Abstract
BackgroundDesmoglein 3 (Dsg3), a desmosomal adhesion protein, is expressed in basal and immediate suprabasal layers of skin and across the entire stratified squamous epithelium of oral mucosa. However, increasing evidence suggests that the role of Dsg3 may involve more than just cell-cell adhesion.Methodology/Principal FindingsTo determine possible additional roles of Dsg3 during epithelial cell adhesion we used overexpression of full-length human Dsg3 cDNA, and RNAi-mediated knockdown of this molecule in various epithelial cell types. Overexpression of Dsg3 resulted in a reduced level of E-cadherin but a colocalisation with the E-cadherin-catenin complex of the adherens junctions. Concomitantly these transfected cells exhibited marked migratory capacity and the formation of filopodial protrusions. These latter events are consistent with Src activation and, indeed, Src-specific inhibition reversed these phenotypes. Moreover Dsg3 knockdown, which also reversed the decreased level of E-cadherin, partially blocked Src phosphorylation.Conclusions/SignificanceOur data are consistent with the possibility that Dsg3, as an up-stream regulator of Src activity, helps regulate adherens junction formation.
Highlights
Desmoglein 3 (Dsg3), a 130 kDa glycoprotein, is a desmosomal cadherin and adhesion molecule
Full length human Dsg3 cDNA, tagged with the c-myc epitope, was cloned into a retroviral vector, pBABE.puro. 48 h after transfection of the retroviral vector in Cos-1 cells, Western blotting of cell lysates for hDsg3.myc revealed a distinct band of the correct size (,130-kDa) that was absent from vGFP control cells (Fig. 1B)
Our studies have utilised a full length human Dsg3 cDNA which allowed the generation of a human cell line stably over-expressing this gene
Summary
Desmoglein 3 (Dsg3), a 130 kDa glycoprotein, is a desmosomal cadherin and adhesion molecule. It is one of seven desmosomal cadherins, of two subfamilies, that have been identified in human tissues comprising four desmogleins (Dsg1–4) and three desmocollins (Dsc1–3) [1,2]. Desmosomes are intercellular junctions that provide strong intercellular links via the desmosome-intermediate filament complex and have a major function in maintaining tissue integrity [1]. Strong evidence supports a role for Dsg in normal desmosomal adhesion [6,7,8,9,10]. Increasing evidence suggests that the role of Dsg may involve more than just cell-cell adhesion
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