Role of protein kinase C in advanced glycation end products-induced epithelial-mesenchymal transition in renal proximal tubular epithelial cells.

The role of protein kinase C (PKC) activation in advanced glycation end products (AGEs)-induced epithelial-mesenchymal transition in renal proximal tubular epithelial cells was investigated. HKC cells were divided into three groups: normal group, AGE-BSA group (100 mg/L AGE-BSA) and AGE-BSA+PKC inhibitor (10 mumol/L chelerythrine chloride) group. PKC activity was measured by PKC assay kit. The expression of Vimentin, and phosphorylated beta-catenin was detected by using Western blotting, and the content of TGF-beta1 was examined by ELISA method. The intracellular disposition of Vimentin was observed by fluorescence microscopy. As compared with normal group, PKC activity was increased significantly in AGE-BSA group. The expression of Vimentin, phosphorylated beta-catenin, and TGF-beta1 was enhanced significantly in AGE-BSA group. The expression of Vimentin, phosphorylated beta-catenin, and TGF-beta1 was significantly blocked by chelerythrine chloride. High expression of Vimentin, phosphorylated beta-catenin, and TGF-beta1 induced by AGE-BSA may be mediated via the activation of PKC signal transduction pathway.