© The Rockefeller University Press,
0021-9525/1998//403 $5.00
The Journal of Cell Biology, Volume 140, Number 2,
, 1998 403-407
In Vitro Degradation of Endothelial Catenins by a Neutrophil Protease
Thomas Moll*,
Elisabetta Dejana
, and
Dietmar Vestweber*
* Institute of Cell Biology, Zentrum für die Molekularbiologie der Entzündung, University of Münster, Germany; and
Istituto di Ricerche Farmacologiche Mario Negri, Milano, Italy
It has been recently proposed that adhesion of polymorphonuclear cells (PMNs) to human umbilical vein endothelial cells leads to the disorganization of the vascular endothelial cadherin–dependent endothelial adherens junctions. Combined immunofluorescence and biochemical data suggested that after adhesion of PMNs to the endothelial cell surface, β-catenin, as well as plakoglobin was lost from the cadherin/catenin complex and from total cell lysates. In this study we present data that strongly suggest that the adhesion-dependent disappearance of endothelial catenins is not mediated by a leukocyte to endothelium signaling event, but is due to the activity of a neutrophil protease that is released upon detergent lysis of the cells.
Abbreviations used in this paper: EC, endothelial cells; HUVEC, human umbilical vein endothelial cells; PFA, paraformaldehyde; PMN, polymorphonuclear cell; VE, vascular endothelial.
Address all correspondence to D. Vestweber, Institute of Cell Biology, ZMBE, Technologiehof Münster, Mendelstrasse 11, D-48149 Münster, Germany. Tel.: 49-251-835-86-17; FAX: 49-251-835-86-16; E-mail:vestweb{at}uni-muenster.de

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