NR AKVO
AU Shyu,W.C.; Kao,M.C.; Chou,W.Y.; Hsu,Y.D.; Soong,B.W.
TI Heat shock modulates prion protein expression in human NT-2 cells
QU Neuroreport 2000 Mar 20; 11(4): 771-4
PT journal article
AB 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 (PrPsc). PrPsc is 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 degrees C for 30 min. After heat-shock treatment, both the level of mRNA and PrPc 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.
MH Gene Expression Regulation/*physiology; Heat-Shock Response/*physiology; Human; PrPc Proteins/analysis/*biosynthesis/*genetics; RNA, Messenger/analysis/metabolism; Support, Non-U.S. Gov't; Time Factors; Tumor Cells, Cultured
AD Department of Neurology, Kang-Ning Hospital, Taipei, Taiwan.
SP englisch
PO England