Summary
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 permeable peptide, to deliver hydrophilic molecules into cells. A tyrosine 654 residue domain mimic peptide of β-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 β-catenin was successfully obtained, which may provide a useful reagent for interfering the human renal tubular epithelial-mesenchymal transition.
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This project was supported by a grant from the National Natural Sciences Foundation of China (No. 30370657).
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Zeng, R., Xu, G., Han, M. et al. Effective penetration of cell-permeable peptide mimic of tyrosine residue 654 domain of β-catenin into human renal tubular epithelial cells. J. Huazhong Univ. Sci. Technol. [Med. Sci.] 27, 630–634 (2007). https://doi.org/10.1007/s11596-007-0602-3
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DOI: https://doi.org/10.1007/s11596-007-0602-3