Evidence map›Paper›PMID 23963955›Full record

ArticleDrug metabolism and disposition: the biological fate of chemicals2013

Relationship between CYP1A2 localization and lipid microdomain formation as a function of lipid composition.

Lauren M Brignac-Huber, James R Reed, Marilyn K Eyer, Wayne L Backes

Open access · bronzeAbstract read
In one paragraph

Article in Drug metabolism and disposition: the biological fate of chemicals, 2013. 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
1.0field-weighted citation impact, top 23% 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, 23 citations in OpenAlex.

  1. Article
  2. Article
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  5. Article
  6. Human Liver Microsomes Immobilized on Magnetizable Beads: A Novel Approach to Study In Vitro Drug Metabolism.Drug metabolism and disposition: the biological fate of chemicals · 2020
    Article
  7. Preparation of Lipid Nanodiscs with Lipid Mixtures.Current protocols in protein science · 2019
    Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Cytochrome P450 Organization and Function Are Modulated by Endoplasmic Reticulum Phospholipid Heterogeneity.Drug metabolism and disposition: the biological fate of chemicals · 2016
    Review
  13. Article
  14. The Role of Protein-Protein and Protein-Membrane Interactions on P450 Function.Drug metabolism and disposition: the biological fate of chemicals · 2016
    Review
  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

4 authors at 1 institution in 1 country.

Lauren M Brignac-HuberDepartment of Pharmacology and Experimental Therapeutics, Stanley S. Scott Cancer Center, Louisiana State University Health Science Center, New Orleans, Louisiana.
James R Reed
Marilyn K Eyer
Wayne L Backes
Louisiana State University Health Sciences Center New Orleans · US

Funding

Role of microbiota in increased influenza severity due to particulate matter exposureP42ES013648 · NIEHS · LOUISIANA STATE UNIV A&M COL BATON ROUGE · PI SPRUNGER, PHILLIP · 2009 to 2024
$27.6M
TOXICOLOGICAL SIGNIFICANCE OF ALKYLBENZENE METABOLISMR01ES004344 · NIEHS · LSU HEALTH SCIENCES CENTER · PI BACKES, WAYNE L · 1996 to 2013
$4.0M
NIEHS NIH HHS P42 ES013648NIEHS NIH HHS R01 ES004344
6 · The paper itself

Abstract

Cytochrome P450 (P450) function requires the interaction of P450 and NADPH-cytochrome P450 reductase (CPR) in membranes, and is frequently studied using reconstituted systems composed solely of phosphatidylcholine. There is increasing evidence that other endoplasmic reticulum (ER) lipids can affect P450 structure, activity, and interactions with CPR. Some of these lipid effects have been attributed to the formation of organized liquid-ordered (l(o)) domains. The goal of this study was to determine if l(o) domains were formed in P450 reconstituted systems mimicking the ER membrane. CYP1A2, when incorporated in "ER-like" lipid vesicles, displayed detergent insolubility after treatment with Brij 98 and centrifugation in a sucrose gradient. Lipid probes were employed to identify domain formation in both ER-like vesicles and model membranes known to form l(o) domains. Changes in fluorescence resonance energy transfer (FRET) using an established donor/acceptor FRET pair in both ER-like and model l(o)-forming systems demonstrated the coexistence of l(o)- and liquid-disordered domains as a function of cholesterol and sphingomyelin content. Similarly, 6-dodecanoyl-2-dimethylaminonaphthalene (laurdan), a probe that reports on membrane organization, showed that cholesterol and sphingomyelin increased membrane order. Finally, brominated-phosphatidylcholine allowed for monitoring of the location of both CPR and CYP1A2 within the l(o) regions of ER-like systems. Taken together, the results demonstrate that ER-like vesicles generate microdomains, and both CYP1A2 and CPR predominantly localize into l(o) membrane regions. Probe fluorescent responses suggest that lipid microdomains form in these vesicles whether or not enzymes are included in the reconstituted systems. Thus, it does not appear that the proteins are critical for stabilizing l(o) domains.

Indexed as

AnimalsCattleChickensCytochrome P-450 CYP1A2Cytochrome P-450 Enzyme SystemEndoplasmic ReticulumLipidsMembrane MicrodomainsPhospholipidsSwineCytochrome P-450 CYP1A2Cytochrome P-450 Enzyme SystemLipidsPhospholipids

Identifiers

PMID23963955
PMCPMC3807054
OpenAlexW2172179183

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.