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Critical Reviews™ in Eukaryotic Gene Expression
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ISSN Imprimir: 1045-4403
ISSN En Línea: 2162-6502

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Critical Reviews™ in Eukaryotic Gene Expression

DOI: 10.1615/CritRevEukaryotGeneExpr.2014010087
pages 181-191

ALDOB Acts as a Novel HBsAg-Binding Protein and Its Coexistence Inhibits Cisplatin-Induced HepG2 Cell Apoptosis

Jing Wu
Department of Gastroenterology, Zhongshan Hospital, Xiamen University, Xiamen, Fujian Province, China
Can Dan
Medical College of Xiamen University, Xiamen, Fujian Province, China, 361005
Hong-Bo Zhao
Department of Gastroenterology, Zhongshan Hospital, Xiamen University, Xiamen, Fujian Province, China
Chuan-Xing Xiao
Department of Gastroenterology, Zhongshan Hospital, Xiamen University, Xiamen, Fujian Province, China
Yun-Peng Liu
Department of Gastroenterology, Zhongshan Hospital, Xiamen University, Xiamen, Fujian Province, China
Li-Juan Si
Department of Gastroenterology, Zhongshan Hospital, Xiamen University, Xiamen, Fujian Province, China
Jian-Lin Ren
Department of Gastroenterology, Zhongshan Hospital, Xiamen University, Xiamen, Fujian Province, China
Bayasi Guleng
Department of Gastroenterology, Zhongshan Hospital, Xiamen University, Xiamen, Fujian Province, China; Medical College of Xiamen University, Xiamen, Fujian Province, China, 361005

SINOPSIS

Chronic infection with hepatitis B virus is a cause of end-stage liver disease and hepatocellular carcinoma (HCC). We previously screened fructose-bisphosphate aldolase B (ALDOB) as a candidate binding protein of hepatitis B surface antigen (HBsAg) using a yeast 2-hybrid assay. In this study we aimed to confirm ALDOB as a binding protein of the S region of the HbsAg (HBs) and to investigate the function and involved mechanism between its interactions during HCC development. Our results demonstrated that both of exogenous and endogenous ALDOB proteins bind to HBs and colocalize in the cytoplasm in vitro. The coexistence of HBs and ALDOB inhibit apoptosis of cisplatin-induced HepG2 cells. Furthermore, western blot analysis showed the coexistence of HBs and ALDOB enhance the phosphorylations of AKT and its downstream of GSK-3β (phosphorylation); decreased expression of the pro-apoptotic proteins Bax, Bid, Bim, and Puma; and increased expression of the prosur-vival proteins Bcl-2, Bcl-xl, and Mcl-1 in HepG2 cells. These findings suggest that interaction between HBs and ALDOB might be applied as a potential therapeutic target during the treatment of HBV-related hepatitis or HCC.