Evidence map›Paper›PMID 24563460›Full record

ArticleThe Journal of biological chemistry2014

Oxidation of endogenous N-arachidonoylserotonin by human cytochrome P450 2U1.

Michal Siller, Sandeep Goyal, Francis K Yoshimoto, Yi Xiao, Shouzou Wei, F Peter Guengerich

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed, 1 pooled it
7.3field-weighted citation impact, top 3% 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

12 citing papers in PubMed, 1 synthesis or guideline pooled it, 37 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. A Role for the Orphan Human Cytochrome P450 2S1 in Polyunsaturated Fatty AcidDrug metabolism and disposition: the biological fate of chemicals · 2019
    Article
  12. Cytochrome P450 2U1, a very peculiar member of the human P450s family.Cellular and molecular life sciences : CMLS · 2017
    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

6 authors at 2 institutions in 2 countries.

Michal SillerDepartment of Biochemistry and Center in Molecular Toxicology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146; Pharmacology and Toxicology Division, Institute of Molecular and Translational Medicine, Palacky University Olomouc, 775 15 Olomouc, Czech Republic.
Sandeep GoyalDepartment of Biochemistry and Center in Molecular Toxicology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146.
Francis K YoshimotoDepartment of Biochemistry and Center in Molecular Toxicology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146.
Yi XiaoDepartment of Biochemistry and Center in Molecular Toxicology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146.
Shouzou WeiDepartment of Biochemistry and Center in Molecular Toxicology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146.
F Peter GuengerichDepartment of Biochemistry and Center in Molecular Toxicology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146. Electronic address: f.guengerich@vanderbilt.edu.
Vanderbilt University · USInstitute of Molecular and Translational Medicine · CZ

Funding

Structural Biology Facility CoreP30ES000267 · NIEHS · VANDERBILT UNIVERSITY · PI GUENGERICH, F PETER · 1985 to 2014
$20.3M
TRAINING PROGRAM IN ENVIRONMENTAL TOXICOLOGYT32ES007028 · NIEHS · VANDERBILT UNIVERSITY · PI F PETER Guengerich, Fiona Edith Harrison · 1985 to 2026
$15.7M
Metabolism of Carcinogens and Drugs by Human P450sR37CA090426 · NCI · VANDERBILT UNIVERSITY · PI GUENGERICH, F PETER · 2006 to 2015
$3.6M
NCI NIH HHS R37 CA090426NIEHS NIH HHS P30 ES000267NIEHS NIH HHS T32 ES007028
6 · The paper itself

Abstract

Cytochrome P450 (P450) 2U1 has been shown to be expressed, at the mRNA level, in human thymus, brain, and several other tissues. Recombinant P450 2U1 was purified and used as a reagent in a metabolomic search for substrates in bovine brain. In addition to fatty acid oxidation reactions, an oxidation of endogenous N-arachidonoylserotonin was characterized. Subsequent NMR and mass spectrometry and chemical synthesis showed that the main product was the result of C-2 oxidation of the indole ring, in contrast to other human P450s that generated different products. N-Arachidonoylserotonin, first synthesized chemically and described as an inhibitor of fatty acid amide hydrolase, had previously been found in porcine and mouse intestine; we demonstrated its presence in bovine and human brain samples. The product (2-oxo) was 4-fold less active than N-arachidonoylserotonin in inhibiting fatty acid amide hydrolase. The rate of oxidation of N-arachidonoylserotonin was similar to that of arachidonic acid, one of the previously identified fatty acid substrates of P450 2U1. The demonstration of the oxidation of N-arachidonoylserotonin by P450 2U1 suggests a possible role in human brain and possibly other sites.

Indexed as

Amino Acid SequenceAnimalsArachidonic AcidsBrainCatalysisCattleChromatography, LiquidCytochrome P-450 Enzyme SystemCytochrome P450 Family 2ErythrocytesEscherichia coliGene Expression Regulation, EnzymologicHumansIndolesLiverMagnetic Resonance SpectroscopyArachidonic AcidsarachidonoylserotoninCYP2U1 protein, humanCytochrome P-450 Enzyme SystemCytochrome P450 Family 2IndolesOxygenSerotoninArachidonic AcidCytochrome P450EicosanoidLipid OxidationMass Spectrometry (MS)

Identifiers

PMID24563460
PMCPMC4036169
OpenAlexW1983702105

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.