Heat shock modulates prion protein expression in human NT-2 cells.
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.
Shyu
W C
WC
Department of Neurology, Kang-Ning Hospital, Taipei, Taiwan.
Kao
M C
MC
Chou
W Y
WY
Hsu
Y D
YD
Soong
B W
BW
D005786:Gene Expression Regulation / Q000502:physiology*; D018869:Heat-Shock Response / Q000502:physiology*; D006801:Humans; D018621:PrPC Proteins / Q000032:analysis / Q000096:biosynthesis* / Q000235:genetics*; D012333:RNA, Messenger / Q000032:analysis / Q000378:metabolism; D013997:Time Factors; D014407:Tumor Cells, Cultured
D018621:PrPC Proteins; D012333:RNA, Messenger