Interaction between various 14-3-3beta segments and PrP in vitro.
- Author:
Ying-Hui LIU
1
;
Yan-Ling HAN
;
Juan SONG
;
Ying WANG
;
Wei ZHOU
;
Bao-Yun ZHANG
;
Chan TIAN
;
Chao-Pin LI
;
Jun HAN
;
Xiao-Ping DONG
Author Information
- Publication Type:Journal Article
- MeSH: 14-3-3 Proteins; metabolism; Animals; Binding Sites; Brain Chemistry; Cricetinae; Endopeptidases; metabolism; PrPSc Proteins; metabolism; Prion Diseases; pathology; Prions; metabolism; Scrapie; physiopathology
- From: Chinese Journal of Experimental and Clinical Virology 2010;24(3):165-167
- CountryChina
- Language:Chinese
-
Abstract:
UNLABELLEDOBJECTIVE To study the potential interaction between PrP protein.
METHODSThe supernatant of health and scrapie-infected hamsters' brain homogenate was prepared, while various recombinant 14-3-3beta or PrP proteins were purified. The possible molecular interaction between 14-3-3beta proteins and PrP was tested by pull-down and immunoprecipitation assays.
RESULTSBoth native PrP(c) and its protease-resistant isoform (PrP(Sc)) formed complexes with 14-3-3beta. The full-length recombinant 14-3-3beta proteins interacted with PrP. The domain responsible for interacting 14-3-3beta was located at N-terminal of 14-3-3beta (residues 1 to 38).
CONCLUSIONThe studies of the association of PrP with 14-3-3beta may further provide insight into a potential role of 14-3-3beta in the biological function of PrP and the pathogenesis of prion disease.
