中國醫藥大學機構典藏 China Medical University Repository, Taiwan:Item 310903500/7101
English  |  正體中文  |  简体中文  |  全文筆數/總筆數 : 29490/55136 (53%)
造訪人次 : 1507479      線上人數 : 707
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
    主頁登入上傳說明關於CMUR管理 到手機版
    請使用永久網址來引用或連結此文件: http://ir.cmu.edu.tw/ir/handle/310903500/7101


    題名: Heat shock modulates prion protein expression in human NT-2 cells
    作者: (Shyu WC)*;高銘欽(Ming-Ching Kao);(Chou WY);(Hsu YD);(Song BW)
    貢獻者: 醫學院臨床醫學研究所
    日期: 2000-03
    上傳時間: 2009-08-26 16:12:40 (UTC+8)
    摘要: The pathological hallmarks of Prion disease are cortical spongiform changes and neuronal loss, which are induced by the accumulation of the scrapie-isoform prion protein (PrP(Sc)). PrP(Sc) is derived from a post-translational modification of the cellular form of prion protein (PrP(C)). Heat-shock proteins, a group of molecular chaperones, are involved in the degradation of denatured proteins and post-translational folding of newly synthesized polypeptides. In an attempt to examine any possible relationship between heat shock stress and an induction of prion protein (PrP), human NT-2 cells were treated with heat shock at 42 degrees C for 30 min. After heat-shock treatment, both the level of mRNA and PrP(C) protein were analyzed at various time points by Northern and Western blot, respectively. There was a 1.5- to 2.5-fold increase in PrP mRNA levels 1 and 3h following heat shock. In addition, a two-fold increase in protein level of PrP was found 3 h after heat-shock treatment. These results suggest that cellular stress induces the elevation of both PrP mRNA and protein synthesis. The up-regulation of prion-protein mRNA and protein, implies that PrP may play a role in cellular stress.
    關聯: NEUROREPORT 11(4)771~774
    顯示於類別:[臨床醫學研究所] 期刊論文

    文件中的檔案:

    檔案 描述 大小格式瀏覽次數
    index.html0KbHTML401檢視/開啟


    在CMUR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