Evidence map›Paper›PMID 26984580›Full record

ArticleAntioxidants & redox signaling2016

Protein S-Glutathionylation Mediates Macrophage Responses to Metabolic Cues from the Extracellular Environment.

Sarah L Ullevig, Hong Seok Kim, John D Short, Sina Tavakoli, Susan T Weintraub, Kevin Downs, Reto Asmis

Abstract read
In one paragraph

Article in Antioxidants & redox signaling, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

20 citing papers in PubMed, 48 citations in OpenAlex.

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  9. An investigation into the impact of deleting one copy of theRedox report : communications in free radical research · 2020
    Article
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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.

Sarah L Ullevig1 Department of Kinesiology, Health, and Nutrition, University of Texas at San Antonio , San Antonio, Texas.
Hong Seok Kim2 Department of Molecular Medicine, College of Medicine, Inha University , Incheon, Korea.
John D Short3 Department of Pharmacology, University of Texas Health Science Center at San Antonio , San Antonio, Texas.
Sina Tavakoli4 Department of Radiology, University of Texas Health Science Center at San Antonio , San Antonio, Texas.
Susan T Weintraub5 Institutional Mass Spectrometry Core Laboratory, University of Texas Health Science Center at San Antonio , San Antonio, Texas.
Kevin Downs7 Department of Cellular and Structural Biology, University of Texas Health Science Center at San Antonio , San Antonio, Texas.
Reto Asmis4 Department of Radiology, University of Texas Health Science Center at San Antonio , San Antonio, Texas.
The University of Texas Health Science Center at San Antonio · USInha University · KRThe University of Texas at San Antonio · US

Funding

RCMI Center for Interdiscplinary Health Research CIHRG12MD007591 · NIMHD · UNIVERSITY OF TEXAS SAN ANTONIO · PI PERRY, GEORGE · 2012 to 2016
$10.4M
Triple Quadrupole Mass Spectrometer for Metabolomics AnalysisS10RR031586 · NCRR · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI WEINTRAUB, SUSAN T · 2011 to 2011
$446k
NCRR NIH HHS S10 RR031586NIMHD NIH HHS G12 MD007591
6 · The paper itself

Abstract

aimsProtein S-glutathionylation, the formation of a mixed disulfide between glutathione and protein thiols, is an oxidative modification that has emerged as a new signaling paradigm, potentially linking oxidative stress to chronic inflammation associated with heart disease, diabetes, cancer, lung disease, and aging. Using a novel, highly sensitive, and selective proteomic approach to identify S-glutathionylated proteins, we tested the hypothesis that monocytes and macrophages sense changes in their microenvironment and respond to metabolic stress by altering their protein thiol S-glutathionylation status.

resultsWe identified over 130 S-glutathionylated proteins, which were associated with a variety of cellular functions, including metabolism, transcription and translation, protein folding, free radical scavenging, cell motility, and cell death. Over 90% of S-glutathionylated proteins identified in metabolically stressed THP-1 monocytes were also found in hydrogen peroxide (H INNOVATION: We provide a novel mechanistic link between metabolic (and thiol oxidative) stress, macrophage dysfunction, and chronic inflammatory diseases associated with metabolic disorders.

conclusionOur data support the concept that changes in the extracellular metabolic microenvironment induce S-glutathionylation of proteins central to macrophage metabolism and a wide array of cellular signaling pathways and functions, which in turn initiate and promote functional and phenotypic changes in macrophages. Antioxid. Redox Signal. 25, 836-851.

Indexed as

CuesProtein Processing, Post-TranslationalAnimalsAtherosclerosisBiomarkersCell LineComputational BiologyExtracellular SpaceFemaleGene ExpressionGlutathioneHumansHydrogen PeroxideMacrophagesMacrophages, PeritonealMaleBiomarkersGlutathioneHydrogen PeroxideatherosclerosismacrophageproteomicsS-glutathionylationthiols

Identifiers

PMID26984580
PMCPMC5107721
OpenAlexW2399927448

What Socratic 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 Socratic graph.