Evidence map›Paper›PMID 19549781›Full record

ArticleThe Journal of biological chemistry2009

S-glutathionylation of the Rpn2 regulatory subunit inhibits 26 S proteasomal function.

Jaroslaw W Zmijewski, Sami Banerjee, Edward Abraham

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

41 citing papers in PubMed, 64 citations in OpenAlex.

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  11. Causative Links between Protein Aggregation and Oxidative Stress: A Review.International journal of molecular sciences · 2019
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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

3 authors at 1 institution in 1 country.

Jaroslaw W ZmijewskiDepartment of Medicine; Center for Free Radical Biology, University of Alabama, Birmingham, Alabama 35294.
Sami BanerjeeDepartment of Medicine.
Edward AbrahamDepartment of Medicine; Center for Free Radical Biology, University of Alabama, Birmingham, Alabama 35294.
University of Alabama at Birmingham · US

Funding

NEUTROPHIL ACTIVATION IN ACUTE LUNG INJURYR01HL062221 · NHLBI · UNIVERSITY OF COLORADO DENVER · PI ABRAHAM, EDWARD · 2000 to 2009
$2.9M
HMGB1 and neutrophil efferocytosis.R01GM087748 · NIGMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI ZMIJEWSKI, JAROSLAW WALDEMAR · 2009 to 2012
$1.2M
NHLBI NIH HHS HL62221NHLBI NIH HHS R01 HL062221NIGMS NIH HHS GM87748NIGMS NIH HHS R01 GM087748
6 · The paper itself

Abstract

Although increased intracellular concentrations of hydrogen peroxide (H2O2) are associated with inhibition of 26 S proteasomal activity, the mechanisms responsible for such effects have not been well delineated. In the present studies, we found that direct exposure of purified 26 S proteasomes to H2O2 had negligible effects on their activity, whereas incubation with glutathione and H2O2 produced >80% decrease in chymotrypsin-like and trypsin-like activities. Rpn1 and Rpn2, which are subunits of the 19 S regulatory particle, undergo S-glutathionylation after exposure of purified 26 S proteasomes to glutathione and H2O2, as well as in HEK 293 cells and neutrophils incubated with H2O2. Increased oxidation of Rpn1 and Rpn2 cysteine thiols was also found in lung extracts from mice in which catalase was inactivated, a condition associated with augmented intracellular concentrations of H2O2 and diminished 26 S proteasomal activity. Although unoxidized Rpn2 enhanced 20 S proteolytic function in vitro, such potentiation was not found when the 20 S core particle was incubated with oxidized Rpn2. The composition of 26 S proteasomes was not altered after exposure to glutathione and H2O2, with similar amounts of Rpn1 and Rpn2 in control or oxidized 26 S proteasomal complexes. These findings identify S-glutathionylation of Rpn2 as a contributory mechanism for H2O2-induced inhibition of 26 S proteasomal function.

Indexed as

AnimalsCell LineCysteineDose-Response Relationship, DrugGlutathioneHumansHydrogen PeroxideLungMembrane ProteinsMiceMice, Inbred C3HMice, Inbred C57BLModels, BiologicalProteasome Endopeptidase ComplexSulfhydryl CompoundsATP dependent 26S proteaseCysteineGlutathioneHydrogen PeroxideMembrane ProteinsProteasome Endopeptidase ComplexribophorinSulfhydryl Compounds

Identifiers

PMID19549781
PMCPMC2755946
OpenAlexW2008173040

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.