Effective Penetration of Cell-permeable Peptide Mimic of Tyrosine Residue 654 Domain of β-catenin into Human Renal Tubular Epithelial Cells
- Author:
Rui ZENG
1
;
Gang XU
;
Min HAN
;
Wei LIU
;
Xiaocheng LIU
Author Information
1. 华中科技大学同济医学院附属同济医院
- Keywords:
β-catenin;
mimic peptide;
cell permeable peptide;
expression;
purification;
penetration
- From:
Journal of Huazhong University of Science and Technology (Medical Sciences)
2007;27(6):630-634
- CountryChina
- Language:Chinese
-
Abstract:
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.
