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From the Institute of Nephrology, University of Wales College of Medicine, Heath Park, Cardiff, Wales
The aim of the current study was to examine the influence of transforming growth factor (TGF)-ß1 on proximal tubular epithelial cell-cell interaction, with particular emphasis on the regulation of adherens junction complex formation. Stimulation of the proximal tubular cell line HK-2 cells by TGF-ß1 led to loss of cell-cell contact and disassembly of both adherens and tight junctional complexes. Adherens junction disassembly was associated with reduction of both Triton-soluble and Triton-insoluble E-cadherin, and an increase in detergent-soluble ß-catenin. Under these conditions, immunoprecipitation and Western analysis demonstrated decreased association of ß-catenin, both with E-cadherin, 
-catenin, and the cell cytoskeleton. Confocal microscopy after immunostaining, showed decreased intensity of peripheral E-cadherin staining, and redistribution of ß-catenin expression to a perinuclear location. Tight junction disassembly was manifest by a reduction in the expression of Triton-soluble occludin and ZO-1 by Western analysis and their disassociation manifested by immunostaining and confocal microscopy. Loss of cell-cell contact and disassembly of adherens junctions were seen after addition of TGF-ß1 to the basolateral aspect of the cells. Immunoprecipitation experiments demonstrated co-localization of E-cadherin, ß-catenin, and TGF-ß1 RII in unstimulated cells. After TGF-ß1 stimulation, the TGF-ß1 RII no longer associated with either E-cadherin or ß-catenin. Dissociation of the adherens junction protein from the TGF-ß1 receptor was associated with increased ß-catenin tyrosine phosphorylation and decreased threonine phosphorylation. Furthermore after receptor ligand binding, ß-catenin became associated with the TGF-ß1-signaling molecules Smad3 and Smad4.
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