Evidence map›Paper›PMID 24974180›Full record

ReviewAdvances in cancer research2014

Gamma-glutamyl transpeptidase: redox regulation and drug resistance.

Marie H Hanigan

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Advances in cancer research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 160 papers, 4 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
160citing papers in PubMed, 4 pooled it
110.0field-weighted citation impact, top 1% 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

160 citing papers in PubMed, 4 syntheses or guidelines pooled it, 267 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Pooled it
  4. Pooled it
  5. Trial
  6. Trial
  7. Hyperpolarized γ-Glutamyl-[1-Molecular imaging and biology · 2026
    Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

100 more citing papers are in PubMed but not listed here.

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

1 author at 1 institution in 1 country.

Marie H HaniganDepartment of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma, USA. Electronic address: marie-hanigan@ouhsc.edu.
University of Oklahoma Health Sciences Center · US

Funding

Structure-Function Studies of MsvR, a Methanogen-Specific Transcriptional RegulaP20GM103640 · NIGMS · UNIVERSITY OF OKLAHOMA · PI MOOERS, BLAINE H. M. · 2012 to 2021
$20.4M
NIGMS NIH HHS P20 GM103640NIGMS NIH HHS P20GM103640
6 · The paper itself

Abstract

The expression of gamma-glutamyl transpeptidase (GGT) is essential to maintaining cysteine levels in the body. GGT is a cell surface enzyme that hydrolyzes the gamma-glutamyl bond of extracellular reduced and oxidized glutathione, initiating their cleavage into glutamate, cysteine (cystine), and glycine. GGT is normally expressed on the apical surface of ducts and glands, salvaging the amino acids from glutathione in the ductal fluids. GGT in tumors is expressed over the entire cell membrane and provides tumors with access to additional cysteine and cystine from reduced and oxidized glutathione in the blood and interstitial fluid. Cysteine is rate-limiting for glutathione synthesis in cells under oxidative stress. The induction of GGT is observed in tumors with elevated levels of intracellular glutathione. Studies in models of hepatocarcinogenesis show that GGT expression in foci of preneoplastic hepatocytes provides a selective advantage to the cells during tumor promotion with agents that deplete intracellular glutathione. Similarly, expression of GGT in tumors enables cells to maintain elevated levels of intracellular glutathione and to rapidly replenish glutathione during treatment with prooxidant anticancer therapy. In the clinic, the expression of GGT in tumors is correlated with drug resistance. The inhibitors of GGT block GGT-positive tumors from accessing the cysteine in extracellular glutathione. They also inhibit GGT activity in the kidney, which results in the excretion of GSH in the urine and a rapid decrease in blood cysteine levels, leading to depletion of intracellular GSH in both GGT-positive and GGT-negative tumors. GGT inhibitors are being developed for clinical use to sensitize tumors to chemotherapy.

Indexed as

Drug Resistance, NeoplasmGene Expression Regulation, EnzymologicOxidation-ReductionAnimalsCatalysisCystinegamma-GlutamyltransferaseGene Expression Regulation, NeoplasticGlutathioneHumansMiceNeoplasmsOxidantsOxygenRatsCystinegamma-GlutamyltransferaseGlutathioneOxidantsOxygenCysteineGamma-glutamyl transferaseGamma-glutamyl transpeptidaseGlutathione

Identifiers

PMID24974180
PMCPMC4388159
OpenAlexW183752289

What OpenQuestion holds

Textmetadata
LicenceTDM
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.