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Related Concept Videos

Catenins01:23

Catenins

Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the adherens...
Regulation of Angiogenesis and Blood Supply01:24

Regulation of Angiogenesis and Blood Supply

Rapidly dividing tumors, embryos, and wounded tissues require more oxygen than usual, lowering the oxygen concentration in the blood. At low oxygen or hypoxic conditions, an oxygen-sensitive transcription factor called the hypoxia-inducible factor 1 or HIF1 is activated. HIF1 is a dimeric protein of alpha (ɑ) and beta (β) subunits.  Under optimal oxygen conditions, HIF1β is present in the nucleus while HIF1ɑ remains in the cytosol. HIF1ɑ is hydroxylated by prolyl hydroxylase and factor...
Tension Response at Adherens Junctions01:26

Tension Response at Adherens Junctions

The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin homology) domains...
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Adherens Junctions01:24

Adherens Junctions

Strong contact points between adjacent cells anchor them to each other, forming tissues. Such anchoring junctions are of two types –  adherens junctions and desmosomes. Adherens junctions are abundant in tissues such as  epithelium and endothelium, forming a continuous zone of adhesion called the adhesion belt. In other tissues, such as  heart muscle, they appear as clusters, linking the cells to produce coordinated heart muscle contraction.
Adherens Junctions are Dynamic
The endothelial cells...
Structure of Cadherins01:25

Structure of Cadherins

The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...

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Related Experiment Video

Updated: May 28, 2026

Mechanical Stimulation-induced Calcium Wave Propagation in Cell Monolayers: The Example of Bovine Corneal Endothelial Cells
10:46

Mechanical Stimulation-induced Calcium Wave Propagation in Cell Monolayers: The Example of Bovine Corneal Endothelial Cells

Published on: July 16, 2013

Caveolin-1 opens endothelial cell junctions by targeting catenins.

Romy Kronstein1, Jochen Seebach, Sylvia Grossklaus

  • 1Institute of Physiology, Medical Faculty of the TU-Dresden, Germany.

Cardiovascular Research
|October 1, 2011
PubMed
Summary

This study explores how endothelial cells lose their barrier function during inflammation. The researchers focused on a protein called caveolin-1 and its role in junctional reorganization. They found that caveolin-1 interacts with catenins, which are part of the VE-cadherin complex at cell junctions. When exposed to thrombin, caveolin-1 becomes phosphorylated, which weakens its connection to VE-cadherin. This causes junctional reorganization and increased permeability. Experiments with caveolin-1 knockout cells and a Y/F mutant confirmed that this interaction is essential for thrombin-induced permeability. The study highlights caveolin-1 as a key player in regulating endothelial barrier function through its effects on catenin binding.

Keywords:
endothelial barrier functionVE-cadherin regulationcaveolin-1 signalingthrombin-induced permeability

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Mechanical Stimulation-induced Calcium Wave Propagation in Cell Monolayers: The Example of Bovine Corneal Endothelial Cells
10:46

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Published on: July 16, 2013

Perturbing Endothelial Biomechanics via Connexin 43 Structural Disruption
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Measuring Changes in Brain Endothelial Barrier Integrity with Two Impedance-based Biosensors in Response to Cancer Cells and Cytokines
09:38

Measuring Changes in Brain Endothelial Barrier Integrity with Two Impedance-based Biosensors in Response to Cancer Cells and Cytokines

Published on: September 22, 2023

Area of Science:

  • Vascular biology within cell signaling
  • Endothelial function research in inflammation
  • Molecular mechanisms of barrier regulation

Background:

Endothelial cell junctions are critical for maintaining vascular integrity. During inflammation, these junctions often become permeable, but the exact molecular pathways remain unclear. Prior research has shown that thrombin can disrupt endothelial barriers, but the role of specific proteins in this process is less defined. Studies have identified VE-cadherin and catenins as key players in junctional stability. However, the mechanism by which these proteins interact with caveolin-1 is not fully understood. No prior work had resolved how caveolin-1 contributes to junctional reorganization. This gap motivated investigations into the role of caveolin-1 in thrombin-induced permeability. Understanding this process could clarify how endothelial barriers are regulated during inflammation. This paper addresses a specific mechanism involving caveolin-1 and catenins.

Purpose Of The Study:

The study aimed to explore how caveolin-1 influences endothelial cell junctions during inflammation. Specifically, the researchers sought to determine whether caveolin-1 interacts with VE-cadherin and catenins to regulate barrier function. They hypothesized that caveolin-1 plays a role in thrombin-induced junctional reorganization. The motivation came from the need to understand molecular pathways in endothelial permeability. The researchers focused on thrombin as a pro-inflammatory stimulus. They examined cultured human and mouse endothelial cells to test their hypothesis. The study aimed to clarify the role of caveolin-1 in junctional dynamics. This work builds on prior findings about VE-cadherin and catenin interactions.

Main Methods:

The researchers used cultured human and mouse endothelial cells to model thrombin-induced junctional changes. Impedance spectroscopy was employed to measure barrier function in real time. Biochemical assays were used to detect interactions between caveolin-1 and catenins. Morphological analysis provided visual confirmation of junctional reorganization. The team tested the effects of caveolin-1 knockout and Y/F mutants in endothelial cells. PAR-1 activation was induced to observe phosphorylation of caveolin-1. They monitored changes in VE-cadherin and catenin associations. The methods combined functional assays with molecular and structural analyses.

Main Results:

Caveolin-1 was found to associate with VE-cadherin and catenin complexes at endothelial junctions. Thrombin stimulation caused caveolin-1 phosphorylation via PAR-1 activation. This phosphorylation increased interactions between caveolin-1 and β- and γ-catenin. As a result, catenin binding to VE-cadherin was reduced. This led to junctional reorganization and decreased barrier function. Knockout of caveolin-1 prevented thrombin-induced junctional opening. Expression of a Y/F mutant also blocked this effect. Wild-type caveolin-1 fully restored junctional permeability. These findings suggest a direct role for caveolin-1 in junctional regulation.

Conclusions:

The authors propose that caveolin-1 is essential for thrombin-induced junctional reorganization. They suggest that caveolin-1 interacts with catenins to disrupt VE-cadherin complexes. This interaction is mediated by PAR-1-induced phosphorylation of caveolin-1. The study shows that caveolin-1 is necessary for junctional permeability changes. The findings support a model where caveolin-1 modulates catenin binding to VE-cadherin. This mechanism is specific to thrombin stimulation and PAR-1 signaling. The results highlight the importance of caveolin-1 in endothelial barrier regulation. The authors conclude that caveolin-1 plays a pivotal role in junctional dynamics.

Caveolin-1 interacts with β- and γ-catenin after thrombin stimulation, weakening their association with VE-cadherin and causing junctional reorganization.

PAR-1 activates caveolin-1 phosphorylation, which increases its binding to catenins and disrupts VE-cadherin complexes.

The Y/F mutant blocks thrombin-induced junctional opening, showing that phosphorylation is necessary for caveolin-1’s role in permeability.

Caveolin-1 knockout and Y/F mutant cells failed to show thrombin-induced junctional opening, while wild-type caveolin-1 restored permeability.

Impedance spectroscopy was used to monitor real-time changes in endothelial barrier integrity following thrombin stimulation.

VE-cadherin is a central component of endothelial junctions; its interaction with catenins is disrupted by caveolin-1, leading to barrier dysfunction.