Vascular endothelial cadherin (VE-cadherin) (VE-cadherin)

Vascular endothelial cadherin (VE-cadherin), also known as CD144, is a transmembrane protein that serves as the primary component of endothelial adherens junctions, essential for maintaining vascular integrity (UniProt P33151). It functions by forming homophilic dimers with VE-cadherin molecules on adjacent cells, thereby regulating endothelial permeability and leukocyte extravasation (Nature Medicine, 2005, 11(3):298-305). A specific pathological interaction occurs when the fibrin E1 fragment, particularly the N-terminal sequence of the B-beta chain (B-beta 15-42), binds to the VE-cadherin extracellular domain, triggering cell retraction and barrier breakdown (Journal of Immunology, 2005, 175(3):1931-1936). This interface is the target of the therapeutic peptide FX06, which competitively inhibits fibrin binding to stabilize the endothelial barrier during inflammatory insults. By preventing the dissociation of VE-cadherin from the cytoskeleton, these agents maintain the zipper-like structure of the endothelium. Clinical applications focus on reducing tissue damage in conditions like myocardial reperfusion injury, acute respiratory distress syndrome (ARDS), and systemic capillary leak syndrome (Journal of Thrombosis and Haemostasis, 2012, 10(8):1504-1512). The target is particularly relevant in critical care settings where excessive vascular leakage leads to organ failure.

Other names

Cadherin-5CD144CDH57B4 antigenVascular endothelial-cadherin

Competitive inhibition of the interaction between fibrin fragment E and VE-cadherin to stabilize endothelial adherens junctions.