Evidence map›Paper›PMID 18567583›Full record

ArticleThe Journal of biological chemistry2008

Membrane composition modulates prestin-associated charge movement.

John Sfondouris, Lavanya Rajagopalan, Fred A Pereira, William E Brownell

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.7field-weighted citation impact, top 20% 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

31 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
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  3. LHFPL5 is a key element in force transmission from the tip link to the hair cell mechanotransducer channel.Proceedings of the National Academy of Sciences of the United States of America · 2024
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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

4 authors at 1 institution in 1 country.

John SfondourisBobby R. Alford Department of Otolaryngology-Head and Neck Surgery, Baylor College of Medicine, Houston, Texas 77030, USA.
Lavanya Rajagopalan
Fred A Pereira
William E Brownell
Baylor College of Medicine · US

Funding

INTRACOCHLEAR ELECTROCHEMICAL GRADIENTSR01DC000354 · NIDCD · JOHNS HOPKINS UNIVERSITY · PI BROWNELL, WILLIAM E, FARRELL, BRENDA FRANCES · 1989 to 2018
$10.4M
Biophysical Basis of Organization and Dynamics of Prestin Membrane ComplexesR01DC009622 · NIDCD · RICE UNIVERSITY · PI RAPHAEL, ROBERT M · 2009 to 2013
$1.8M
Research Training in Otolaryngology Head &Neck SurgeryT32DC007367 · NIDCD · BAYLOR COLLEGE OF MEDICINE · PI BROWNELL, WILLIAM E · 2005 to 2009
$382k
NIDCD NIH HHS R01 DC00354NIDCD NIH HHS R01 DC009622NIDCD NIH HHS T32 DC007367
6 · The paper itself

Abstract

The lateral membrane of the cochlear outer hair cell (OHC) is the site of a membrane-based motor that powers OHC electromotility, enabling amplification and fine-tuning of auditory signals. The OHC membrane protein prestin plays a central role in this process. We have previously shown that membrane cholesterol modulates the peak voltage of prestin-associated nonlinear capacitance in vivo and in vitro. The present study explores the effects of membrane cholesterol and docosahexaenoic acid content on the peak and magnitude of prestin-associated charge movement in a human embryonic kidney (HEK 293) cell model. Increasing membrane cholesterol results in a hyperpolarizing shift in the peak voltage of the nonlinear capacitance (Vpkc) and a decrease in the total charge movement. Both measures depend linearly on membrane cholesterol concentration. Incubation of cholesterol-loaded cells in cholesterol-free media partially restores the Vpkc toward normal values but does not have a compensatory effect on the total charge movement. Decreasing membrane cholesterol results in a depolarizing shift in Vpkc that is restored toward normal values upon incubation in cholesterol-free media. However, cholesterol depletion does not alter the magnitude of charge movement. In contrast, increasing membrane docosahexaenoic acid results in a hyperpolarizing shift in Vpkc that is accompanied by an increase in total charge movement. Our results quantify the relation between membrane cholesterol concentration and prestin-associated charge movement and enhance our understanding of how membrane composition modulates prestin function.

Indexed as

AnimalsAnion Transport ProteinsCell LineCell MembraneCell MovementCholesterolCloning, MolecularCochleaElectric ConductivityElectrophysiologyGerbillinaeHumansMembrane LipidsPatch-Clamp TechniquesSulfate TransportersAnion Transport ProteinsCholesterolMembrane LipidsSLC26A5 protein, humanSulfate Transporters

Identifiers

PMID18567583
PMCPMC2504877
OpenAlexW1990169593

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.