Evidence map›Paper›PMID 20836986›Full record

ArticleArchives of biochemistry and biophysics2010

Glutathione transferase A4-4 resists adduction by 4-hydroxynonenal.

Laura M Shireman, Kimberly A Kripps, Larissa M Balogh, Kip P Conner, Dale Whittington, William M Atkins

Abstract read
In one paragraph

Article in Archives of biochemistry and biophysics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
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

13 citing papers in PubMed.

  1. Lipid Peroxidation-Related Redox Signaling in Osteosarcoma.International journal of molecular sciences · 2024
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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

6 authors.

Laura M ShiremanDepartment of Medicinal Chemistry, University of Washington, Seattle, 98195-7610, USA.
Kimberly A Kripps
Larissa M Balogh
Kip P Conner
Dale Whittington
William M Atkins

Funding

GRADUATE TRAINING IN CELLULAR &MOLECULAR PHARMACOLOGYT32GM007752 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BROWN, JOAN HELLER, HANDEL, TRACY M · 1985 to 2023
$13.5M
Pharmacological Sciences SupplementT32GM007750 · NIGMS · UNIVERSITY OF WASHINGTON · PI ATKINS, WILLIAM M · 1985 to 2023
$12.6M
Glutathione S-Transferases and Oxidative StressR01GM062284 · NIGMS · UNIVERSITY OF WASHINGTON · PI ATKINS, WILLIAM M · 2002 to 2011
$2.0M
NIGMS NIH HHS GM 62284NIGMS NIH HHS R01 GM062284NIGMS NIH HHS T32 GM007750NIGMS NIH HHS T32 GM007752NIGMS NIH HHS T32GM 07752
6 · The paper itself

Abstract

4-Hydroxy-2-trans-nonenal (HNE) is a lipid peroxidation product that contributes to the pathophysiology of several diseases with components of oxidative stress. The electrophilic nature of HNE results in covalent adduct formation with proteins, fatty acids and DNA. However, it remains unclear whether enzymes that metabolize HNE avoid inactivation by it. Glutathione transferase A4-4 (GST A4-4) plays a significant role in the elimination of HNE by conjugating it with glutathione (GSH), with catalytic activity toward HNE that is dramatically higher than the homologous GST A1-1 or distantly related GSTs. To determine whether enzymes that metabolize HNE resist its covalent adduction, the rates of adduction of these GST isoforms were compared and the functional effects of adduction on catalytic properties were determined. Although GST A4-4 and GST A1-1 have striking structural similarity, GST A4-4 was insensitive to adduction by HNE under conditions that yield modest adduction of GST A1-1 and extensive adduction of GST P1-1. Furthermore, adduction of GST P1-1 by HNE eliminated its activity toward the substrates 1-chloro-2,4-dinitrobenzene (CDNB) and toward HNE itself. HNE effects on GST A4-4 and A1-1 were less significant. The results indicate that enzymes that metabolize HNE may have evolved structurally to resist covalent adduction by it.

Indexed as

AldehydesCatalysisCrystallography, X-RayDinitrochlorobenzeneGlutathione S-Transferase piGlutathione TransferaseIsoenzymesKineticsModels, MolecularProtein Conformation4-hydroxy-2-nonenalAldehydesDinitrochlorobenzeneglutathione S-transferase alphaGlutathione S-Transferase piGlutathione TransferaseIsoenzymesleukotriene-C4 synthase

Identifiers

PMID20836986
PMCPMC2972508

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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.