Evidence map›Paper›PMID 20488244›Full record

ArticleFree radical biology & medicine2010

Peroxiredoxin-2 expression is increased in beta-thalassemic mouse red cells but is displaced from the membrane as a marker of oxidative stress.

Alessandro Matte, Philip S Low, Franco Turrini, Mariarita Bertoldi, Maria Estela Campanella, Daniela Spano, Antonella Pantaleo, Angela Siciliano, Lucia De Franceschi

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Article in Free radical biology & medicine, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

39 citing papers in PubMed, 62 citations in OpenAlex.

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  5. Nrf2 Plays a Key Role in Erythropoiesis during Aging.Antioxidants (Basel, Switzerland) · 2024
    Article
  6. Peroxiredoxins in erythrocytes: far beyond the antioxidant role.Journal of molecular medicine (Berlin, Germany) · 2023
    Review
  7. Crosstalk betweenGenes · 2023
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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 4 institutions in 2 countries.

Alessandro MatteSection of Internal Medicine, Department of Clinical and Experimental Medicine, University of Verona, 37134 Verona, Italy.
Philip S Low
Franco Turrini
Mariarita Bertoldi
Maria Estela Campanella
Daniela Spano
Antonella Pantaleo
Angela Siciliano
Lucia De Franceschi
University of Verona · ITPurdue University West Lafayette · USInstitute of Biomembranes, Bioenergetics and Molecular Biotechnologies · ITUniversity of Turin · IT

Funding

Studies of Erythrocyte Membrane StructureR01GM024417 · NIGMS · PURDUE UNIVERSITY WEST LAFAYETTE · PI LOW, PHILIP STEWART · 1985 to 2020
$5.4M
ERYTHROCYTE MEMBRANE STRUCTURER37GM024417 · NIGMS · PURDUE UNIVERSITY WEST LAFAYETTE · PI LOW, PHILIP STEWART · 1999 to 2008
$3.5M
NIGMS NIH HHS GM24417NIGMS NIH HHS R01 GM024417NIGMS NIH HHS R37 GM024417Telethon GGP07007
6 · The paper itself

Abstract

Peroxiredoxin 2 (Prx2), the third most abundant cytoplasmic protein in red blood cells (RBCs), is involved in the defense against oxidative stress. Although much is known about Prx2 in healthy RBCs, its role in pathological RBCs remains largely unexplored. Here, we show that the expression and net content of Prx2 are markedly increased in RBCs from two mouse models of beta-thalassemia (beta-thal; Hbb(th/th) and Hbb(th3/+) strains). We also demonstrate that the increased expression of Prx2 correlates with the severity of the disease and that the amount of Prx2 bound to the membrane is markedly reduced in beta-thal mouse RBCs. To explore the impact of oxidative stress on Prx2 membrane association, we examined Prx2 dimerization and membrane translocation in murine RBCs exposed to various oxidants (phenylhydrazine, PHZ; diamide; H(2)O(2)). PHZ-treated RBCs, which mimic the membrane damage in beta-thal RBCs, exhibited a kinetic correlation among Prx2 membrane displacement, intracellular methemoglobin levels, and hemichrome membrane association, suggesting the possible masking of Prx2 docking sites by membrane-bound hemichromes, providing a possible mechanism for the accumulation of oxidized/dimerized Prx2 in the cytoplasm and the increased membrane damage in beta-thal RBCs. Thus, reduced access of Prx2 to the membrane in beta-thal RBCs represents a new factor that could contribute to the oxidative damage characterizing the pathology.

Indexed as

Animalsbeta-ThalassemiaDiamideDisease Models, AnimalErythrocyte MembraneErythrocytesFemaleHemeproteinsHydrogen PeroxideMaleMiceMice, Inbred C57BLOxidative StressPeroxiredoxinsPhenylhydrazinesDiamideHemeproteinshemichromeHydrogen PeroxidePeroxiredoxinsphenylhydrazinePhenylhydrazines

Identifiers

PMID20488244
PMCPMC3395234
OpenAlexW2083538044

What OpenQuestion holds

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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.