Evidence map›Paper›PMID 36662875›Full record

ArticlePloS one2023

The NLRP6 protein is very faintly expressed in several normal and cancerous epithelial cells and may be confused with an unrelated protein.

Abdallah Mound, Gautier Goormachtigh, Fabrice Bray, Stéphanie Flament, Christian Rolando, Richard Ruez, Nathalie Martin, Amélie Decourcelle, Vanessa Dehennaut, Jean-Michel Saliou and 2 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact, top 100% 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

1 citing paper in PubMed, 0 citations in OpenAlex.

  1. 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

12 authors at 2 institutions in 1 country.

Abdallah MoundUniv. Lille, CNRS, Inserm, CHU Lille, UMR9020-U1277-CANTHER-Cancer Heterogeneity Plasticity and Resistance to Therapies, Lille, France.
Gautier GoormachtighUniv. Lille, CNRS, Inserm, CHU Lille, UMR9020-U1277-CANTHER-Cancer Heterogeneity Plasticity and Resistance to Therapies, Lille, France.
Fabrice BrayUniv. Lille, CNRS, USR 3290-MSAP-Miniaturization for Synthesis, Analysis & Proteomics, Lille, France.
Stéphanie FlamentUniv. Lille, CNRS, USR 3290-MSAP-Miniaturization for Synthesis, Analysis & Proteomics, Lille, France.
Christian RolandoUniv. Lille, CNRS, USR 3290-MSAP-Miniaturization for Synthesis, Analysis & Proteomics, Lille, France.ORCID 0000-0002-3266-8860
Richard RuezUniv. Lille, Inserm, U1003 -PhyCell-Laboratoire de Physiologie Cellulaire, Lille, France.
Nathalie MartinUniv. Lille, CNRS, Inserm, CHU Lille, UMR9020-U1277-CANTHER-Cancer Heterogeneity Plasticity and Resistance to Therapies, Lille, France.
Amélie DecourcelleUniv. Lille, CNRS, Inserm, CHU Lille, UMR9020-U1277-CANTHER-Cancer Heterogeneity Plasticity and Resistance to Therapies, Lille, France.
Vanessa DehennautUniv. Lille, CNRS, Inserm, CHU Lille, UMR9020-U1277-CANTHER-Cancer Heterogeneity Plasticity and Resistance to Therapies, Lille, France.
Jean-Michel SaliouUniv. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, US 41 -UMS2014 -PLBS, Lille, France.
Mathias ChamaillardUniv. Lille, Inserm, U1003 -PhyCell-Laboratoire de Physiologie Cellulaire, Lille, France.
Corinne AbbadieUniv. Lille, CNRS, Inserm, CHU Lille, UMR9020-U1277-CANTHER-Cancer Heterogeneity Plasticity and Resistance to Therapies, Lille, France.ORCID 0000-0002-8174-2393
Centre National de la Recherche Scientifique · FRInserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nod-Like Receptor Pyrin domain-containing protein 6 (NLRP6), a member of the Nucleotide-oligomerization domain-Like Receptor (NLR) family of proteins, assembles together with the ASC protein to form an inflammasome upon stimulation by bacterial lipoteichoic acid and double-stranded DNA. Besides its expression in myeloid cells, NLRP6 is also expressed in intestinal epithelial cells where it may contribute to the maintenance of gut homeostasis and negatively controls colorectal tumorigenesis. Here, we report that NLRP6 is very faintly expressed in several colon cancer cell lines, detected only in cytoplasmic small dots were it colocalizes with ASC. Consequently, it is very hardly detected by standard western-blotting techniques by several presently available commercial antibodies which, in contrast, highly cross-react with a protein of 90kDa that we demonstrate to be unrelated to NLRP6. We report here these results to caution the community not to confuse the 90kDa protein with the endogenous human NLRP6.

Indexed as

InflammasomesNeoplasmsEpithelial CellsHomeostasisHumansIntracellular Signaling Peptides and ProteinsInflammasomesIntracellular Signaling Peptides and ProteinsNLRP6 protein, human

Identifiers

PMID36662875
PMCPMC9858803
OpenAlexW4317556158

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.