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From the Istituto di Ricerche Farmacologiche Mario Negri, Milano, Italy (F.B., L.C., M.C., I.M.-P., P.N., J.G., M.I., M.G.L., E.D.), and CEA-CENG, Laboratoire d'Hématologie, DBMS, INSERM U217, Grenoble, France (D.G., E.D.).
Correspondence to E. Dejana, CEA-CENG, Laboratoire d'Hématologie, DBMS, INSERM U217, 17, rue des Martyrs, 38054 Grenoble, Cedex 9, France. E-mail elisabetta@bossons.ceng.cea.fr.
Abstract Human vascular endothelial cadherin
(VE-cadherin, 7B4/cadherin-5) is an
endothelial-specific cadherin localized at the
intercellular junctions. To directly investigate the functional role of
this molecule we cloned the full-length cDNA from human
endothelial cells and transfected its coding region
into Chinese hamster ovary cells. The product of the transfected
cDNA had the same molecular weight as the natural VE-cadherin in human
endothelial cells, and reacted with several VE-cadherin
mouse monoclonal antibodies. Furthermore, it selectively concentrated
at intercellular junctions, where it codistributed with
-catenin.
VE-cadherin conferred adhesive properties to transfected cells. It
mediated homophilic, calcium-dependent aggregation and cell-to-cell
adhesion. In addition, it decreased intercellular permeability to
highmolecular weight molecules and reduced cell migration rate across
a wounded area. Thus, VE-cadherin may exert a relevant role in
endothelial cell biology through control of the
cohesion and organization of the intercellular junctions.
Key Words: cadherin endothelium transfection
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