Evidence map›Paper›PMID 20942796›Full record

ArticleDrug metabolism letters2011

Inhibition of cytochrome P450 1A2-mediated metabolism and production of reactive oxygen species by heme oxygenase-1 in rat liver microsomes.

James R Reed, George F Cawley, Wayne L Backes

Abstract read
In one paragraph

Article in Drug metabolism letters, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

22 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
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  3. Article
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  8. α- and β-Naphthoflavone synergistically attenuate HExperimental and therapeutic medicine · 2017
    Article
  9. Review
  10. Review
  11. Immobilized Cytochrome P450 for Monitoring of P450-P450 Interactions and Metabolism.Drug metabolism and disposition: the biological fate of chemicals · 2016
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
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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.

James R ReedDepartment of Pharmacology and the Stanley S. Scott Cancer Center, Louisiana State University Health Sciences Center, 1901 Perdido St., New Orleans, LA 70112, USA. rreed@lsuhsc.edu
George F Cawley
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 NOEL, ALEXANDRA · 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 ES004344NIEHS NIH HHS R01-ES004344
6 · The paper itself

Abstract

Heme oxygenase-1 (HO-1) is induced in most cell types by many forms of environmental stress and is believed to play a protective role in cells exposed to oxidative stress. Metabolism by cytochromes P450 (P450) is highly inefficient as the oxidation of substrate is associated with the production of varying proportions of hydrogen peroxide and/or superoxide. This study tests the hypothesis that heme oxygenase-1 (HO-1) plays a protective role against oxidative stress by competing with P450 for binding to the common redox partner, the NADPH P450 reductase (CPR) and in the process, diminishing P450 metabolism and the associated production of reactive oxygen species (ROS). Liver microsomes were isolated from uninduced rats and rats that were treated with cadmium and/or β-napthoflavone (BNF) to induce HO-1 and/or CYP1A2. HO-1 induction was associated with slower rates of metabolism of the CYP1A2-specific substrate, 7-ethoxyresorufin. Furthermore, HO-1 induction also was associated with slower rates of hydrogen peroxide and hydroxyl radical production by microsomes from rats induced for CYP1A2. The inhibition associated with HO-1 induction was not dependent on the addition of heme to the microsomal incubations. The effects of HO-1 induction were less dramatic in the absence of substrate for CYP1A2, suggesting that the enzyme was more effective in inhibiting the CYP1A2-related activity than the CPR-related production of superoxide (that dismutates to form hydrogen peroxide).

Indexed as

Oxidative StressAnimalsbeta-NaphthoflavoneCadmium ChlorideCytochrome P-450 CYP1A2CytochromesEnzyme InductionHemeHeme Oxygenase (Decyclizing)Hydrogen PeroxideHydroxyl RadicalIn Vitro TechniquesKineticsLiverMaleMicrosomes, Liverbeta-NaphthoflavoneCadmium ChlorideCyp1a2 protein, ratCytochrome P-450 CYP1A2CytochromesethoxyresorufinHemeHeme Oxygenase (Decyclizing)Hmox1 protein, ratHydrogen PeroxideHydroxyl RadicalNADPH-Ferrihemoprotein ReductaseOxazinesReactive Oxygen Species

Identifiers

PMID20942796
PMCPMC3252637
OpenAlexW2169730190

What OpenQuestion holds

Textmetadata
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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.