Interaction between various 14-3-3beta segments and PrP in vitro / 中华实验和临床病毒学杂志
Chinese Journal of Experimental and Clinical Virology
;
(6): 165-167, 2010.
Article
in Chinese
| WPRIM
| ID: wpr-316935
ABSTRACT
<p><b>UNLABELLED</b>OBJECTIVE To study the potential interaction between PrP protein.</p><p><b>METHODS</b>The 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.</p><p><b>RESULTS</b>Both 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).</p><p><b>CONCLUSION</b>The 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.</p>
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Pathology
/
Endopeptidases
/
Scrapie
/
Binding Sites
/
Brain Chemistry
/
Prions
/
Prion Diseases
/
PrPSc Proteins
/
14-3-3 Proteins
/
Metabolism
Limits:
Animals
Language:
Chinese
Journal:
Chinese Journal of Experimental and Clinical Virology
Year:
2010
Type:
Article
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