Author/Editor		Bazzoni, G; Martinez-Estrada, OM; Dejana, E
Title		Molecular architecture of interendothelial junctions
Type		članek
Source		In: Pathophysiological, clinical and laboratory aspects of thromboembolic disease. Proceedings of the 8th advanced teaching course in thrombosis and haemostasis; 2001 Mar 22-27; Kranjska gora. Ljubljana: University medical center, Department of angiology,
Publication year		2001
Volume		str. 30-4
Language		eng
Abstract		Endothelial cell-cell junctions play an important role in vascular hemostasis. Two junctional proteins, namely JAM-l and VE-cadherin; are localized at tight and adherens and junctions, respectively. While VE-cadherin is only expressed in endothelial cells, JAM-1 is also expressed in epithelial cells. Here, we will focus on the role of JAM-1 in the molecular architecture of endothelial tight junctions. The extracellular domain of JAM-1 can form dimers and mediate homophilic binding, The intracellular domain (and in particular a PDZ-binding motif) enables JAM-1 to interact with structural and signaling proteins, such as ZO-1, cingulin, CASK, and AF-6. Study of the molecular interactions of JAM-1 may help understand the functional role of JAM-1 in the control of paracellular permeability and leukocyte transmigration.
Descriptors		ENDOTHELIUM, VASCULAR INTERCELLULAR JUNCTIONS CELL ADHESION MOLECULES