Evidence map›Paper›PMID 24512907›Full record

ArticleFree radical biology & medicine2014

The cellular distribution of extracellular superoxide dismutase in macrophages is altered by cellular activation but unaffected by the naturally occurring R213G substitution.

Randi H Gottfredsen, David A Goldstrohm, John M Hartney, Ulrike G Larsen, Russell P Bowler, Steen V Petersen

Open access · greenAbstract read
In one paragraph

Article in Free radical biology & medicine, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.6field-weighted citation impact, top 12% 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

16 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Redistribution of EC-SOD resolves bleomycin-induced inflammationFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  6. Article
  7. Article
  8. Mitochondria in innate immune signaling.Translational research : the journal of laboratory and clinical medicine · 2018
    Review
  9. Article
  10. Review
  11. Extracellular superoxide dismutase and its role in cancer.Free radical biology & medicine · 2017
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. 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

6 authors at 3 institutions in 2 countries.

Randi H GottfredsenDepartment of Biomedicine, Aarhus University, DK-8000 Aarhus, Denmark.
David A GoldstrohmDepartment of Medicine, National Jewish Health, Denver, CO 80206, USA.
John M HartneyDepartment of Medicine, National Jewish Health, Denver, CO 80206, USA.
Ulrike G LarsenDepartment of Biomedicine, Aarhus University, DK-8000 Aarhus, Denmark.
Russell P BowlerDepartment of Medicine, National Jewish Health, Denver, CO 80206, USA.
Steen V PetersenDepartment of Biomedicine, Aarhus University, DK-8000 Aarhus, Denmark. Electronic address: svp@biokemi.au.dk.
Aarhus University · DKUniversity of Colorado Denver · USNational Jewish Health · US

Funding

Investigating the role of the R213G SOD3 polymorphism in lung diseaseR01HL111288 · NHLBI · NATIONAL JEWISH HEALTH · PI BOWLER, RUSSELL PAUL · 2012 to 2015
$1.1M
NHLBI NIH HHS HL11-1288NHLBI NIH HHS R01 HL111288
6 · The paper itself

Abstract

Extracellular superoxide dismutase (EC-SOD) is responsible for the dismutation of the superoxide radical produced in the extracellular space and known to be expressed by inflammatory cells, including macrophages and neutrophils. Here we show that EC-SOD is produced by resting macrophages and associated with the cell surface via the extracellular matrix (ECM)-binding region. Upon cellular activation induced by lipopolysaccharide, EC-SOD is relocated and detected both in the cell culture medium and in lipid raft structures. Although the secreted material presented a significantly reduced ligand-binding capacity, this could not be correlated to proteolytic removal of the ECM-binding region, because the integrity of the material recovered from the medium was comparable to that of the cell surface-associated protein. The naturally occurring R213G amino acid substitution located in the ECM-binding region of EC-SOD is known to affect the binding characteristics of the protein. However, the analysis of macrophages expressing R213G EC-SOD did not present evidence of an altered cellular distribution. Our results suggest that EC-SOD plays a dynamic role in the inflammatory response mounted by activated macrophages.

Indexed as

Amino Acid SubstitutionAnimalsExtracellular MatrixExtracellular SpaceHumansInflammationLipopolysaccharidesMacrophagesMiceMutationNeutrophilsProtein BindingSuperoxide DismutaseSuperoxidesLipopolysaccharidesSod3 protein, mouseSuperoxide DismutaseSuperoxidesAntioxidantExtracellular superoxide dismutaseFree radicalsInflammationMacrophage

Identifiers

PMID24512907
PMCPMC4440334
OpenAlexW2014582520

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.