Chia Nan University of Pharmacy & Science Institutional Repository:Item 310902800/25158
English  |  正體中文  |  简体中文  |  全文筆數/總筆數 : 18074/20272 (89%)
造訪人次 : 4385259      線上人數 : 1108
RC Version 7.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
搜尋範圍 查詢小技巧:
  • 您可在西文檢索詞彙前後加上"雙引號",以獲取較精準的檢索結果
  • 若欲以作者姓名搜尋,建議至進階搜尋限定作者欄位,可獲得較完整資料
  • 進階搜尋
    請使用永久網址來引用或連結此文件: https://ir.cnu.edu.tw/handle/310902800/25158


    標題: Hepatitis B virus surface antigen interacts with acid alpha-glucosidase and alters glycogen metabolism
    作者: 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
    貢獻者: 生物科技系
    關鍵字: acid alpha-glucosidase
    carbohydrate metabolism
    glycogen
    hepatitis B virus large surface protein
    hepatocellular carcinoma
    日期: 2010-06
    上傳時間: 2012-03-30 15:17:49 (UTC+8)
    出版者: Wiley-Blackwell
    摘要: 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.
    關聯: hepatology research 40(6):p.633-640
    顯示於類別:[生物科技系(所)] 期刊論文

    文件中的檔案:

    檔案 描述 大小格式瀏覽次數
    99_28_j.pdf415KbAdobe PDF196檢視/開啟
    index.html0KbHTML1815檢視/開啟


    在CNU IR中所有的資料項目都受到原著作權保護.

    TAIR相關文章

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