Evidence map›Paper›PMID 37544101›Full record

ArticleJournal of inorganic biochemistry2023

Influence of cholesterol on kinetic parameters for human aromatase (P450 19A1) in phospholipid nanodiscs.

Nirupama Sumangala, Sang-Choul Im, Juan Valentín-Goyco, Richard J Auchus

Open access · greenAbstract read
In one paragraph

Article in Journal of inorganic biochemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
  2. Article
  3. The Nanodisc System for Investigating Protein-Lipid Interactions.Methods in molecular biology (Clifton, N.J.) · 2026
    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

4 authors at 1 institution in 1 country.

Nirupama SumangalaDivision of Metabolism, Endocrinology, & Diabetes, Department of Internal Medicine, Ann Arbor, MI 48109, USA; Program in Biophysics, University of Michigan, Ann Arbor, MI 48109, USA.
Sang-Choul ImDivision of Metabolism, Endocrinology, & Diabetes, Department of Internal Medicine, Ann Arbor, MI 48109, USA; Department of Pharmacology, University of Michigan, Ann Arbor, MI 48109, USA; Veterans Affairs Medical Center, Ann Arbor, MI 48105, United States.
Juan Valentín-GoycoDivision of Metabolism, Endocrinology, & Diabetes, Department of Internal Medicine, Ann Arbor, MI 48109, USA; Department of Pharmacology, University of Michigan, Ann Arbor, MI 48109, USA.
Richard J AuchusDivision of Metabolism, Endocrinology, & Diabetes, Department of Internal Medicine, Ann Arbor, MI 48109, USA; Program in Biophysics, University of Michigan, Ann Arbor, MI 48109, USA; Department of Pharmacology, University of Michigan, Ann Arbor, MI 48109, USA; Veterans Affairs Medical Center, Ann Arbor, MI 48105, United States. Electronic address: rauchus@med.umich.edu.
University of Michigan · US

Funding

Activation of androgen biosynthesis and drug metabolism by cytochrome b5R01GM086596 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI RICHARD J. AUCHUS · 2009 to 2026
$4.8M
Processivity and Catalytic Mechanism of Aldosterone SynthaseF31GM149006 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI VALENTIN-GOYCO, JUAN JOSE · 2023 to 2024
$60k
NIGMS NIH HHS F31 GM149006NIGMS NIH HHS R01 GM086596
6 · The paper itself

Abstract

Cholesterol, a significant constituent of the endoplasmic reticulum membrane, exerts a substantial effect on the membrane's biophysical and mechanical properties. Cholesterol, however, is often neglected in model systems used to study membrane-bound proteins. For example, the influence of cholesterol on the enzymatic functions of type 2 cytochromes P450, which require a phospholipid bilayer and the redox partner P450-oxidoreductase (POR) for activity, are rarely investigated. Human aromatase (P450 19A1) catalyzes three sequential oxygenations of 19‑carbon steroids to estrogens and is widely expressed across various tissues, which are characterized by varying cholesterol compositions. Our study examined the impact of cholesterol on the functionality of the P450 19A1 complex with POR. Nanodiscs containing P450 19A1 with 20% cholesterol/80% phospholipid had similar rates and affinity of androstenedione binding as phospholipid-only P450 19A1 nanodiscs, and rates of product formation were indistinguishable among these conditions. In contrast, the rate of the first electron transfer from POR to P450 19A1 was 3-fold faster in cholesterol-containing nanodiscs than in phospholipid-only nanodiscs. These results suggest that cholesterol influences some aspects of POR interaction with P450 19A1 and might serve as an additional regulatory mechanism in this catalytic system.

Indexed as

AromatasePhospholipidsCholesterolHumansOxidation-ReductionSteroidsAromataseCholesterolPhospholipidsSteroidsAromataseCholesterolelectron transferEstrogenNanodiscSteroidogenesis

Identifiers

PMID37544101
PMCPMC11260420
OpenAlexW4385216933

What OpenQuestion holds

Textmetadata
LicenceTDM
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.