Effective penetration of cell-permeable peptide mimic of tyrosine residue 654 domain of beta-catenin into human renal tubular epithelial cells.
- Author:
Rui, ZENG
;
Gang, XU
;
Min, HAN
- Publication Type:Journal Article
- MeSH:
Carrier Proteins/*metabolism;
Epithelial Cells/cytology;
Epithelial Cells/*metabolism;
Fibroblasts/cytology;
Fibroblasts/metabolism;
Kidney Tubules/*cytology;
Peptides/metabolism;
Permeability;
Phosphorylation;
Tyrosine/*metabolism;
beta Catenin/*metabolism
- From:
Journal of Huazhong University of Science and Technology (Medical Sciences)
2007;27(6):630-4
- CountryChina
- Language:English
-
Abstract:
Phosphorylation of beta-catenin tyrosine residue 654 plays an important role in the epithelial to myofibroblast transition (EMT). Introducing mimic peptide of tyrosine residue 654 domain of beta-catenin into cells may influence phosphorylation of beta-catenin tyrosine residue 654. To deliver this mimic peptide into renal epithelial cells, we used penetratin as a vector, which is a novel cell permeable peptide, to deliver hydrophilic molecules into cells. A tyrosine 654 residue domain mimic peptide of beta-catenin (PM) with fused penetratin was constructed, purified and then detected for the penetration 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 beta-catenin was successfully obtained, which may provide a useful reagent for interfering the human renal tubular epithelial-mesenchymal transition.
