Cadherin5

Cadherin5, also known as VE-cadherin (vascular endothelial cadherin), is a classical cadherin protein that plays a critical role in maintaining the integrity of endothelial cell junctions in blood vessels. It is encoded by the *CDH5* gene located on chromosome 16 in humans. VE-cadherin is primarily expressed in endothelial cells lining blood vessels, where it contributes to the formation and stabilization of adherens junctions, which are essential for vascular permeability and angiogenesis.

The structure of VE-cadherin consists of five extracellular cadherin repeats, a transmembrane domain, and a cytoplasmic tail. The extracellular domain mediates homophilic binding between adjacent endothelial cells, while the cytoplasmic tail interacts with cytoskeletal proteins and signaling molecules, such as β-catenin and p120-catenin, to regulate junctional stability. Mutations or dysfunction in VE-cadherin have been linked to vascular abnormalities, including increased permeability and impaired angiogenesis, which can contribute to diseases such as diabetes, hypertension, and cancer.

VE-cadherin also participates in signaling pathways that influence endothelial cell behavior. For example, it regulates the activity of small GTPases like Rho and Rac, which control cytoskeletal dynamics and cell migration. Additionally, VE-cadherin interacts with growth factor receptors, such as vascular endothelial growth factor receptor 2 (VEGFR2), to modulate signaling responses that promote vascular development and repair.

In research, VE-cadherin has been studied as a potential therapeutic target for vascular diseases. Disrupting its function can lead to excessive vascular leakage, while enhancing its stability may improve endothelial barrier function. Furthermore, its role in tumor angiogenesis has made it a focus for anti-cancer strategies, as inhibiting VE-cadherin could disrupt blood supply to tumors. Overall, VE-cadherin remains a key molecule in vascular biology with broad implications for health and disease.