Evidence map›Paper›PMID 31485755›Full record

ArticleInflammation research : official journal of the European Histamine Research Society ... [et al.]2019

Regulation of oxidized LDL-induced inflammatory process through NLRP3 inflammasome activation by the deubiquitinating enzyme BRCC36.

Mohit Singh, Bhawna Kumari, Umesh C S Yadav

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Article in Inflammation research : official journal of the European Histamine Research Society ... [et al.], 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

15 citing papers in PubMed, 42 citations in OpenAlex.

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  13. Deubiquitinases: Modulators of Different Types of Regulated Cell Death.International journal of molecular sciences · 2021
    Review
  14. Article
  15. Crosstalk between ER stress, NLRP3 inflammasome, and inflammation.Applied microbiology and biotechnology · 2020
    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

3 authors at 1 institution in 1 country.

Mohit SinghMetabolic Disorders and Inflammatory Pathologies Laboratory, School of Life Sciences, Central University of Gujarat, Sector-30, Gandhinagar, 382030, Gujarat, India.
Bhawna KumariMetabolic Disorders and Inflammatory Pathologies Laboratory, School of Life Sciences, Central University of Gujarat, Sector-30, Gandhinagar, 382030, Gujarat, India.
Umesh C S YadavMetabolic Disorders and Inflammatory Pathologies Laboratory, School of Life Sciences, Central University of Gujarat, Sector-30, Gandhinagar, 382030, Gujarat, India. umeshyadav@cug.ac.in.
Central University of Gujarat · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

objectiveOxidized Low-Density Lipoprotein (oxLDL) is a well-established pro-inflammatory marker that activates the NLRP3 inflammasome. Ubiquitination plays an important role in modulating the stability and functions of various proteins. BRCC36 is a ubiquitin-modifying enzyme that plays a crucial role in protein stabilization and activation in the cytosol, but its role in OxLDL-induced NLRP3 inflammasome activation is not known. Here, we have investigated the role of deubiquitinating enzyme BRCC36 in regulating NLRP3 inflammasome during oxLDL stimulation.

methodsRaw 264.7 murine macrophages were stimulated with oxLDL and effect of BRCC36 deubiquitination activity was assessed by fluorometric assay, and protein expression was assessed by Western blotting. The level of IL-1β measured by ELISA and LDH activity as pyroptotic cell death marker was assessed by fluorometric assay.

resultsThe results showed that oxLDL increased the level of NLRP3 in macrophages and also the level of active caspase-1 and IL-1β. It also modulated the expression of deubiquitinating enzymes and caused pyroptotic cell death as indicated by LDH release. Inhibiting the proteasomal activity by MG132 and siRNA-mediated silencing of BRCC36 in macrophages potentially suppressed oxLDL-induced NLRP3 inflammasome activation and IL-1β secretion. Furthermore, the inhibition of proteasomal deubiquitinating activity with specific BRCC36 inhibitor G5 also reduced the inflammatory cell death.

conclusionTaken together, our study suggests that deubiquitinating enzyme BRCC36 inhibition could potentially suppress oxLDL-induced inflammatory process by inhibiting NLRP3 activation and resultant IL-1β secretion.

Indexed as

AnimalsDeubiquitinating EnzymesInflammasomesInflammationInterleukin-1betaLipoproteins, LDLMiceNLR Family, Pyrin Domain-Containing 3 ProteinPyroptosisRAW 264.7 CellsReactive Oxygen SpeciesBRCC3 protein, mouseDeubiquitinating EnzymesIL1B protein, mouseInflammasomesInterleukin-1betaLipoproteins, LDLNLR Family, Pyrin Domain-Containing 3 ProteinNlrp3 protein, mouseoxidized low density lipoproteinReactive Oxygen SpeciesBRCC36DeubiquitinationInflammationNLRP3 inflammasomeoxLDLRaw264.7 macrophages

Identifiers

PMID31485755
OpenAlexW2971681827

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Registered trials

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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.