Effective penetration of cell-permeable peptide mimic of tyrosine residue 654 domain of beta-catenin into human renal tubular epithelial cells / 华中科技大学学报(医学)(英德文版)
Journal of Huazhong University of Science and Technology (Medical Sciences)
; (6): 630-4, 2007.
Article
in En
| WPRIM
| ID: wpr-635005
Responsible library:
WPRO
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.
Full text:
1
Index:
WPRIM
Main subject:
Peptides
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Permeability
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Phosphorylation
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Tyrosine
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Carrier Proteins
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Epithelial Cells
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Beta Catenin
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Fibroblasts
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Kidney Tubules
Language:
En
Journal:
Journal of Huazhong University of Science and Technology (Medical Sciences)
Year:
2007
Type:
Article