Evidence map›Paper›PMID 34389806›Full record

ArticleBritish journal of cancer2021

Peroxiredoxin-1 Tyr194 phosphorylation regulates LOX-dependent extracellular matrix remodelling in breast cancer.

Shireen Attaran, John J Skoko, Barbara L Hopkins, Megan K Wright, Laurel E Wood, Alparslan Asan, Hyun Ae Woo, Adam Feinberg, Carola A Neumann

Open access · greenAbstract read
In one paragraph

Article in British journal of cancer, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed, 1 pooled it
0.9field-weighted citation impact, top 27% 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

10 citing papers in PubMed, 1 synthesis or guideline pooled it, 18 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Review
  9. Article
  10. 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

9 authors at 4 institutions in 2 countries.

Shireen AttaranDepartment of Pharmacology & Chemical Biology, University of Pittsburgh, Pittsburgh, PA, USA.
John J SkokoDepartment of Pharmacology & Chemical Biology, University of Pittsburgh, Pittsburgh, PA, USA.
Barbara L HopkinsWomen's Cancer Research Center, UPMC Hillman Cancer Center, Pittsburgh, PA, USA.
Megan K WrightUniversity of Pittsburgh, School of Medicine, Pittsburgh, PA, USA.
Laurel E WoodDepartment of Pharmacology & Chemical Biology, University of Pittsburgh, Pittsburgh, PA, USA.
Alparslan AsanDepartment of Pharmacology & Chemical Biology, University of Pittsburgh, Pittsburgh, PA, USA.
Hyun Ae WooCollege of Pharmacy, Graduate School of Pharmaceutical Sciences, Ewha Womans University, Seoul, Republic of Korea.
Adam FeinbergDepartment of Materials Science and Engineering and Biomedical Engineering, Carnegie Mellon University, Pittsburgh, PA, USA.ORCID http://orcid.org/0000-0003-3338-5456
Carola A NeumannDepartment of Pharmacology & Chemical Biology, University of Pittsburgh, Pittsburgh, PA, USA. neumannc@upmc.edu.ORCID http://orcid.org/0000-0003-2801-9531
University of Pittsburgh · USCarnegie Mellon University · USEwha Womans University · KRUPMC Health System · US

Funding

VECTOR CORE FACILITYP30CA047904 · NCI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI Jessie Nedrow · 1988 to 2026
$158.0M
The Role of Peroxiredoxin1 & Reactive Oxygen Species in Breast Tumor InitiationR01CA131350 · NCI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI NEUMANN, CAROLA ANKE · 2010 to 2014
$1.5M
Inhibition of DNA double strand break repair in TNBC by nitro-fatty acidsR56CA233817 · NCI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI NEUMANN, CAROLA ANKE · 2019 to 2020
$687k
NCI NIH HHS P30 CA047904NCI NIH HHS R01 CA131350NCI NIH HHS R56 CA233817
6 · The paper itself

Abstract

backgroundPeroxiredoxin 1 (PRDX1) belongs to an abundant family of peroxidases whose role in cancer is still unresolved. While mouse knockout studies demonstrate a tumour suppressive role for PRDX1, in cancer cell xenografts, results denote PRDX1 as a drug target. Probably, this phenotypic discrepancy stems from distinct roles of PRDX1 in certain cell types or stages of tumour progression.

methodsWe demonstrate an important cell-autonomous function for PRDX1 utilising a syngeneic mouse model (BALB/c) and mammary fibroblasts (MFs) obtained from it.

resultsLoss of PRDX1 in vivo promotes collagen remodelling known to promote breast cancer progression. PRDX1 inactivation in MFs occurs via SRC-induced phosphorylation of PRDX1 TYR194 and not through the expected direct oxidation of CYS52 in PRDX1 by ROS. TYR194-phosphorylated PRDX1 fails to bind to lysyl oxidases (LOX) and leads to the accumulation of extracellular LOX proteins which supports enhanced collagen remodelling associated with breast cancer progression.

conclusionsThis study reveals a cell type-specific tumour suppressive role for PRDX1 that is supported by survival analyses, depending on PRDX1 protein levels in breast cancer cohorts.

Indexed as

AnimalsBreast NeoplasmsCell Line, TumorCollagenExtracellular MatrixFemaleGene Expression Regulation, NeoplasticHEK293 CellsHumansMicePeroxiredoxinsPhosphorylationPrognosisProtein-Lysine 6-OxidaseSurvival AnalysisTyrosineCollagenLOX protein, humanPeroxiredoxinsPRDX1 protein, humanProtein-Lysine 6-OxidaseTyrosine

Identifiers

PMID34389806
PMCPMC8505437
OpenAlexW3188782771

What OpenQuestion holds

Textmetadata
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.