The interaction between ubiquitin C-terminal hydrolase 37 and glucose-regulated protein 78 in hepatocellular carcinoma

被引:26
作者
Fang, Ying [1 ]
Mu, Jingui [2 ]
Ma, Yushui [1 ]
Ma, Duan [2 ]
Fu, Da [1 ]
Shen, Xizhong [1 ]
机构
[1] Fudan Univ, Dept Gastroenterol, Zhongshan Hosp, Shanghai 200032, Peoples R China
[2] Fudan Univ, Shanghai Med Sch, Key Lab Mol Med, Auspice Minist Educ, Shanghai 200032, Peoples R China
基金
中国博士后科学基金;
关键词
UCH37; GRP78; Interaction; HCC; UCH37 DEUBIQUITINATING ENZYME; CHROMATIN-REMODELING COMPLEX; NF-KAPPA-B; SUBSTRATE-SPECIFICITY; GRP78; CANCER; PROTEASOME; ACTIVATION; OVEREXPRESSION; EXPRESSION;
D O I
10.1007/s11010-011-0999-7
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The ubiquitin C-terminal hydrolase (UCH) is a subfamily of deubiquitinating enzymes, which consists of four members: UCH-L1, UCH-L3, UCH37, and BRCA1-associated protein-1. Although there is growing evidence that UCH enzymes and human malignancies are closely correlated, there have been few studies on UCH37, especially on its interactions with other proteins. In the current study, a functional proteomic analysis was performed to screen UCH37-interacting proteins in hepatocellular carcinoma (HCC), and glucose-regulated protein 78 was identified as one interacting with UCH37, which was confirmed by co-immunoprecipitation and confocal laser scanning microscopy analysis, suggesting that their interaction could provide a new insight into the mechanism of HCC.
引用
收藏
页码:59 / 66
页数:8
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