paper›PMID 19580808›Full record

ArticleExperimental cell research2009

Hsp27 associates with the titin filament system in heat-shocked zebrafish cardiomyocytes.

Nathan R Tucker, Eric A Shelden

Open access · greenAbstract read
In one paragraph

Article in Experimental cell research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.2field-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

11 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Effect of glutamine on heat-shock protein beta 1 (Food science and biotechnology · 2018
    Article
  3. Therapeutic potential of heat shock protein induction for muscular dystrophy and other muscle wasting conditions.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Small heat shock proteins in redox metabolism: implications for cardiovascular diseases.The international journal of biochemistry & cell biology · 2012
    Review
  10. Review
  11. 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

2 authors at 1 institution in 1 country.

Nathan R TuckerSchool of Molecular Biosciences, Washington State University, Pullman, WA 99164, USA.
Eric A Shelden
Washington State University · US

Funding

TRAINING IN BIOTECHNOLOGY: EMPHASIS ON PROTEIN CHEMISTRYT32GM008336 · NIGMS · WASHINGTON STATE UNIVERSITY · PI CALL, DOUGLAS R. · 1989 to 2023
$8.9M
NIGMS NIH HHS T32 GM008336NIGMS NIH HHS T32-GM008336
6 · The paper itself

Abstract

Injury to muscle tissue plays a central role in various cardiovascular pathologies. Overexpression of the small heat shock protein Hsp27 protects muscle cells against thermal, oxidative and ischemic stress. However, underlying mechanisms of this protection have not been resolved. A distinctive feature of muscle cells is the stress-induced association of Hsp27 with the sarcomere. The association of Hsp27 with the cytoskeleton, in both muscle and non-muscle cells, is thought to represent interaction with Z-line components or filamentous actin. Here, we examined the association of Hsp27 with myofibrils in adult zebrafish myocardium subjected to hyperthermia and mechanical stretching. Consistent with previously published results, Hsp27 in resting length myofibrils localized to narrowly defined regions, or bands, which colocalized with Z-line markers. However, analysis of stretched myofibrils revealed that the association of Hsp27 with myofibrils was independent of desmin, alpha-actinin, myosin, and filamentous actin. Instead, Hsp27 maintained a consistent relationship with a marker for the titin A/I border over various sarcomeric lengths. Finally, extraction of actin filaments revealed that Hsp27 binds to a component of the remaining sarcomere. Together, these novel data support a mechanism of Hsp27 function where interactions with the titin filament system protect myofibrils from stress-induced degradation.

Indexed as

Actin CytoskeletonActinsAnimalsConnectinDesminHeat-Shock ResponseHSP27 Heat-Shock ProteinsMuscle ProteinsMusclesMyocardiumMyocytes, CardiacMyofibrilsMyosinsProtein KinasesZebrafishZebrafish ProteinsActinsConnectinDesminHSP27 Heat-Shock Proteinshspb1 protein, zebrafishMuscle ProteinsMyosinsProtein KinasesZebrafish Proteins

Identifiers

PMID19580808
PMCPMC2908402
OpenAlexW1998414533

What OpenQuestion holds

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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.