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Updated: Jan 19, 2026

Perturbing Endothelial Biomechanics via Connexin 43 Structural Disruption

Perturbing Endothelial Biomechanics via Connexin 43 Structural Disruption

Published on: October 4, 2019

Probing Endothelial Cell Mechanics Through Connexin 43 Disruption.

M M Islam¹, R L Steward^1,2

¹Department of Mechanical and Aerospace Engineering.

Experimental Mechanics

|September 24, 2019

Summary

This summary is machine-generated.

Connexin 43 (Cx43) gap junctions significantly influence endothelial cell mechanics. Disrupting Cx43 with chalcone alters intercellular stresses and cell movement, revealing Cx43

Keywords:

Connexin43 Gap junctions Intercellular stresses Monolayer stress microscopy biomechanics endothelial cells traction force microscopy

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Published on: March 28, 2014

Area of Science:

Endothelial cell biology
Biophysics
Cellular mechanics

Background:

Endothelial cells generate and transmit intercellular stresses via cell-cell junctions.
While adherens and tight junctions are implicated, the role of gap junctions remains unclear.
Connexin 43 (Cx43) is a key gap junction protein in endothelial cells.

Purpose of the Study:

To investigate the relationship between Cx43 and endothelial cell biomechanics.
To determine the impact of Cx43 disruption on intercellular stresses and cell mechanics.

Main Methods:

Human umbilical vein endothelial cells (HUVECs) were treated with varying concentrations of 2,5-dihydroxychalcone (chalcone), a Cx43 inhibitor.
Traction force microscopy and monolayer stress microscopy were used to measure cell-substrate tractions and cell-cell intercellular stresses.
Cellular velocities and strain energies were also quantified.

Main Results:

Low chalcone concentration increased normal intercellular stresses by 17%, while high concentration decreased them by 55%.
Shear stresses decreased by 16% (low) and 66% (high) chalcone.
Cellular tractions, velocities, and strain energies significantly decreased with increasing chalcone concentration.

Conclusions:

Cx43 plays a crucial role in maintaining endothelial cell biomechanics.
Disruption of Cx43 alters intercellular stress transmission and cellular mechanical properties.
These findings elucidate the contribution of Cx43 to endothelial cell function.