Evidence map›Paper›PMID 19140803›Full record

ArticleThe Biochemical journal2009

Mitogen-activated protein kinase-mediated phosphorylation of peroxiredoxin 6 regulates its phospholipase A(2) activity.

Yongzheng Wu, Sheldon I Feinstein, Yefim Manevich, Ibrul Chowdhury, Jhang Ho Pak, Altaf Kazi, Chandra Dodia, David W Speicher, Aron B Fisher

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

59 citing papers in PubMed, 94 citations in OpenAlex.

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  17. Genetic inactivation of the phospholipase AAmerican journal of physiology. Lung cellular and molecular physiology · 2019
    Article
  18. Mouse Models of Genetically Altered Peroxiredoxin 6.Antioxidants (Basel, Switzerland) · 2019
    Review
  19. Review
  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

9 authors at 2 institutions in 1 country.

Yongzheng WuInstitute for Environmental Medicine, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6068, U.S.A.
Sheldon I Feinstein
Yefim Manevich
Ibrul Chowdhury
Jhang Ho Pak
Altaf Kazi
Chandra Dodia
David W Speicher
Aron B Fisher
University of Pennsylvania · USThe Wistar Institute · 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
Membrane Proteins of Normal and Abnormal Red CellsR01HL038794 · NHLBI · WISTAR INSTITUTE · PI SPEICHER, DAVID W. · 1987 to 2013
$5.1M
NHLBI NIH HHS HL 19737NHLBI NIH HHS HL 79063NHLBI NIH HHS P01 HL019737NHLBI NIH HHS P01 HL079063NHLBI NIH HHS R01 HL038794
6 · The paper itself

Abstract

Prdx6 (peroxiredoxin 6), a bifunctional protein with both GSH peroxidase and PLA(2) (phospholipase A(2)) [aiPLA(2) (acidic calcium-independent PLA(2))] activities, is responsible for the metabolism of lung surfactant phospholipids. We propose that the aiPLA(2) activity of the enzyme is regulated through phosphorylation. Incubation of isolated rat alveolar type II cells (AECII) with PMA, a PKC (protein kinase C) agonist, had no effect on Prdx6 expression but led to approximately 75% increase in aiPLA(2) activity that was abolished by pretreatment of cells with the MAPK (mitogen-activated protein kinase) inhibitors, SB202190 or PD98059. Prdx6 phosphorylation after incubation of AECII with PMA was demonstrated by autoradiography after immunoprecipitation with either anti-phosphothreonine o-phosphoserine antibodies. in vitro, several active isoforms of ERK (extracellular-signal-regulated kinase) and p38 phosphorylated Prdx6, resulting in an 11-fold increase in aiPLA(2) activity. The increased activity was calcium-independent and was abolished by the aiPLA(2) inhibitors, surfactant protein A and hexadecyl-3-trifluorethylglycero-sn-2-phospho-methanol (MJ33). The peroxidase activity of Prdx6 was unaffected by phosphorylation. Mass spectroscopic analysis of in vitro phosphorylated Prdx6 showed a unique phosphorylation site at Thr-177 and mutation of this residue abolished protein phosphorylation and the increase in MAPK-mediated activity. These results show that the MAPKs can mediate phosphorylation of Prdx6 at Thr-177 with a consequent marked increase in its aiPLA(2) activity.

Indexed as

AnimalsCell ExtractsElectrophoresis, Gel, Two-DimensionalEndocytosisHumansImmunoprecipitationMitogen-Activated Protein KinasesMutationPeroxiredoxin VIPhospholipases A2PhosphorylationProtein Kinase CProtein Kinase InhibitorsProtein Processing, Post-TranslationalPulmonary AlveoliRatsCell ExtractsMitogen-Activated Protein KinasesPeroxiredoxin VIPhospholipases A2Protein Kinase CProtein Kinase InhibitorsTetradecanoylphorbol AcetateThreonine

Identifiers

PMID19140803
PMCPMC2770719
OpenAlexW1980168717

What OpenQuestion holds

Textmetadata
LicenceTDM
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.