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Updated: Jun 14, 2026

In Vitro Model of Physiological and Pathological Blood Flow with Application to Investigations of Vascular Cell Remodeling
Published on: November 3, 2015
Vimentin expression influences flow dependent VASP phosphorylation and regulates cell migration and proliferation
Natalie Lund1, Daniel Henrion, Petra Tiede
1Medical Department II, University Hospital Lübeck, Lübeck, Germany.
Vimentin, an intermediate filament, is crucial for endothelial cell migration and proliferation by scaffolding VASP and enabling its phosphorylation. Suppressing vimentin significantly impairs these cellular functions.
Area of Science:
- Cell Biology
- Biochemistry
- Biophysics
Background:
- The cytoskeleton integrates cellular signals for complex functions.
- Vimentin, an intermediate filament, is vital for endothelial cell morphogenesis and leukocyte transmigration.
Purpose of the Study:
- To investigate the role of vimentin in endothelial cell migration, proliferation, and VASP phosphorylation.
- To elucidate the mechanism by which vimentin influences VASP localization and activity.
Main Methods:
- Vimentin suppression using siRNA in endothelial cells.
- Videomicroscopy and Boyden chamber assays for migration and transmigration.
- BrdU incorporation for proliferation assessment.
- Confocal microscopy for protein localization.
- Vimentin knockout mice studies.
Main Results:
- Vimentin suppression reduced endothelial cell migration by 50% and transmigration by 42.5%.
- Cell proliferation decreased by 43% upon vimentin suppression.
- Vimentin colocalized with VASP and PKG; vimentin suppression caused VASP translocation and reduced VASP phosphorylation.
- Vimentin knockout mice showed decreased VASP phosphorylation in arteries.
Conclusions:
- Vimentin acts as a scaffold essential for VASP localization and PKG-mediated VASP phosphorylation.
- Vimentin controls endothelial cell migration, proliferation, and morphogenesis through VASP phosphorylation.
- A link between vimentin, VASP phosphorylation, and actin dynamics is proposed to explain vimentin's role in endothelial cells.
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