Interaction between various PrP segments and GFAP in vitro.
- Author:
Chen-Fang DONG
1
;
Bing SHAN
;
Xiao-Fan WANG
;
Jun HAN
;
Xiao-Ping DONG
Author Information
- Publication Type:Journal Article
- MeSH: Animals; Brain; metabolism; Cricetinae; Gene Deletion; Glial Fibrillary Acidic Protein; genetics; metabolism; Immunoprecipitation; Mice; Prions; genetics; metabolism; Protein Binding; Recombinant Proteins; metabolism
- From: Chinese Journal of Experimental and Clinical Virology 2007;21(3):214-216
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVETo study the potential interaction between PrP protein and glial fibrillary acidic protein (GFAP) and identify the binding region within PrP with GFAP.
METHODSThe supernatant of healthy and scrapie-infected hamsters' brain homogenate was prepared, while various recombinant PrP or GFAP proteins were expressed using prokaryotic-expressing or in-vitro translation system. The possible molecular interaction between PrP proteins and GFAP was tested by Pull-down and immunoprecipitation assays.
RESULTSBoth native PrP(C) and its protease-resistant isoform (PrP(Sc)) formed complexes with the native GFAP. The full-length recombinant PrP proteins interacted with GFAP. The domain responsible for interacting GFAP was located at C-terminal of PrP (residues 91 to 231).
CONCLUSIONThe studies of the association of PrP with GFAP may further provide insight into a potential role of GFAP in the biological function of PrP and the pathogenesis of prion disease.
