中國醫藥大學機構典藏 China Medical University Repository, Taiwan:Item 310903500/7101
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    题名: 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)
    贡献者: 醫學院臨床醫學研究所
    日期: 2000-03
    上传时间: 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
    显示于类别:[臨床醫學研究所] 期刊論文

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