Effective Penetration of Cell-permeable Peptide Mimic of Tyrosine Residue 654 Domain of β-catenin in

• 作 者: ZENG Rui XU Gang HAN Min LIU W
• 机 构: Division of Nephrology, Department of Internal Medicine, Tongji Hospital, Huazhong University of Sci
• 出 处: 华中科技大学学报（医学）（英德文版）
• 发表日期: 2007年6期
• 关键词: β-catenin mimic peptide cell permeable peptide expression purification penetrati

Phosphorylation of β-catenin tyrosine residue 654 plays an important role in the epithelial to myofibroblast transition (EMT). Introducing mimic peptide of tyrosine residue 654 domain of β-catenin into cells may influence phosphorylation of β-catenin tyrosine residue 654. To deliver this mimic peptide into renal epithelial cells, we used penetratin as a vector, which is a novel cell perme-able peptide, to deliver hydrophilic molecules into cells. A tyrosine 654 residue domain mimic pep-tide of β-catenin (PM) with fused penetratin was constructed, purified and then detected for the pene-tration of the mimic peptide into human renal tubular epithelial cells (HK-2). The results showed that purified fusion mimic peptide could efficiently and rapidly translocate into human renal tubular epithelial cells. It is concluded that a cell-permeable peptides mimic of tyrosine residue 654 domain of β-catenin was successfully obtained, which may provide a useful reagent for interfering the human renal tubular epithelial-mesenchymal transition.