Evidence map›Paper›PMID 12693988›Full record

ArticleThe Biochemical journal2003

Subcellular localization of methionine sulphoxide reductase A (MsrA): evidence for mitochondrial and cytosolic isoforms in rat liver cells.

Stéphanie Vougier, Jean Mary, Bertrand Friguet

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

40 citing papers in PubMed, 112 citations in OpenAlex.

  1. Article
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  4. Article
  5. Proteomic analyses revealed the antibacterial mechanism ofCurrent research in food science · 2022
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Astragaloside IV rescues MPPExperimental and therapeutic medicine · 2017
    Article
  12. Article
  13. Article
  14. Article
  15. Control of mitochondrial integrity in ageing and disease.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014
    Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Myristoylated methionine sulfoxide reductase A protects the heart from ischemia-reperfusion injury.American journal of physiology. Heart and circulatory physiology · 2011
    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

3 authors at 1 institution in 1 country.

Stéphanie VougierLaboratoire de Biologie et Biochimie Cellulaire du Vieillissement, Université Denis Diderot-Paris 7, CC 7128, 2 place Jussieu, 75251 Paris Cedex 05, France.
Jean Mary
Bertrand Friguet
Université Paris Cité · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins are sensitive to reactive oxygen species, and the accumulation of oxidized proteins has been implicated in the aging process and in other age-related pathologies. In proteins, methionine residues are especially sensitive to oxidation, leading to S - and R -methionine sulphoxide diastereoisomers, the reversion of which is achieved by the peptide methionine sulphoxide reductases MsrA and MsrB respectively. The MsrA enzyme, in addition to its role in repair, forms part of the reactive oxygen species scavenging systems that are important in cellular antioxidant defence. MsrA is present in most living organisms, and the mammalian enzyme has been detected in all tissues investigated. In the present study, we investigated the subcellular distribution of MsrA in rat liver cells. Since it seemed likely that MsrA may be localized in areas where reactive oxygen species are produced, rat liver mitochondrial matrix and cytosolic extracts were prepared. The presence of MsrA was assayed in these subcellular compartments by monitoring peptide methionine sulphoxide reductase enzymic activity, by Western blotting and by in situ immunolocalization by electron microscopy using a specific antibody. Moreover, MsrA was identified by MS in a partially purified cytosolic fraction and in a mitochondrial matrix crude extract. Rat MsrA isoforms are encoded by a single gene, and it is suggested that the precursor of the mitochondrial form contains an N-terminal cleavable signal sequence that localizes the MsrA to this organelle. Finally, two-dimensional gel electrophoresis followed by Western-blot analysis of partially purified MsrA from the cytosol and mitochondria, and comparison with the two-dimensional patterns of oxidized recombinant MsrA, revealed oxidative modifications of cysteine residues.

Indexed as

Amino Acid SequenceAnimalsBlotting, WesternCells, CulturedCytosolElectrophoresis, Gel, Two-DimensionalIsoenzymesLiverMass SpectrometryMethionine Sulfoxide ReductasesMicroscopy, ElectronMitochondria, LiverMolecular Sequence DataOxidation-ReductionOxidoreductasesPeptide FragmentsIsoenzymesmethionine sulfoxide reductaseMethionine Sulfoxide ReductasesOxidoreductasesPeptide FragmentsRecombinant Proteins

Identifiers

PMID12693988
PMCPMC1223498
OpenAlexW1976338581

What OpenQuestion holds

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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.