Evidence map›Paper›PMID 15909997›Full record

ArticleBiochemistry2005

Transglutaminase activity is present in highly purified nonsynaptosomal mouse brain and liver mitochondria.

Boris F Krasnikov, Soo-Youl Kim, Stephen J McConoughey, Hoon Ryu, Hui Xu, Irina Stavrovskaya, Siiri E Iismaa, Bryony M Mearns, Rajiv R Ratan, John P Blass and 2 more

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

16 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Transglutaminase 2: a molecular Swiss army knife.Biochimica et biophysica acta · 2012
    Review
  6. Article
  7. Article
  8. Physio-pathological roles of transglutaminase-catalyzed reactions.World journal of biological chemistry · 2010
    Article
  9. Measurement of cysteine S-conjugate β-lyase activity.Current protocols in toxicology · 2010
    Article
  10. Review
  11. Article
  12. Article
  13. Transglutaminases and neurodegeneration.Journal of neurochemistry · 2009
    Review
  14. Metabolism of the cysteine S-conjugate of busulfan involves a beta-lyase reaction.Drug metabolism and disposition: the biological fate of chemicals · 2008
    Article
  15. Article
  16. 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

12 authors at 3 institutions in 2 countries.

Boris F KrasnikovDepartment of Neurology and Neurosciences, and Medicine, Weill Medical College of Cornell University, New York City, New York 10021, USA.
Soo-Youl Kim
Stephen J McConoughey
Hoon Ryu
Hui Xu
Irina Stavrovskaya
Siiri E Iismaa
Bryony M Mearns
Rajiv R Ratan
John P Blass
Gary E Gibson
Arthur J L Cooper
Cornell University · USVictor Chang Cardiac Research Institute · AUBurke Medical Research Institute · US

Funding

TRANSCRIPTIONAL RESPONSES TO MITOCHONDRIAL DYSFUNCTIONP01AG014930 · NIA · WINIFRED MASTERSON BURKE MED RES INST · PI GIBSON, GARY E · 1999 to 2020
$30.7M
Zinc Regulation &Toxicity in Cellular Energy MetabolismR01NS038741 · NINDS · WINIFRED MASTERSON BURKE MED RES INST · PI BROWN, ABRAHAM M · 1999 to 2006
$1.9M
NIA NIH HHS P01 AG014930NIA NIH HHS P01 AG14930NINDS NIH HHS NS38741NINDS NIH HHS R01 NS038741
6 · The paper itself

Abstract

Several active transglutaminase (TGase) isoforms are known to be present in human and rodent tissues, at least three of which, namely, TGase 1, TGase 2 (tissue transglutaminase), and TGase 3, are present in the brain. TGase activity is known to be present in the cytosolic, nuclear, and extracellular compartments of the brain. Here, we show that highly purified mouse brain nonsynaptosomal mitochondria and mouse liver mitochondria and mitoplast fractions derived from these preparations possess TGase activity. Western blotting and experiments with TGase 2 knock-out (KO) mice ruled out the possibility that most of the mitochondrial/mitoplast TGase activity is due to TGase 2, the TGase isoform responsible for the majority of the activity ([14C]putrescine-binding assay) in whole brain and liver homogenates. The identity of the mitochondrial/mitoplast TGase(s) is not yet known. Possibly, the activity may be due to one of the other TGase isoforms or perhaps to a protein that does not belong to the classical TGase family. This activity may play a role in regulation of mitochondrial function both in normal physiology and in disease. Its nature and regulation deserve further study.

Indexed as

AnimalsBlotting, WesternBrainCadaverineCalciumCarbon RadioisotopesCaseinsCross ReactionsElectrophoresis, Polyacrylamide GelFluoresceinGTP-Binding ProteinsGuinea PigsImmune SeraMaleMiceMice, Inbred C57BLCadaverineCalciumCarbon RadioisotopesCaseinsFluoresceinGTP-Binding ProteinsImmune SeraN,N-dimethylcaseinProtein Glutamine gamma Glutamyltransferase 2PutrescineTransglutaminases

Identifiers

PMID15909997
PMCPMC2597021
OpenAlexW2015310598

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.