Evidence map›Paper›PMID 12020353›Full record

ArticleThe Biochemical journal2002

Multiple isoforms of mitochondrial glutathione S-transferases and their differential induction under oxidative stress.

Haider Raza, Marie-Anne Robin, Ji-Kang Fang, Narayan G Avadhani

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

56 citing papers in PubMed, 169 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Insufficient fumarase contributes to hypertension by an imbalance of redox metabolism in Dahl salt-sensitive rats.Hypertension research : official journal of the Japanese Society of Hypertension · 2019
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article
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

4 authors at 1 institution in 1 country.

Haider RazaDepartment of Animal Biology and the Mari Lowe Center for Comparative Oncology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, PA 19104-6047, U.S.A.
Marie-Anne Robin
Ji-Kang Fang
Narayan G Avadhani
University of Pennsylvania · US

Funding

Role of Mitochondria-Targeted CYP2D6 in Chemical ToxicityR01GM034883 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI AVADHANI, NARAYAN G · 1985 to 2018
$6.1M
NIGMS NIH HHS GM34883-17
6 · The paper itself

Abstract

The mitochondrial respiratory chain, which consumes approx. 85-90% of the oxygen utilized by cells, is a major source of reactive oxygen species (ROS). Mitochondrial genetic and biosynthetic systems are highly susceptible to ROS toxicity. Intramitochondrial glutathione (GSH) is a major defence against ROS. In the present study, we have investigated the nature of the glutathione S-transferase (GST) pool in mouse liver mitochondria, and have purified three distinct forms of GST: GSTA1-1 and GSTA4-4 of the Alpha family, and GSTM1-1 belonging to the Mu family. The mitochondrial localization of these multiple GSTs was confirmed using a combination of immunoblot analysis, protease protection assay, enzyme activity, N-terminal amino acid sequencing, peptide mapping and confocal immunofluorescence analysis. Additionally, exogenously added 4-hydroxynonenal (HNE), a reactive byproduct of lipid peroxidation, to COS cells differentially affected the cytosolic and mitochondrial GSH pools in a dose- and time-dependent manner. Our results show that HNE-mediated mitochondrial oxidative stress caused a decrease in the GSH pool, increased membrane lipid peroxidation, and increased levels of GSTs, glutathione peroxidase and Hsp70 (heat-shock protein 70). The HNE-induced oxidative stress persisted for longer in the mitochondrial compartment, where the recovery of GSH pool was slower than in the cytosolic compartment. Our study, for the first time, demonstrates the presence in mitochondria of multiple forms of GSTs that show molecular properties similar to those of their cytosolic counterparts. Our results suggest that mitochondrial GSTs may play an important role in defence against chemical and oxidative stress.

Indexed as

Oxidative StressAldehydesAmino Acid SequenceAnimalsCOS CellsCytosolEnzyme ActivationGlutathione TransferaseHSP70 Heat-Shock ProteinsLipid PeroxidationMaleMiceMice, Inbred ICRMicroscopy, ConfocalMicroscopy, FluorescenceMitochondria4-hydroxy-2-nonenalAldehydesGlutathione TransferaseHSP70 Heat-Shock ProteinsProtein IsoformsReactive Oxygen Species

Identifiers

PMID12020353
PMCPMC1222767
OpenAlexW2073746174

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.