Differential Localization of VE- and N-Cadherins in Human Endothelial Cells: VE-Cadherin Competes with N-Cadherin for Junctional Localization

doi:10.1083/jcb.140.6.1475

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© The Rockefeller University Press, 0021-9525/1998//1475 $5.00
The Journal of Cell Biology, Volume 140, Number 6, , 1998 1475-1484

Article

Differential Localization of VE- and N-Cadherins in Human Endothelial Cells: VE-Cadherin Competes with N-Cadherin for Junctional Localization

Pilar Navarro^*, Luigi Ruco, and Elisabetta Dejana^*

^* Laboratory of Vascular Biology, Istituto di Ricerche Farmacologiche Mario Negri, Milan, Italy; and II° Dipartimento di Medicina Sperimentale e Patologia, Universitá di Roma La Sapienza, Rome, Italy

The two major cadherins of endothelial cells are neural (N)-cadherinand vascular endothelial (VE)- cadherin. Despite similar levelof protein expression only VE-cadherin is located at cell–cellcontacts, whereas N-cadherin is distributed over the wholecell membrane. Cotransfection of VE-cadherin and N-cadherinin CHO cells resulted in the same distribution as that observedin endothelial cells indicating that the behavior of the twocadherins was not cell specific but related to their structuralcharacteristics. Similar amounts of ${alpha}$ - and β-catenins andplakoglobin were associated to VE- and N-cadherins, whereasp120 was higher in the VE-cadherin complex. The presence ofVE-cadherin did not affect N-cadherin homotypic adhesive propertiesor its capacity to localize at junctions when cotransfectantswere cocultured with cells transfected with N-cadherin only.To define the molecular domain responsible for the VE-cadherin–dominantactivity we prepared a chimeric construct formed by VE-cadherin extracellular region linked to N-cadherin intracellular domain.The chimera lost the capacity to exclude N-cadherin from junctionsindicating that the extracellular domain of VE-cadherin aloneis not sufficient for the preferential localization of themolecule at the junctions. A truncated mutant of VE-cadherinretaining the full extracellular domain and a short cytoplasmictail (Arg⁶²¹–Pro⁷⁰²) lacking the catenin-binding regionwas able to exclude N-cadherin from junctions. This indicatesthat the Arg⁶²¹–Pro⁷⁰² sequence in the VE-cadherin cytoplasmictail is required for N-cadherin exclusion from junctions. Competitionbetween cadherins for their clustering at intercellular junctionsin the same cell has never been described before. We speculate that, in the endothelium, VE- and N-cadherin play differentroles; whereas VE-cadherin mostly promotes the homotypic interactionbetween endothelial cells, N-cadherin may be responsible forthe anchorage of the endothelium to other surrounding cell typesexpressing N-cadherin such as vascular smooth muscle cellsor pericytes.

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Address all correspondence to Pilar Navarro, Istituto di RicercheFarmacologiche Mario Negri, Via Eritrea 62, 20157 Milano, Italia.Tel.: (39) 2-39014477. Fax: (39) 2-3546277. E-mail: pilar{at}irfmn.mnegri.it

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