Evidence map›Paper›PMID 24037260›Full record

ArticleJournal of muscle research and cell motility2013

Localisation of AMPK γ subunits in cardiac and skeletal muscles.

Katalin Pinter, Robert T Grignani, Hugh Watkins, Charles Redwood

Open access · hybridAbstract read
In one paragraph

Article in Journal of muscle research and cell motility, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

22 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. AMPK Localization: A Key to Differential Energy Regulation.International journal of molecular sciences · 2021
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. The Roles of AMPK in Revascularization.Cardiology research and practice · 2020
    Review
  12. Interplay Between Calcium and AMPK Signaling in Human Cytomegalovirus Infection.Frontiers in cellular and infection microbiology · 2020
    Review
  13. Article
  14. AMPK: Regulation of Metabolic Dynamics in the Context of Autophagy.International journal of molecular sciences · 2018
    Review
  15. AMPK in skeletal muscle function and metabolism.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018
    Review
  16. AMPK: guardian of metabolism and mitochondrial homeostasis.Nature reviews. Molecular cell biology · 2018
    Review
  17. Article
  18. Review
  19. Article
  20. 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 2 countries.

Katalin PinterDepartment of Cardiovascular Medicine, John Radcliffe Hospital, University of Oxford, West Wing Level 6, Oxford, OX3 9DU, UK.
Robert T Grignani
Hugh Watkins
Charles Redwood
University of Oxford · GBJohn Radcliffe Hospital · GBNational University of Singapore · SG

Funding

British Heart Foundation PG/13/5/29973British Heart Foundation RG/07/012/24110Wellcome Trust 090532
6 · The paper itself

Abstract

The trimeric protein AMP-activated protein kinase (AMPK) is an important sensor of energetic status and cellular stress, and mutations in genes encoding two of the regulatory γ subunits cause inherited disorders of either cardiac or skeletal muscle. AMPKγ2 mutations cause hypertrophic cardiomyopathy with glycogen deposition and conduction abnormalities; mutations in AMPKγ3 result in increased skeletal muscle glycogen. In order to gain further insight into the roles of the different γ subunits in muscle and into possible disease mechanisms, we localised the γ2 and γ3 subunits, along with the more abundant γ1 subunit, by immunofluorescence in cardiomyocytes and skeletal muscle fibres. The predominant cardiac γ2 variant, γ2-3B, gave a striated pattern in cardiomyocytes, aligning with the Z-disk but with punctate staining similar to T-tubule (L-type Ca(2+) channel) and sarcoplasmic reticulum (SERCA2) markers. In skeletal muscle fibres AMPKγ3 localises to the I band, presenting a uniform staining that flanks the Z-disk, also coinciding with the position of Ca(2+) influx in these muscles. The localisation of γ2-3B- and γ3-containing AMPK suggests that these trimers may have similar functions in the different muscles. AMPK containing γ2-3B was detected in oxidative skeletal muscles which had low expression of γ3, confirming that these two regulatory subunits may be co-ordinately regulated in response to metabolic requirements. Compartmentalisation of AMPK complexes is most likely dependent on the regulatory γ subunit and this differential localisation may direct substrate selection and specify particular functional roles.

Indexed as

AMP-Activated Protein KinasesAnimalsCardiomyopathiesHumansMiceMice, Inbred C57BLMicroscopy, ConfocalMuscle, SkeletalMyocardiumProtein SubunitsAMP-Activated Protein KinasesProtein Subunits

Identifiers

PMID24037260
PMCPMC3853370
OpenAlexW2067546983

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.