Evidence map›Paper›PMID 26687331›Full record

ReviewCancer medicine2016

Xanthine oxidoreductase in cancer: more than a differentiation marker.

Maria Giulia Battelli, Letizia Polito, Massimo Bortolotti, Andrea Bolognesi

Open access · goldAbstract readReview
In one paragraph

Review in Cancer medicine, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed, 1 pooled it
3.5field-weighted citation impact, top 7% 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

84 citing papers in PubMed, 1 synthesis or guideline pooled it, 161 citations in OpenAlex.

  1. Pooled it
  2. Cancer risk in Korean patients with gout.The Korean journal of internal medicine · 2022
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24 more citing papers are in PubMed but not listed here.

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.

Maria Giulia BattelliDepartment of Experimental, Diagnostic and Specialty Medicine - DIMES, Alma Mater Studiorum - University of Bologna, General Pathology Unit, Via S. Giacomo 14, 40126, Bologna, Italy.
Letizia PolitoDepartment of Experimental, Diagnostic and Specialty Medicine - DIMES, Alma Mater Studiorum - University of Bologna, General Pathology Unit, Via S. Giacomo 14, 40126, Bologna, Italy.
Massimo BortolottiDepartment of Experimental, Diagnostic and Specialty Medicine - DIMES, Alma Mater Studiorum - University of Bologna, General Pathology Unit, Via S. Giacomo 14, 40126, Bologna, Italy.
Andrea BolognesiDepartment of Experimental, Diagnostic and Specialty Medicine - DIMES, Alma Mater Studiorum - University of Bologna, General Pathology Unit, Via S. Giacomo 14, 40126, Bologna, Italy.
University of Bologna · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human xanthine oxidoreductase (XOR) catalyzes the last two steps of purine catabolism and is present in two interconvertible forms, which may utilize O2 or NAD(+) as electron acceptors. In addition to uric acid, XOR products may comprise reactive oxygen and nitrogen species that have many biologic effects, including inflammation, endothelial dysfunction, and cytotoxicity, as well as mutagenesis and induction of proliferation. XOR is strictly modulated at the transcriptional and post-translational levels, and its expression and activity are highly variable in cancer. Xanthine oxidoreductase (XOR) expression has been negatively associated with a high malignity grade and a worse prognosis in neoplasms of the breast, liver, gastrointestinal tract, and kidney, which normally express a high level of XOR protein. However, the level of XOR expression may be associated with a worse outcome in cancer of low XOR-expressing cells, in relation to the inflammatory response elicited through the tissue damage induced by tumor growth. Xanthine oxidoreductase (XOR) has been implicated in the process of oncogenesis either directly because it is able to catalyze the metabolic activation of carcinogenic substances or indirectly through the action of XOR-derived reactive oxygen and nitrogen species. The role of uric acid is characterized by both oxidant and antioxidant action; thus, it is still debatable whether control of uricemia may be helpful to improve the outcomes of tumor illness.

Indexed as

AnimalsGene Expression Regulation, NeoplasticHumansNeoplasmsPrognosisReactive Nitrogen SpeciesReactive Oxygen SpeciesUric AcidXanthine DehydrogenaseReactive Nitrogen SpeciesReactive Oxygen SpeciesUric AcidXanthine DehydrogenaseDifferentiationoncogenesisreactive oxygen and nitrogen speciesuric acidxanthine oxidoreductase

Identifiers

PMID26687331
PMCPMC4799950
OpenAlexW2272073785

What OpenQuestion holds

Textmetadata
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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.