Evidence map›Paper›PMID 19700648›Full record

ArticleAmerican journal of physiology. Lung cellular and molecular physiology2009

Identification of the amino acid sequence that targets peroxiredoxin 6 to lysosome-like structures of lung epithelial cells.

Elena M Sorokina, Sheldon I Feinstein, Tatyana N Milovanova, Aron B Fisher

Open access · greenAbstract read
In one paragraph

Article in American journal of physiology. Lung cellular and molecular physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

29 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. The Roles of Phospholipase AFrontiers in cell and developmental biology · 2021
    Review
  9. Review
  10. Review
  11. Mouse Models of Genetically Altered Peroxiredoxin 6.Antioxidants (Basel, Switzerland) · 2019
    Review
  12. Article
  13. The Role of Peroxiredoxin 6 in Cell Signaling.Antioxidants (Basel, Switzerland) · 2018
    Review
  14. The phospholipase AJournal of lipid research · 2018
    Review
  15. Article
  16. Review
  17. 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 1 institution in 1 country.

Elena M SorokinaInstitute for Environmental Medicine, University of Pennsylvania, One John Morgan Bldg., 3620 Hamilton Walk, Philadelphia, PA 19104, USA.
Sheldon I Feinstein
Tatyana N Milovanova
Aron B Fisher
University of Pennsylvania · US

Funding

UPTAKE AND REUTILIZATION OF SURFACTANT COMPONENTSP01HL019737 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI FISHER, ARON B. · 1985 to 2013
$23.6M
Reactive oxygen species and anti-oxidants in ALIP01HL079063 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI BATES, SANDRA R · 2005 to 2009
$12.1M
Role of Peroxiredoxin 6 in the Repair of Peroxidized Cell MembranesR01HL102016 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI FISHER, ARON B. · 2010 to 2018
$4.6M
NHLBI NIH HHS HL-19737NHLBI NIH HHS HL-79063
6 · The paper itself

Abstract

Peroxiredoxin 6 (Prdx6), an enzyme with glutathione peroxidase and PLA2 (aiPLA2) activities, is highly expressed in respiratory epithelium, where it participates in phospholipid turnover and antioxidant defense. Prdx6 has been localized by immunocytochemistry and subcellular fractionation to acidic organelles (lung lamellar bodies and lysosomes) and cytosol. On the basis of their pH optima, we have postulated that protein subcellular localization determines the balance between the two activities of Prdx6. Using green fluorescent protein-labeled protein expression in alveolar epithelial cell lines, we showed Prdx6 localization to organellar structures resembling lamellar bodies in mouse lung epithelial (MLE-12) cells and lysosomes in A549 cells. Localization within lamellar bodies/lysosomes was in the luminal compartment. Targeting to lysosome-like organelles was abolished by the deletion of amino acids 31-40 from the Prdx6 NH2-terminal region; deletion of the COOH-terminal region had no effect. A green fluorescent protein-labeled peptide containing only amino acids 31-40 showed lysosomal targeting that was abolished by mutation of S32 or G34 within the peptide. Studies with mutated protein indicated that lipid binding was not necessary for Prdx6 targeting. This peptide sequence has no homology to known organellar targeting motifs. These studies indicate that the localization of Prdx6 in acidic organelles and consequent PLA2 activity depend on a novel 10-aa peptide located at positions 31-40 of the protein.

Indexed as

Protein Sorting SignalsAmino Acid SequenceAnimalsCell LineEpithelial CellsGreen Fluorescent ProteinsHumansHydrogen-Ion ConcentrationLiposomesLungLysosomesMiceMutagenesis, Site-DirectedMutant ProteinsMutationPeptidesGreen Fluorescent ProteinsLiposomesMutant ProteinsPeptidesPeroxiredoxin VIProtein Sorting SignalsRecombinant Fusion Proteins

Identifiers

PMID19700648
PMCPMC2777491
OpenAlexW1991015116

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.