Hepatitis B virus surface antigen interacts with acid alpha-glucosidase and alters glycogen metabolism

doi:10.1111/j.1872-034X.2010.00645.x

CNU IR > Pharmacy and Science > Dept. of Biotechnology (including master's program) > Periodical Articles > Item 310902800/25158

Please use this identifier to cite or link to this item: https://ir.cnu.edu.tw/handle/310902800/25158

Title:	Hepatitis B virus surface antigen interacts with acid alpha-glucosidase and alters glycogen metabolism
Authors:	Jui-Hsiang Hung Chiao-Wen Yan Ih-Jen Su Wan-Chi Lin Hui-Ching Wang Huan-Yao Lei Wen-Tsan Chang Wenya Huang Te-Jung Lu Ming-Derg Lai
Contributors:	生物科技系
Keywords:	acid alpha-glucosidase carbohydrate metabolism glycogen hepatitis B virus large surface protein hepatocellular carcinoma
Date:	2010-06
Issue Date:	2012-03-30 15:17:49 (UTC+8)
Publisher:	Wiley-Blackwell
Abstract:	Aim: Hepatitis B virus (HBV) infection is highly correlated with hepatocellular carcinoma. Previous studies have reported that expression of hepatitis B virus pre-S2 mutant surface antigen is related to hepatoma development. An aberrant carbohydrate metabolism is a hallmark of malignant transformation. Methods: We performed yeast two-hybrid screening with HBV pre-S2-del large surface protein (pre-S2Δ) by using human liver cDNA library, and identified the acid alpha-glucosidase (acid α-glucosidase) as the novel cellular interacting protein of pre-S2Δ. The association of pre-S2Δ with the acid α-glucosidase was confirmed by confocal immunofluorescence and co-immunoprecipitation assay. Further, the acid α-glucosidase activity and glycogen content were analyzed in ML-1 cells expressing pre-S2Δ. Results: The interaction between HBV large surface protein and acid α-glucosidase was demonstrated with co-immunoprecipitation in vitro and in vivo, and the binding was mediated through c-terminal region 889-952 amino acid of acid α-glucosidase. On the other hand, HBV large surface protein interacted with acid α-glucosidase through N-terminal region 1–157 amino acid of HBV large surface protein. Expression of HBV large surface protein enhanced acid α-glucosidase activity and resulted in decrease of cellular glycogen. Conclusion: Our result demonstrates that HBV large surface protein interacts with acid α-glucosidase which plays an important role in glycogen balance. Together, these data suggest a novel pathway by which HBV large surface protein affects carbohydrate metabolism.
Relation:	hepatology research 40(6)：p.633-640
Appears in Collections:	[Dept. of Biotechnology (including master's program)] Periodical Articles

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