Evidence map›Paper›PMID 19237425›Full record

ArticleThe Journal of physiology2009

The deacetylase enzyme SIRT1 is not associated with oxidative capacity in rat heart and skeletal muscle and its overexpression reduces mitochondrial biogenesis.

Brendon J Gurd, Yuko Yoshida, James Lally, Graham P Holloway, Arend Bonen

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
5.3field-weighted citation impact, top 5% 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

44 citing papers in PubMed, 88 citations in OpenAlex.

  1. Trial
  2. Trial
  3. Skeletal muscle NAMPT is induced by exercise in humans.American journal of physiology. Endocrinology and metabolism · 2010
    Trial
  4. Article
  5. Review
  6. NADSports medicine (Auckland, N.Z.) · 2022
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Resistive Training and Molecular Regulators of Vascular-Metabolic Risk in Chronic Stroke.Journal of stroke and cerebrovascular diseases : the official journal of National Stroke Association · 2017
    Article
  17. Sirt1 and the Mitochondria.Molecules and cells · 2016
    Review
  18. Article
  19. Article
  20. Review
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.

Brendon J GurdDepartment of Human Health and Nutritional Science, University of Guelph, Guelph, Ontario, Canada, N1G 2W1.
Yuko Yoshida
James Lally
Graham P Holloway
Arend Bonen
University of Guelph · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Deacetylation of PGC-1alpha by SIRT1 is thought to be an important step in increasing PGC-1alpha transcriptional activity, since in muscle cell lines SIRT1 induces PGC-1alpha protein expression and mitochondrial biogenesis. We examined the relationship between SIRT1 protein and activity, PGC-1alpha and markers of mitochondrial density, (a) across a range of metabolically heterogeneous skeletal muscles and the heart, and when mitochondrial biogenesis was stimulated by (b) chronic muscle stimulation (7 days) and (c) AICAR administration (5 days), and finally, (d) we also examined the effects of SIRT1 overexpression on mitochondrial biogenesis and PGC-1alpha. SIRT1 protein and activity were correlated (r = 0.97). There were negative correlations between SIRT1 protein and PGC-1alpha (r = -0.95), COX IV (r = -0.94) and citrate synthase (r = -0.97). Chronic muscle stimulation and AICAR upregulated PGC-1alpha protein (22-159%) and oxidative capacity (COX IV, 20-69%); in each instance SIRT1 protein was downregulated by 20-40%, while SIRT1 intrinsic activity was increased. SIRT1 overexpression in rodent muscle increased SIRT1 protein (+240%) and doubled SIRT1 activity, but PGC-1alpha (-25%), mtTFA (-14%) and COX IV (-10%) proteins were downregulated. Taken altogether these experiments are not consistent with the notion that SIRT1 protein plays an obligatory regulatory role in the process of PGC-1alpha-mediated mitochondrial biogenesis in mammalian muscle.

Indexed as

Aminoimidazole CarboxamideAnimalsBlotting, WesternCell LineCitrate (si)-SynthaseDNA-Binding ProteinsElectric StimulationElectron Transport Complex IVFemaleHypoglycemic AgentsMitochondria, HeartMitochondrial ProteinsMitochondria, MuscleMuscle Fibers, Fast-TwitchMuscle Fibers, Slow-TwitchMuscle, SkeletalAICA ribonucleotideAminoimidazole CarboxamideCitrate (si)-SynthaseDNA-Binding ProteinsElectron Transport Complex IVHypoglycemic AgentsMitochondrial Proteinsmitochondrial transcription factor APeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaPpargc1a protein, ratRibonucleotidesRNA-Binding ProteinsSirt1 protein, ratSirtuin 1SirtuinsTranscription Factors

Identifiers

PMID19237425
PMCPMC2683967
OpenAlexW1833127055

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.