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β-transducin repeat-containing E3 ubiquitin protein ligase inhibits migration, invasion and proliferation of glioma cells.

Authors :
Jun Liang
Wei-Feng Wang
Shao Xie
Xian-Li Zhang
Wei-Feng Qi
Xiu-Ping Zhou
Jin-Xia Hu
Qiong Shi
Ru-Tong Yu
Source :
Oncology Letters. Sep2017, Vol. 14 Issue 3, p3131-3135. 5p.
Publication Year :
2017

Abstract

β-transducin repeat-containing E3 ubiquitin protein ligase (β-TrCP) serves as the substrate recognition subunit for the Skp1-Cullin1-F-box protein E3 ubiquitin ligase, which recognizes the double phosphorylated DSG (X)2+nS destruction motif in various substrates that are essential for numerous aspects of tumorigenesis and regulates several important signaling pathways. However, the biological significance of β-TrCP in glioma progression remains largely unknown. A previous study by the authors demonstrated that the levels of β-TrCP protein expression in brain glioma tissues were significantly lower compared with non-tumorous tissues and that higher grades of gliomas exhibited lower levels of β-TrCP expression in comparison with lower glioma grades. In addition, low β-TrCP expression was associated with poor prognosis in patients with glioma. Subsequently, the present study aimed to investigate the effect of β-TrCP on migratory, invasive and proliferative abilities of glioma cells. β-TrCP plasmids were transfected into cultured U251 and U87 glioma cells, and changes in migration, invasion and proliferation were analyzed using wound healing, Transwell and EdU assays. It was identified that the overexpression of β-TrCP inhibited migration, invasion and proliferation in glioma cells. In summary, these results indicate that β-TrCP may serve a protective role against the progression of glioma by suppressing cell migration, invasion and proliferation. The potential mechanism of β-TrCP I glioma cells requires additional investigation. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
17921074
Volume :
14
Issue :
3
Database :
Academic Search Index
Journal :
Oncology Letters
Publication Type :
Academic Journal
Accession number :
124347153
Full Text :
https://doi.org/10.3892/ol.2017.6533