Evidence map›Paper›PMID 25377544›Full record

ArticleHistochemistry and cell biology2015

Immunolabeling of gamma-glutamyl transferase 5 in normal human tissues reveals that expression and localization differ from gamma-glutamyl transferase 1.

Marie H Hanigan, Elizabeth M Gillies, Stephanie Wickham, Nancy Wakeham, Celeste R Wirsig-Wiechmann

Abstract readComparative Study
In one paragraph

Article in Histochemistry and cell biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed, 2 pooled it
0.6field-weighted citation impact, top 34% 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

18 citing papers in PubMed, 2 syntheses or guidelines pooled it, 33 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Article
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  8. Identification ofFrontiers in genetics · 2022
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  14. Proximal TubuleThe Journal of pharmacology and experimental therapeutics · 2019
    Article
  15. Article
  16. Article
  17. Review
  18. GGT5 Is an Independent Prognostic Biomarker in Stomach Adenocarcinoma.Canadian journal of gastroenterology & hepatology
    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

5 authors at 1 institution in 1 country.

Marie H HaniganDepartment of Cell Biology, University of Oklahoma Health Sciences Center, BMSB 553, 940 S.L.Young Blvd, Oklahoma City, OK, 73104, USA, marie-hanigan@ouhsc.edu.
Elizabeth M Gillies
Stephanie Wickham
Nancy Wakeham
Celeste R Wirsig-Wiechmann
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

Gamma-glutamyl transferase (GGT5) was discovered due to its ability to convert leukotriene C4 (LTC4, a glutathione S-conjugate) to LTD4 and may have an important role in the immune system. However, it was not known which cells express the enzyme in humans. We have developed a sensitive and specific antibody that can be used to detect human GGT5 on Western blots and in fixed tissue sections. We localized GGT5 expression in normal human tissues. We observed GGT5 expressed by macrophages present in many tissues, including tissue-fixed macrophages such as Kupffer cells in the liver and dust cells in the lung. GGT5 was expressed in some of the same tissues that have been shown to express gamma-glutamyl transferase (GGT1), the only other enzymatically active protein in this family. But, the two enzymes were often expressed by different cell types within the tissue. For example, GGT5 was expressed by the interstitial cells of the kidney, whereas GGT1 is expressed on the apical surface of the renal proximal tubules. Other tissues with GGT5-positive cells included: adrenal gland, salivary gland, pituitary, thymus, spleen, liver, bone marrow, small intestine, stomach, testis, prostate and placenta. GGT5 and GGT1 are cell surface enzymes. The different pattern of expression results in their access to different extracellular fluids and therefore different substrates. GGT5 has access to substrates in blood and intercellular fluids, while GGT1 has access primarily to fluids in ducts and glands throughout the body. These data provide new insights into the different functions of these two related enzymes.

Indexed as

ImmunohistochemistryAnimalsAntibody SpecificityBlotting, Westerngamma-GlutamyltransferaseHumansIsoenzymesMiceNIH 3T3 CellsSubstrate SpecificityTissue Array AnalysisTransfectiongamma-Glutamyltransferasegamma-glutamyltransferase, humanIsoenzymes

Identifiers

PMID25377544
PMCPMC4393757
OpenAlexW2008605560

What OpenQuestion holds

Textmetadata
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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.