Ena/VASP is required for endothelial barrier function in vivo.

Document Type

Article

Publication Date

2007

Keywords

Actomyosin, Animals, Antigens-CD31, Aorta, Blood-Vessels, Cell-Adhesion-Molecules, Cells-Cultured, Cytoskeleton, Edema, Embryo-Mammalian, Endothelial-Cells, Endothelium-Vascular, Female, Heart, Hemorrhage, Humans, Immunohistochemistry, Intercellular-Junctions, Mice-Knockout, Pregnancy, Umbilical-Veins

First Page

761

Last Page

775

JAX Source

J Cell Biol 2007 Nov; 179(4):761-75.

Abstract

Enabled/vasodilator-stimulated phosphoprotein (Ena/VASP) proteins are key actin regulators that localize at regions of dynamic actin remodeling, including cellular protrusions and cell-cell and cell-matrix junctions. Several studies have suggested that Ena/VASP proteins are involved in the formation and function of cellular junctions. Here, we establish the importance of Ena/VASP in endothelial junctions in vivo by analysis of Ena/VASP-deficient animals. In the absence of Ena/VASP, the vasculature exhibits patterning defects and lacks structural integrity, leading to edema, hemorrhaging, and late stage embryonic lethality. In endothelial cells, we find that Ena/VASP activity is required for normal F-actin content, actomyosin contractility, and proper response to shear stress. These findings demonstrate that Ena/VASP is critical for actin cytoskeleton remodeling events involved in the maintenance of functional endothelia.

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