Chia Nan University of Pharmacy & Science Institutional Repository:Item 310902800/25158
English  |  正體中文  |  简体中文  |  Items with full text/Total items : 17776/20117 (88%)
Visitors : 10937847      Online Users : 170
RC Version 7.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
Scope Tips:
  • please add "double quotation mark" for query phrases to get precise results
  • please goto advance search for comprehansive author search
  • Adv. Search
    HomeLoginUploadHelpAboutAdminister Goto mobile version
    Please use this identifier to cite or link to this item:

    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
    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

    Files in This Item:

    File Description SizeFormat
    99_28_j.pdf415KbAdobe PDF196View/Open

    All items in CNU IR are protected by copyright, with all rights reserved.

    DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - Feedback