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Related Experiment Video

Updated: May 10, 2026

Study of the Actin Cytoskeleton in Live Endothelial Cells Expressing GFP-Actin

Study of the Actin Cytoskeleton in Live Endothelial Cells Expressing GFP-Actin

Published on: November 18, 2011

Ezrin/radixin/moesin proteins differentially regulate endothelial hyperpermeability after thrombin.

Djanybek M Adyshev¹, Steven M Dudek, Nurgul Moldobaeva

¹Institute for Personalized Respiratory Medicine, Department of Medicine, Section of Pulmonary, Critical Care, Sleep, and Allergy, University of Illinois at Chicago, COMRB 3154, MC 719, 909 S. Wolcott Ave., Chicago, IL 60612, USA. dadyshev@uic.edu

American Journal of Physiology. Lung Cellular and Molecular Physiology

|June 5, 2013

Summary

Thrombin disrupts endothelial cell barriers, affecting ERM proteins. Moesin worsens barrier dysfunction, while radixin protects it, offering new therapeutic targets for inflammatory conditions.

Keywords:

ERM PKC barrier dysfunction cytoskeleton endothelial cells phosphorylation thrombin

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An in vivo Assay to Test Blood Vessel Permeability

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Published on: March 16, 2013

Area of Science:

Endothelial cell biology
Cellular signaling
Protein biochemistry

Background:

Inflammatory agonists like thrombin disrupt endothelial cell (EC) barriers, causing pulmonary edema and hypoxemia.
Thrombin activates protein kinase C (PKC) and alters EC permeability by affecting F-actin stress fibers and actomyosin contraction.
Ezrin, radixin, and moesin (ERM) proteins are actin-binding proteins involved in EC barrier function.

Purpose of the Study:

To investigate the role of ERM proteins in thrombin-induced EC barrier disruption.
To determine if ERM proteins are phosphorylated by thrombin signaling and translocate to the EC periphery.
To explore the differential roles of moesin and radixin in modulating EC permeability.

Main Methods:

Utilized siRNA to deplete specific ERM proteins (moesin, radixin, or all three).
Measured transendothelial electrical resistance (TEER) to assess EC barrier permeability.
Analyzed cytoskeletal rearrangements, paracellular gap formation, and phospho-myosin light chain accumulation.

Main Results:

Thrombin induced ERM phosphorylation at specific threonine residues in a PKC-dependent manner, with translocation to the EC periphery.
Depletion of moesin or all ERM proteins attenuated thrombin-induced barrier dysfunction.
Radixin depletion, however, exacerbated thrombin-induced barrier permeability increase.

Conclusions:

ERM proteins play differential roles in thrombin-induced EC barrier modulation.
Moesin contributes to barrier dysfunction, whereas radixin provides a protective effect.
Targeting ERM proteins, particularly moesin and radixin, may offer therapeutic strategies for inflammatory barrier dysfunction.