VECadherin

VE-cadherin, also known as vascular endothelial cadherin or CDH5, is a calcium-dependent cell–cell adhesion protein expressed primarily at endothelial adherens junctions. It plays a central role in maintaining the integrity of the vascular endothelium and regulating intercellular cohesion within blood vessels.

The protein is a single-pass type I transmembrane glycoprotein with five extracellular cadherin repeats (EC1–EC5). The extracellular domain mediates homophilic, calcium-dependent adhesion between neighboring endothelial cells. The cytoplasmic tail binds to catenins, including β-catenin and p120-catenin, and connects to the actin cytoskeleton via α-catenin, forming a cohesive adherens junction complex.

VE-cadherin supports endothelial barrier function and regulates vascular permeability, angiogenesis, and vascular remodeling. Junction stability is modulated by signaling pathways involving VEGF, Src-family kinases, and inflammatory mediators. Phosphorylation and endocytosis of VE-cadherin can lead to junctional disassembly and increased permeability, processes that are important during angiogenesis and inflammatory responses.

Regulation of VE-cadherin expression and junctional organization is dynamic and context-dependent, with developmental and pathological differences. Genetic loss of VE-cadherin in animal models disrupts vessel integrity and causes embryonic lethality, highlighting its essential role in vascular development. In diseases such as inflammation, sepsis, and cancer, altered VE-cadherin function contributes to vascular leak and abnormal angiogenesis.

The human CDH5 gene encodes VE-cadherin. The protein is commonly referred to by aliases including VE-cad, VE-Cadherin, and CDH5.