Heat shock modulates prion protein expression in human NT-2 cells.
Neuroreport
; 11(4): 771-4, 2000 Mar 20.
Article
in En
| MEDLINE
| ID: mdl-10757517
ABSTRACT
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.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Gene Expression Regulation
/
PrPC Proteins
/
Heat-Shock Response
Limits:
Humans
Language:
En
Journal:
Neuroreport
Journal subject:
NEUROLOGIA
Year:
2000
Type:
Article
Affiliation country:
Taiwan