Evidence map›Paper›PMID 28516247›Full record

ArticleArchives of toxicology2017

Genetic heterogeneity among slow acetylator N-acetyltransferase 2 phenotypes in cryopreserved human hepatocytes.

Mark A Doll, David W Hein

Abstract read
In one paragraph

Article in Archives of toxicology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-weighted citation impact, top 25% 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

14 citing papers in PubMed, 25 citations in OpenAlex.

  1. Research (Washington, D.C.) · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. HumanFrontiers in pharmacology · 2022
    Article
  7. Article
  8. Case Study 10: A Case to Investigate Acetyl Transferase Kinetics.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Drug metabolism and disposition: the biological fate of chemicals · 2017
    Article
  14. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Mark A DollDepartment of Pharmacology and Toxicology and James Graham Brown Cancer Center, University of Louisville Health Sciences Center, Kosair Charities CTR, 505 South Hancock Street, Louisville, KY, 40202, USA.
David W HeinDepartment of Pharmacology and Toxicology and James Graham Brown Cancer Center, University of Louisville Health Sciences Center, Kosair Charities CTR, 505 South Hancock Street, Louisville, KY, 40202, USA. d.hein@louisville.edu.ORCID http://orcid.org/0000-0003-3261-9775
University of Louisville · US

Funding

Role of oxidized linoleic acid metabolites in the pathogenesis of alcoholic liver diseaseP20GM113226 · NIGMS · UNIVERSITY OF LOUISVILLE · PI GHARE, SMITA S · 2016 to 2025
$24.1M
University of Louisville Cancer Education ProgramR25CA134283 · NCI · UNIVERSITY OF LOUISVILLE · PI HEIN, DAVID W, KIDD, LA CREIS RENEE · 2011 to 2022
$3.1M
NCI NIH HHS R25 CA134283NIGMS NIH HHS P20 GM113226
6 · The paper itself

Abstract

Genetic polymorphisms in human N-acetyltransferase 2 (NAT2) modify the metabolism of numerous drugs and carcinogens. These genetic polymorphisms modify both drug efficacy and toxicity and cancer risk associated with carcinogen exposure. Previous studies have suggested phenotypic heterogeneity among different NAT2 slow acetylator genotypes. NAT2 phenotype was investigated in vitro and in situ in samples of human hepatocytes obtained from various NAT2 slow and intermediate NAT2 acetylator genotypes. NAT2 gene dose response (NAT2*5B/*5B > NAT2*5B/*6A > NAT2*6A/*6A) was observed towards the N-acetylation of the NAT2-specific drug sulfamethazine by human hepatocytes both in vitro and in situ. N-acetylation of 4-aminobiphenyl, an arylamine carcinogen substrate for both N-acetyltransferase 1 and NAT2, showed the same trend both in vitro and in situ although the differences were not significant (p > 0.05). The N-acetylation of the N-acetyltransferase 1-specific substrate p-aminobenzoic acid did not follow this trend. In comparisons of NAT2 intermediate acetylator genotypes, differences in N-acetylation between NAT2*4/*5B and NAT2*4/*6B hepatocytes were not observed in vitro or in situ towards any of these substrates. These results further support phenotypic heterogeneity among NAT2 slow acetylator genotypes, consistent with differential risks of drug failure or toxicity and cancer associated with carcinogen exposure.

Indexed as

Genetic Heterogeneity4-Aminobenzoic AcidAminobiphenyl CompoundsArylamine N-AcetyltransferaseCells, CulturedCryopreservationHaplotypesHepatocytesHumansSulfamethazine4-Aminobenzoic Acid4-biphenylamineAminobiphenyl CompoundsArylamine N-AcetyltransferaseNAT2 protein, humanSulfamethazine4-AminobiphenylHuman hepatocytesN-acetyltransferase 2Slow acetylator genotypeSulfamethazine

Identifiers

PMID28516247
PMCPMC5713641
OpenAlexW2615279325

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Registered trials

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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.