Evidence map›Paper›PMID 11737866›Full record

ArticleBMC pharmacology2001

Minipig cytochrome P450 3A, 2A and 2C enzymes have similar properties to human analogs.

P Soucek, R Zuber, E Anzenbacherová, P Anzenbacher, F P Guengerich

Open access · bronzeAbstract read
In one paragraph

Article in BMC pharmacology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

20 citing papers in PubMed, 105 citations in OpenAlex.

  1. Article
  2. Article
  3. Large Animal Models of Breast Cancer.Frontiers in oncology · 2022
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  7. Review
  8. Article
  9. Porcine cytochrome 2A19 and 2E1.Basic & clinical pharmacology & toxicology · 2019
    Review
  10. Review
  11. Article
  12. Cannabidiol Does Not Convert to ΔCannabis and cannabinoid research · 2017
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Ontogeny of drug elimination by the human kidney.Pediatric nephrology (Berlin, Germany) · 2006
    Review
  18. Article
  19. Review
  20. Cytochromes P450 and experimental models of drug metabolism.Journal of cellular and molecular medicine
    Review
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 3 institutions in 2 countries.

P SoucekGroup of Biotransformations, Center for Occupational Diseases, National Institute of Public Health, Srobarova 48, Praha 10, 100 42, Czech Republic. psoucek@szu.cz
R Zuber
E Anzenbacherová
P Anzenbacher
F P Guengerich
Palacký University Olomouc · CZNational Institute of Public Health · CZVanderbilt University Medical Center · US

Funding

Structural Biology Facility CoreP30ES000267 · NIEHS · VANDERBILT UNIVERSITY · PI GUENGERICH, F PETER · 1985 to 2014
$20.3M
ENZYMIC ACTIVATION OF CHEMICAL CARCINOGENSR35CA044353 · NCI · VANDERBILT UNIVERSITY · PI GUENGERICH, F PETER · 1987 to 2000
$974k
NCI NIH HHS R35 CA44353NIEHS NIH HHS P0I ES00267NIEHS NIH HHS P30 ES000267
6 · The paper itself

Abstract

backgroundThe search for an optimal experimental model in pharmacology is recently focused on (mini)pigs as they seem not only to be an alternative source of cells and tissues for xenotherapy but also an alternative species for studies on drug metabolism in man due to similarities between (mini) pig and human drug metabolizing systems. The purpose of this work is to characterize minipig liver microsomal cytochromes P450 (CYPs) by comparing their N-terminal sequences with corresponding human orthologs.

resultsThe microsomal CYPs exhibit similar activities to their human orthologous enzymes (CYP3A4, nifedipine oxidation; 2A6, coumarin 7-hydroxylation; 2D6, bufuralol 1'-hydroxylation; 2E1, p-nitrophenol hydroxylation; and 2C9, tolbutamide hydroxylation). Specific minipig CYP (2A, 2C and 3A) enzymes were partially purified and proteins identified by immunostaining (using antibodies against the respective human CYPs) were used for N-terminal amino acid sequencing. From comparisons, it can be concluded that the sequence of the first 20 amino acids at the N-terminus of minipig CYP2A is highly similar to human CYP2A6 (70% identity). The N-terminal sequence of CYP2C shared about 50% similarity with human 2C9. The results on the minipig liver microsomal CYP3A yielded identical data with those obtained for amino acid sequences of the pig CYP3A29 showing 60% identity with human CYP3A4.

conclusionsThus, our results further support the view that minipigs may serve as model animals in pharmacological/toxicological studies with substrates of human CYP enzymes, namely, of the CYP3A and CYP2A forms.

Indexed as

AnimalsAryl Hydrocarbon HydroxylasesCytochrome P-450 CYP3ACytochrome P-450 Enzyme SystemHumansMicrosomes, LiverSequence Analysis, ProteinSpecies SpecificitySteroid HydroxylasesSubstrate SpecificitySwine, MiniatureAryl Hydrocarbon HydroxylasesCYP3A4 protein, humanCYP3A protein, humancytochrome P-450 CYP2C subfamilyCytochrome P-450 CYP3ACytochrome P-450 Enzyme Systemsteroid hormone 7-alpha-hydroxylaseSteroid Hydroxylases

Identifiers

PMID11737866
PMCPMC60991
OpenAlexW2123063654

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.