Evidence map›Paper›PMID 22824865›Full record

ArticleFree radical biology & medicine2012

Ceruloplasmin (ferroxidase) oxidizes hydroxylamine probes: deceptive implications for free radical detection.

Douglas Ganini, Donatella Canistro, JinJie Jiang, JinJie Jang, Krisztian Stadler, Ronald P Mason, Maria B Kadiiska

Erratum issuedAbstract read
In one paragraph

Article in Free radical biology & medicine, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

11 citing papers in PubMed, 27 citations in OpenAlex.

  1. Copper speciation in dairy cattle with different productivity levels.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2025
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Molecular Functions of Ceruloplasmin in Metabolic Disease Pathology.Diabetes, metabolic syndrome and obesity : targets and therapy · 2022
    Review
  8. Article
  9. Review
  10. Article
  11. Article
4 · The record

Corrections and comments

  • Erratum issued
    Jang, JinJie [corrected to Jiang, JinJie]
5 · Who and what money

Authors and funding

7 authors at 4 institutions in 2 countries.

Douglas GaniniFree Radical Metabolism Section, Laboratory of Toxicology and Pharmacology, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709, USA.
Donatella Canistro
JinJie Jiang
JinJie Jang
Krisztian Stadler
Ronald P Mason
Maria B Kadiiska
National Institute of Environmental Health Sciences · USNational Institutes of Health · USPennington Biomedical Research Center · USUniversity of Bologna · IT

Funding

Protein Derived RadicalsZIAES050139 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI MASON, RONALD P · 2009 to 2018
$17.5M
PROTEIN DERIVED RADICALSZ01ES050139 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI MASON, RONALD P · 1995 to 2008
$4.7M
Intramural NIH HHS Z01 ES050139Intramural NIH HHS ZIA ES050139
6 · The paper itself

Abstract

Ceruloplasmin (ferroxidase) is a copper-binding protein known to promote Fe(2+) oxidation in plasma of mammals. In addition to its classical ferroxidase activity, ceruloplasmin is known to catalyze the oxidation of various substrates, such as amines and catechols. Assays based on cyclic hydroxylamine oxidation are used to quantify and detect free radicals in biological samples ex vivo and in vitro. We show here that human ceruloplasmin promotes the oxidation of the cyclic hydroxylamine 1-hydroxy-3-carboxy-2,2,5,5-tetramethylpyrrolidine hydrochloride (CPH) and related probes in Chelex-treated phosphate buffer and rat serum. The reaction is suppressed by the metal chelators DTPA, EDTA, and desferal, whereas heparin and bathocuproine have no effect. Catalase or superoxide dismutase additions do not interfere with the CPH-oxidation yield, demonstrating that oxygen-derived free radicals are not involved in the CPH oxidation mediated by ceruloplasmin. Plasma samples immunodepleted of ceruloplasmin have lower levels of CPH oxidation, which confirms the role of ceruloplasmin (ferroxidase) as a biological oxidizing agent of cyclic hydroxylamines. In conclusion, we show that the ferroxidase activity of ceruloplasmin is a possible biological source of artifacts in the cyclic hydroxylamine-oxidation assay used for reactive oxygen species detection and quantification.

Indexed as

Biological AssayAnimalsArtifactsCatalaseCeruloplasminChelating AgentsDeferoxamineEdetic AcidFree RadicalsHeparinHumansHydroxylaminesOxidantsOxidation-ReductionPentetic AcidPhenanthrolinesbathocuproineCatalaseCeruloplasminChelating AgentsDeferoxamineEdetic AcidFree RadicalsHeparinHydroxylaminesOxidantsPentetic AcidPhenanthrolinesSuperoxide Dismutase

Identifiers

PMID22824865
PMCPMC3448871
OpenAlexW1994866496

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.