Evidence map›Paper›PMID 35740014›Full record

ArticleAntioxidants (Basel, Switzerland)2022

Uric Acid Reacts with Peroxidasin, Decreases Collagen IV Crosslink, Impairs Human Endothelial Cell Migration and Adhesion.

Bianca Dempsey, Litiele Cezar Cruz, Marcela Franco Mineiro, Railmara Pereira da Silva, Flavia Carla Meotti

Open access · goldAbstract read
In one paragraph

Article in Antioxidants (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

9 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. The role of peroxidasin in solid cancer progression.Biochemical Society transactions · 2023
    Review
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

5 authors at 1 institution in 1 country.

Bianca DempseyDepartment of Biochemistry, Institute of Chemistry, University of São Paulo, Av. Prof Lineu Prestes, 748. Office 1004, São Paulo 05508-000, Brazil.ORCID 0000-0001-7319-7113
Litiele Cezar CruzDepartment of Biochemistry, Institute of Chemistry, University of São Paulo, Av. Prof Lineu Prestes, 748. Office 1004, São Paulo 05508-000, Brazil.ORCID 0000-0002-6724-7812
Marcela Franco MineiroDepartment of Biochemistry, Institute of Chemistry, University of São Paulo, Av. Prof Lineu Prestes, 748. Office 1004, São Paulo 05508-000, Brazil.
Railmara Pereira da SilvaDepartment of Biochemistry, Institute of Chemistry, University of São Paulo, Av. Prof Lineu Prestes, 748. Office 1004, São Paulo 05508-000, Brazil.ORCID 0000-0002-2831-4955
Flavia Carla MeottiDepartment of Biochemistry, Institute of Chemistry, University of São Paulo, Av. Prof Lineu Prestes, 748. Office 1004, São Paulo 05508-000, Brazil.
Universidade de São Paulo · BR

Funding

São Paulo Research Foundation 2012/12663-1São Paulo Research Foundation 2016/00696-3São Paulo Research Foundation CEPID Redoxoma 2013/07937-8São Paulo Research Foundation Young Investigator 2 - 2018/14898-2
6 · The paper itself

Abstract

Uric acid is considered the main substrate for peroxidases in plasma. The oxidation of uric acid by human peroxidases generates urate free radical and urate hydroperoxide, which might affect endothelial function and explain, at least in part, the harmful effects of uric acid on the vascular system. Peroxidasin (PXDN), the most recent heme-peroxidase described in humans, catalyzes the formation of hypobromous acid, which mediates collagen IV crosslinks in the extracellular matrix. This enzyme has gained increasing scientific interest since it is associated with cardiovascular disease, cancer, and renal fibrosis. The main objective here was to investigate whether uric acid would react with PXDN and compromise the function of the enzyme in human endothelial cells. Urate decreased Amplex Red oxidation and brominating activity in the extracellular matrix (ECM) from HEK293/PXDN overexpressing cells and in the secretome of HUVECs. Parallelly, urate was oxidized to 5-hydroxyisourate. It also decreased collagen IV crosslink in isolated ECM from PFHR9 cells. Urate, the PXDN inhibitor phloroglucinol, and the PXDN knockdown impaired migration and adhesion of HUVECs. These results demonstrated that uric acid can affect extracellular matrix formation by competing for PXDN. The oxidation of uric acid by PXDN is likely a relevant mechanism in the endothelial dysfunction related to this metabolite.

Indexed as

collagen IVcrosslinkextracellular matrixHUVECoxidationperoxidasinuric acid

Identifiers

PMID35740014
PMCPMC9220231
OpenAlexW4281889019

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.