Evidence map›Paper›PMID 38732158›Full record

ArticleInternational journal of molecular sciences2024

Altered Plasma Membrane Lipid Composition in Hypertensive Neutrophils Impacts Epithelial Sodium Channel (ENaC) Endocytosis.

Yolanda Ríos-Medina, Pedro Rico-Chávez, Ivette Martínez-Vieyra, Juan C Durán-Álvarez, Mario Rodriguez-Varela, Ruth Rincón-Heredia, César Reyes-López, Doris Cerecedo

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Lipid Regulation of Mechanosensitive Ion Channels.International journal of molecular sciences · 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

8 authors.

Yolanda Ríos-MedinaLaboratorio de Hematobiología, Escuela Nacional de Medicina y Homeopatía, Instituto Politécnico Nacional, Mexico City 07230, Mexico.
Pedro Rico-ChávezLaboratorio de Hematobiología, Escuela Nacional de Medicina y Homeopatía, Instituto Politécnico Nacional, Mexico City 07230, Mexico.
Ivette Martínez-VieyraLaboratorio de Hematobiología, Escuela Nacional de Medicina y Homeopatía, Instituto Politécnico Nacional, Mexico City 07230, Mexico.ORCID 0000-0002-4414-5469
Juan C Durán-ÁlvarezInstituto de Ciencias Aplicadas y Tecnología, Universidad Nacional Autónoma de México, Mexico City 04510, Mexico.ORCID 0000-0002-5247-6719
Mario Rodriguez-VarelaInstituto de Ciencias Aplicadas y Tecnología, Universidad Nacional Autónoma de México, Mexico City 04510, Mexico.
Ruth Rincón-HerediaInstituto de Fisiología Celular, Universidad Nacional Autónoma de México, Mexico City 04510, Mexico.ORCID 0000-0002-5070-938X
César Reyes-LópezLaboratorio de Bioquímica Estructural, Escuela Nacional de Medicina y Homeopatía, Instituto Politécnico Nacional, Mexico City 07230, Mexico.ORCID 0000-0002-9860-8983
Doris CerecedoLaboratorio de Hematobiología, Escuela Nacional de Medicina y Homeopatía, Instituto Politécnico Nacional, Mexico City 07230, Mexico.ORCID 0000-0002-0015-8081

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biological membranes are composed of a lipid bilayer with embedded proteins, including ion channels like the epithelial sodium channel (ENaC), which are critical for sodium homeostasis and implicated in arterial hypertension (HTN). Changes in the lipid composition of the plasma membrane can significantly impact cellular processes related to physiological functions. We hypothesized that the observed overexpression of ENaC in neutrophils from HTN patients might result from alterations in the structuring domains within the plasma membrane, disrupting the endocytic processes responsible for ENaC retrieval. This study assessed the structural lipid composition of neutrophil plasma membranes from HTN patients along with the expression patterns of key elements regulating ENaC at the plasma membrane. Our findings suggest alterations in microdomain structure and SGK1 kinase activity, which could prolong ENaC presence on the plasma membrane. Additionally, we propose that the proteasomal and lysosomal degradation pathways are insufficient to diminish ENaC presence at the plasma membrane in HTN. These results highlight the importance of understanding ENaC retrieval mechanisms and suggest that targeting these mechanisms could provide insights for developing drugs to prevent and treat HTN.

Indexed as

Cell MembraneEndocytosisEpithelial Sodium ChannelsHypertensionNeutrophilsFemaleHumansImmediate-Early ProteinsMaleMembrane LipidsMembrane MicrodomainsMiddle AgedProtein Serine-Threonine KinasesSerum-Glucocorticoid Regulated KinasesEpithelial Sodium ChannelsImmediate-Early ProteinsMembrane LipidsProtein Serine-Threonine KinasesSerum-Glucocorticoid Regulated KinasesENaC regulatory complexendosome degradationmembrane lipidsneutrophilsproteasome

Identifiers

PMID38732158
PMCPMC11084340

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.