Anti-VE Cadherin antibody

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

VE Cadherin also known as CD144 or Cadherin-5 is a protein of about 135 kDa involved in cell adhesion. It is a transmembrane protein characterized by its presence at endothelial cell junctions. VE Cadherin belongs to the cadherin superfamily and its expression predominantly occurs in vascular endothelial cells. This protein facilitates the adhesion between adjacent endothelial cells maintaining the integrity of endothelial barriers.

Biological function summary

VE Cadherin performs essential roles in vascular development and permeability. It is a component of adherens junctions and connects with catenins to mediate cell-cell adhesion through calcium-dependent binding. This protein's adhesive function is critical for blood vessel maturation and response to inflammatory stimuli. Altering VE Cadherin expression impacts vascular stability and endothelial cell layering.

Pathways

VE Cadherin interacts with the Wnt and VEGF signaling pathways. It plays a role in the regulation of endothelial cell survival and migration. The interaction with β-catenin is important in the Wnt pathway influencing the transcription of target genes that modulate cell behavior. In the VEGF pathway VE Cadherin's association with protein kinase C highlights its involvement in endothelial permeability and angiogenesis processes.

Associated diseases and disorders

VE Cadherin dysregulation links to cancer progression and atherosclerosis. Its role in maintaining endothelial barrier integrity implicates it in tumor metastasis where disrupted cell adhesion facilitates cancer cell dissemination. Additionally altered VE Cadherin expression or function associates with atherosclerotic disease where damaged vascular endothelium leads to plaque formation. The connection of VE Cadherin with β-catenin in these conditions highlights its significance in pathological angiogenesis and vascular remodeling.