Heat shock modulates prion protein expression in human NT‐2 cells
作者:
Woei-Cherng Shyu,
Ming-Ching Kao,
Wei-Yuan Chou,
Yaw-Don Hsu,
Bing-Wen Soong,
期刊:
NeuroReport
(OVID Available online 2000)
卷期:
Volume 11,
issue 4
页码: 771-774
ISSN:0959-4965
年代: 2000
出版商: OVID
关键词: heat shock;NT-2 cells;Prion protein;Stress response protein
数据来源: OVID
摘要:
The pathological hallmarks of Prion disease are cortical spongi-form changes and neuronal loss, which are induced by the accumulation of the scrapie-isoform prion protein (PrPSc). PrPScis derived from a post-translational modification of the cellular form of prion protein (PrPC). 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°C for 30 min. After heat-shock treatment, both the level of mRNA and PrPCprotein 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 3 h 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.
点击下载:
PDF
(736KB)
返 回