Alternations of tau protein and its phosphorylated profiles in the experimental hamsters infected by scrapie agents 263K and 139A.
- Author:
Gui-rong WANG
1
;
Song SHI
;
Chen GAO
;
Bao-yun ZHANG
;
Chan TIAN
;
Chen-fang DONG
;
Rui-min ZHOU
;
Xiao-li LI
;
Cao CHEN
;
Xiao-ping DONG
Author Information
1. State Key Laboratory for Infectious Disease Prevention and Control, National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Beijing 100052, China.
- Publication Type:Journal Article
- MeSH:
Animals;
Blotting, Western;
Brain;
metabolism;
Cricetinae;
Gene Expression Regulation;
physiology;
Phosphorylation;
Polymerase Chain Reaction;
PrPSc Proteins;
pathogenicity;
Prion Diseases;
metabolism;
tau Proteins;
metabolism
- From:
Chinese Journal of Virology
2009;25(3):202-207
- CountryChina
- Language:Chinese
-
Abstract:
In human prion diseases, phosphorylated-tau deposition has been described in a rare genetic form, Gerstmann-Straussler-Scheinker disease, but is not considered part of the neuropathological picture of Creutzfeldt-Jakob disease. To investigate the possible changes of tau and phosphorylated tau (Ser396/Ser404) in transmissible spongiform encephalopathies (TSEs), the expressions and transcriptions of above biological factors in the brain tissues of 263K- and 139A-infected hamsters were evaluated by Western blots and Real Time PCR, respectively, followed by quantitative analyses of immunoblot images and relative transcriptional levels compared with normal animals. The contents of total tau increased, but phosphorylated tau at Ser396 and Ser404 decreased, regardless of the types of scrapie agents and clinical incubations. Transcriptions of two tau isoforms were also markedly increased. These findings suggested that dephosphorylation of tau at Ser396/Ser404 was a illness-correlative phenomenon in TSEs. Alterations of tau and phosphorylated tau (Ser396/Ser404) were either intermediate or consequent events in TSE pathogenesis and proposed the potential linkage of these bioactive proteins with the pathogenesis of prion diseases.
