Evidence map›Paper›PMID 32759774›Full record

ArticleInternational journal of molecular sciences2020

α1AMP-Activated Protein Kinase Protects against Lipopolysaccharide-Induced Endothelial Barrier Disruption via Junctional Reinforcement and Activation of the p38 MAPK/HSP27 Pathway.

Marine Angé, Diego Castanares-Zapatero, Julien De Poortere, Cécile Dufeys, Guillaume E Courtoy, Caroline Bouzin, Rozenn Quarck, Luc Bertrand, Christophe Beauloye, Sandrine Horman

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

10 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Atypical p38 Signaling, Activation, and Implications for Disease.International journal of molecular sciences · 2021
    Review
  10. 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

10 authors at 3 institutions in 1 country.

Marine AngéPôle de Recherche Cardiovasculaire (CARD), Institut de Recherche Expérimentale et Clinique (IREC), Université Catholique de Louvain (UCLouvain), 1200 Brussels, Belgium.ORCID 0000-0002-8357-7096
Diego Castanares-ZapateroPôle de Recherche Cardiovasculaire (CARD), Institut de Recherche Expérimentale et Clinique (IREC), Université Catholique de Louvain (UCLouvain), 1200 Brussels, Belgium.ORCID 0000-0001-7112-2070
Julien De PoorterePôle de Recherche Cardiovasculaire (CARD), Institut de Recherche Expérimentale et Clinique (IREC), Université Catholique de Louvain (UCLouvain), 1200 Brussels, Belgium.
Cécile DufeysPôle de Recherche Cardiovasculaire (CARD), Institut de Recherche Expérimentale et Clinique (IREC), Université Catholique de Louvain (UCLouvain), 1200 Brussels, Belgium.ORCID 0000-0002-2042-7218
Guillaume E CourtoyIREC Imaging Platform, Institut de Recherche Expérimentale et Clinique (IREC), Université Catholique de Louvain (UCLouvain), 1200 Brussels, Belgium.ORCID 0000-0001-9311-2105
Caroline BouzinIREC Imaging Platform, Institut de Recherche Expérimentale et Clinique (IREC), Université Catholique de Louvain (UCLouvain), 1200 Brussels, Belgium.
Rozenn QuarckDepartment of Chronic Diseases & Metabolism (CHROMETA), Laboratory of Respiratory Diseases & Thoracic Surgery (BREATHE), KU Leuven, 3000 Leuven, Belgium.ORCID 0000-0002-8293-6261
Luc BertrandPôle de Recherche Cardiovasculaire (CARD), Institut de Recherche Expérimentale et Clinique (IREC), Université Catholique de Louvain (UCLouvain), 1200 Brussels, Belgium.ORCID 0000-0003-0655-7099
Christophe BeauloyePôle de Recherche Cardiovasculaire (CARD), Institut de Recherche Expérimentale et Clinique (IREC), Université Catholique de Louvain (UCLouvain), 1200 Brussels, Belgium.
Sandrine HormanPôle de Recherche Cardiovasculaire (CARD), Institut de Recherche Expérimentale et Clinique (IREC), Université Catholique de Louvain (UCLouvain), 1200 Brussels, Belgium.
UCLouvain · BECliniques Universitaires Saint-Luc · BEKU Leuven · BE

Funding

Action de Recherche Concertée de la Communauté Wallonie-Bruxelles, Belgium ARC 16/21-074Fonds National de la Recherche Scientifique et Médicale (FNRS, Belgium) T0241.16
6 · The paper itself

Abstract

Vascular hyperpermeability is a determinant factor in the pathophysiology of sepsis. While, AMP-activated protein kinase (AMPK) is known to play a role in maintaining endothelial barrier function in this condition. Therefore, we investigated the underlying molecular mechanisms of this protective effect. α1AMPK expression and/or activity was modulated in human dermal microvascular endothelial cells using either α1AMPK-targeting small interfering RNA or the direct pharmacological AMPK activator 991, prior to lipopolysaccharide (LPS) treatment. Western blotting was used to analyze the expression and/or phosphorylation of proteins that compose cellular junctions (zonula occludens-1 (ZO-1), vascular endothelial cadherin (VE-Cad), connexin 43 (Cx43)) or that regulate actin cytoskeleton (p38 MAPK; heat shock protein 27 (HSP27)). Functional endothelial permeability was assessed by in vitro Transwell assays, and quantification of cellular junctions in the plasma membrane was assessed by immunofluorescence. Actin cytoskeleton remodeling was evaluated through actin fluorescent staining. We consequently demonstrate that α1AMPK deficiency is associated with reduced expression of CX43, ZO-1, and VE-Cad, and that the drastic loss of CX43 is likely responsible for the subsequent decreased expression and localization of ZO-1 and VE-Cad in the plasma membrane. Moreover, α1AMPK activation by 991 protects against LPS-induced endothelial barrier disruption by reinforcing cortical actin cytoskeleton. This is due to a mechanism that involves the phosphorylation of p38 MAPK and HSP27, which is nonetheless independent of the small GTPase Rac1. This results in a drastic decrease of LPS-induced hyperpermeability. We conclude that α1AMPK activators that are suitable for clinical use may provide a specific therapeutic intervention that limits sepsis-induced vascular leakage.

Indexed as

AMP-Activated Protein KinasesAntigens, CDCadherin 5CadherinsCapillary PermeabilityConnexin 43Endothelial CellsHSP27 Heat-Shock ProteinsHumansLipopolysaccharidesp38 Mitogen-Activated Protein KinasesRNA, Small InterferingSepsisSignal TransductionZonula Occludens-1 ProteinAMP-Activated Protein KinasesAntigens, CDCadherin 5CadherinsConnexin 43HSP27 Heat-Shock ProteinsLipopolysaccharidesp38 Mitogen-Activated Protein KinasesPRKAA1 protein, humanRNA, Small InterferingTJP1 protein, humanZonula Occludens-1 Proteinactin cytoskeletonconnexin 43endothelial permeabilityheat shock protein 27lipopolysaccharidesepsisVE-cadherinzonula occludens-1α1AMPK

Identifiers

PMID32759774
PMCPMC7432762
OpenAlexW3047606085

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.