In vitro degradation of endothelial catenins by a neutrophil protease.
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, beta-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.
Moll
T
T
Institute of Cell Biology, Zentrum für die Molekularbiologie der Entzündung, University of Münster, Germany.
Dejana
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E
Vestweber
D
D
D015820:Cadherins / Q000378:metabolism; D002448:Cell Adhesion; D002478:Cells, Cultured; D003598:Cytoskeletal Proteins / Q000378:metabolism*; D051180:Desmoplakins; D010450:Endopeptidases / Q000097:blood*; D004730:Endothelium, Vascular / Q000378:metabolism*; D019084:Fluorescent Antibody Technique, Indirect; D006801:Humans; D009504:Neutrophils / Q000201:enzymology*; D015534:Trans-Activators; D051176:beta Catenin; D051185:gamma Catenin
C495270:CTNNB1 protein, human; D015820:Cadherins; D003598:Cytoskeletal Proteins; D051180:Desmoplakins; D015534:Trans-Activators; D051176:beta Catenin; D051185:gamma Catenin; D010450:Endopeptidases