Interendothelial junctions and their role in the control of angiogenesis, vascular permeability and leukocyte transmigration

• Published in: Thrombosis and haemostasis Vol. 86; no. 1; p. 308
• Main Authors: Dejana, E, Spagnuolo, R, Bazzoni, G
• Format: Journal Article
• Language: English
• Published: Germany 01.07.2001
• Subjects: Animals; Cadherins - chemistry; Cadherins - metabolism; Cadherins - physiology; Capillary Permeability; Cell Adhesion Molecules; Chemotaxis, Leukocyte; Endothelium, Vascular - cytology; Endothelium, Vascular - ultrastructure; Gap Junctions - chemistry; Gap Junctions - physiology; Hemostasis; Humans; Membrane Proteins - chemistry; Membrane Proteins - metabolism; Membrane Proteins - physiology; Neovascularization, Physiologic; Receptors, Cell Surface
• ISSN: 0340-6245
• DOI: 10.1055/s-0037-1616228

Endothelial cell-cell junctions play an important role in vascular hemostasis. The two junctional proteins VE-cadherin and JAM-1 are localized at adherens and tight junctions, respectively. VE-cadherin is only expressed by endothelial cells, suggesting that it can exert cell specific function. Absence of VE-cadherin or blocking of its adhesive activity prevents a normal organization of new vascular structures, suggesting that VE-cadherin may be a molecular target of antiangiogenic therapy. In addition, the ability of permeability-increasing agents and adherent leukocytes to modify VE-cadherin/catenin organization may be related to a role in the control of vascular permeability and leukocyte infiltration. JAM-1 is an integral membrane protein expressed in endothelial and epithelial cells. Its extracellular domain can dimerize and bind homophilically. The intracellular domain (and in particular a PDZ-binding motif) enables JAM-1 to interact with structural and signaling proteins. Study of the molecular interactions of JAM-1 may help explain mechanisms of JAM-mediated function, such as control of paracellular permeability and leukocyte transmigration.