Evidence map›Paper›PMID 30760703›Full record

ArticleCell death & disease2019

Subverted regulation of Nox1 NADPH oxidase-dependent oxidant generation by protein disulfide isomerase A1 in colon carcinoma cells with overactivated KRas.

Tiphany Coralie De Bessa, Alessandra Pagano, Ana Iochabel Soares Moretti, Percillia Victoria Santos Oliveira, Samir Andrade Mendonça, Herve Kovacic, Francisco Rafael Martins Laurindo

Open access · goldAbstract read
In one paragraph

Article in Cell death & disease, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.6field-weighted citation impact, top 20% 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

12 citing papers in PubMed, 24 citations in OpenAlex.

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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

7 authors at 3 institutions in 2 countries.

Tiphany Coralie De BessaLIM 64, Instituto do Coracao (InCor), Hospital das Clinicas HCFMUSP, Faculdade de Medicina, Universidade de Sao Paulo, Sao Paulo, SP, Brazil.ORCID http://orcid.org/0000-0002-5771-259X
Alessandra PaganoAix Marseille Univ, CNRS, UMR 7051, INP, Inst Neurophysiopathol, Faculté de Pharmacie, 27, Boulevard Jean Moulin - 13385 Marseille CEDEX 5-France, Marseille, France.
Ana Iochabel Soares MorettiLIM 64, Instituto do Coracao (InCor), Hospital das Clinicas HCFMUSP, Faculdade de Medicina, Universidade de Sao Paulo, Sao Paulo, SP, Brazil.ORCID http://orcid.org/0000-0003-3402-5778
Percillia Victoria Santos OliveiraLIM 64, Instituto do Coracao (InCor), Hospital das Clinicas HCFMUSP, Faculdade de Medicina, Universidade de Sao Paulo, Sao Paulo, SP, Brazil.
Samir Andrade MendonçaCentro de Investigação Translacional em Oncologia do Instituto do Câncer do Estado de São Paulo (Icesp), Faculdade de Medicina, Universidade de Sao Paulo, Sao Paulo, SP, Brazil.
Herve KovacicAix Marseille Univ, CNRS, UMR 7051, INP, Inst Neurophysiopathol, Faculté de Pharmacie, 27, Boulevard Jean Moulin - 13385 Marseille CEDEX 5-France, Marseille, France. herve.kovacic@univ-amu.fr.
Francisco Rafael Martins LaurindoLIM 64, Instituto do Coracao (InCor), Hospital das Clinicas HCFMUSP, Faculdade de Medicina, Universidade de Sao Paulo, Sao Paulo, SP, Brazil. francisco.laurindo@incor.usp.br.
Centre National de la Recherche Scientifique · FRHospital das Clínicas da Faculdade de Medicina da Universidade de São Paulo · BRUniversidade de São Paulo · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein disulfide isomerases including PDIA1 are implicated in cancer progression, but underlying mechanisms are unclear. PDIA1 is known to support vascular Nox1 NADPH oxidase expression/activation. Since deregulated reactive oxygen species (ROS) production underlies tumor growth, we proposed that PDIA1 is an upstream regulator of tumor-associated ROS. We focused on colorectal cancer (CRC) with distinct KRas activation levels. Analysis of RNAseq databanks and direct validation indicated enhanced PDIA1 expression in CRC with constitutive high (HCT116) vs. moderate (HKE3) and basal (Caco2) Ras activity. PDIA1 supported Nox1-dependent superoxide production in CRC; however, we first reported a dual effect correlated with Ras-level activity: in Caco2 and HKE3 cells, loss-of-function experiments indicate that PDIA1 sustains Nox1-dependent superoxide production, while in HCT116 cells PDIA1 restricted superoxide production, a behavior associated with increased Rac1 expression/activity. Transfection of Rac1

Indexed as

Caco-2 CellsCell MovementCell ProliferationColonic NeoplasmsGlycogen Synthase Kinase 3 betaHCT116 CellsHumansNADPH Oxidase 1Procollagen-Proline DioxygenaseProtein Disulfide-IsomerasesProto-Oncogene Proteins p21(ras)rac1 GTP-Binding ProteinReactive Oxygen SpeciesSignal TransductionSTAT3 Transcription FactorTransfectionGlycogen Synthase Kinase 3 betaGSK3B protein, humanKRAS protein, humanNADPH Oxidase 1NOX1 protein, humanP4HB protein, humanProcollagen-Proline DioxygenaseProtein Disulfide-IsomerasesProto-Oncogene Proteins p21(ras)rac1 GTP-Binding ProteinRAC1 protein, humanReactive Oxygen SpeciesSTAT3 protein, humanSTAT3 Transcription Factor

Identifiers

PMID30760703
PMCPMC6374413
OpenAlexW2913806382

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.