Evidence map›Paper›PMID 24532005›Full record

ArticleMolecular and cellular biochemistry2014

Lysine suppresses protein degradation through autophagic-lysosomal system in C2C12 myotubes.

Tomonori Sato, Yoshiaki Ito, Taku Nedachi, Takashi Nagasawa

Abstract read
PubMed Publisher
In one paragraph

Article in Molecular and cellular biochemistry, 2014. 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
2.1field-weighted citation impact, top 13% 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, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. α-Ketoglutarate prevents skeletal muscle protein degradation and muscle atrophy through PHD3/ADRB2 pathway.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018
    Article
  18. Article
  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 2 institutions in 1 country.

Tomonori SatoDepartment of Biological Chemistry and Food Science, Graduate School of Agriculture, Iwate University, Morioka, Iwate, 020-8550, Japan.
Yoshiaki Ito
Taku Nedachi
Takashi Nagasawa
Iwate University · JPToyo University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Muscle mass is determined between protein synthesis and protein degradation. Reduction of muscle mass leads to bedridden condition and attenuation of resistance to diseases. Moreover, bedridden condition leads to additional muscle loss due to disuse muscle atrophy. In our previous study (Sato et al. 2013), we showed that administered lysine (Lys), one of essential amino acid, suppressed protein degradation in skeletal muscle. In this study, we investigated that the mechanism of the suppressive effects of Lys on skeletal muscle proteolysis in C2C12 cell line. C2C12 myotubes were incubated in the serum-free medium containing 10 mM Lys or 20 mM Lys, and myofibrillar protein degradation was determined by the rates of 3-methylhistidine (MeHis) release from the cells. The mammalian target of rapamycin (mTOR) activity from the phosphorylation levels of p70-ribosormal protein S6 kinase 1 and eIF4E-binding protein 1 and the autophagic-lysosomal system activity from the ratio of LC3-II/I in C2C12 myotubes stimulated by 10 mM Lys for 0-3 h were measured. The rates of MeHis release were markedly reduced by addition of Lys. The autophagic-lysosomal system activity was inhibited upon 30 min of Lys supplementation. The activity of mTOR was significantly increased upon 30 min of Lys supplementation. The suppressive effect of Lys on the proteolysis by the autophagic-lysosomal system was maintained partially when mTOR activity was inhibited by 100 nM rapamycin, suggesting that some regulator other than mTOR signaling, for example, Akt, might also suppress the autophagic-lysosomal system. From these results, we suggested that Lys suppressed the activity of the autophagic-lysosomal system in part through activation of mTOR and reduced myofibrillar protein degradation in C2C12 myotubes.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsAutophagyCarrier ProteinsCell Cycle ProteinsEukaryotic Initiation FactorsGene Expression RegulationLysineLysosomesMethylhistidinesMiceMicrotubule-Associated ProteinsMuscle Fibers, SkeletalMuscle ProteinsMyofibrilsPhosphoproteinsAdaptor Proteins, Signal TransducingCarrier ProteinsCell Cycle ProteinsEif4ebp1 protein, mouseEukaryotic Initiation FactorsLysineMap1lc3b protein, mouseMethylhistidinesMicrotubule-Associated ProteinsMuscle ProteinsPhosphoproteinsProteasome Endopeptidase ComplexRNA, MessengerTOR Serine-Threonine KinasesTrim63 protein, mouseTripartite Motif ProteinsUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID24532005
OpenAlexW2024700954

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.