Evidence map›Paper›PMID 32372066›Full record

ArticleScientific reports2020

Human arylamine N-acetyltransferase 2 genotype-dependent protein expression in cryopreserved human hepatocytes.

Raúl A Salazar-González, Mark A Doll, David W Hein

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 24% 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

15 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Precision Medicine Strategies to Improve Isoniazid Therapy in Patients with Tuberculosis.European journal of drug metabolism and pharmacokinetics · 2024
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. HumanFrontiers in pharmacology · 2022
    Article
  14. ArylamineFrontiers in pharmacology · 2022
    Article
  15. 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

3 authors at 1 institution in 1 country.

Raúl A Salazar-GonzálezDepartment of Pharmacology & Toxicology and James Graham Brown Cancer Center, University of Louisville School of Medicine, Louisville, Kentucky, 40202, USA.
Mark A DollDepartment of Pharmacology & Toxicology and James Graham Brown Cancer Center, University of Louisville School of Medicine, Louisville, Kentucky, 40202, USA.
David W HeinDepartment of Pharmacology & Toxicology and James Graham Brown Cancer Center, University of Louisville School of Medicine, Louisville, Kentucky, 40202, USA. david.hein@louisville.edu.
University of Louisville · US

Funding

Role of oxidized linoleic acid metabolites in the pathogenesis of alcoholic liver diseaseP20GM113226 · NIGMS · UNIVERSITY OF LOUISVILLE · PI MCCLAIN, CRAIG J. · 2016 to 2025
$24.1M
The Role of Nutrition in the Development/Progression of Alcohol-Induced Organ InjuryP50AA024337 · NIAAA · UNIVERSITY OF LOUISVILLE · PI CRAIG J. MCCLAIN · 2016 to 2026
$17.9M
NIAAA NIH HHS P50 AA024337NIGMS NIH HHS P20 GM113226
6 · The paper itself

Abstract

Human N-acetyltransferases (NAT; EC 2.3.1.5) catalyze the N-acetylation of arylamine and hydrazine drugs and the O-acetylation of N-hydroxylated metabolites of aromatic and heterocyclic amines. Two different isoforms of this protein, N-acetyltransferase 1 (NAT1) and N-acetyltransferase 2 (NAT2), are expressed in human hepatocytes. Both are encoded by a single 870-bp open reading frame that exhibits genetic polymorphisms in human populations. NAT1 and NAT2 share more than 85% gene and protein sequence, making it challenging to produce antibodies with high specificity for NAT1 or NAT2. In the present study, we compared methods for the quantification of immunoreactive NAT1 and NAT2 with seven different antibodies and investigated the relationship of NAT2 genotype to NAT2 mRNA and protein expression in cryopreserved human hepatocytes. Sulfamethazine (NAT2-selective substrate) and NAT2 protein expression differed significantly with NAT2 acetylator genotype (p < 0.0001). NAT2 protein expression and sulfamethazine NAT2 catalytic activity correlated highly across the cryopreserved human hepatocytes of rapid, intermediate, and slow acetylator NAT2 genotypes. In conclusion, our data describe a specific analytical method for the quantification of NAT1 and NAT2 protein expression. We showed that the NAT2 activity in human hepatocytes is directly correlated to expression levels of NAT2 protein but not mRNA.

Indexed as

CryopreservationGene ExpressionGenotypeArylamine N-AcetyltransferaseCells, CulturedEnzyme ActivationHepatocytesHumansIsoenzymesPolymorphism, Single NucleotideRNA, MessengerArylamine N-AcetyltransferaseIsoenzymesN-acetyltransferase 1NAT2 protein, humanRNA, Messenger

Identifiers

PMID32372066
PMCPMC7200704
OpenAlexW3023931426

What OpenQuestion holds

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LicenceCC BY
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.