کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1905624 | 1534725 | 2008 | 6 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Human cellular prion protein interacts directly with clusterin protein Human cellular prion protein interacts directly with clusterin protein](/preview/png/1905624.png)
Prion protein is a glycosyl-phosphatidyl-inositol anchored glycoprotein localized on the surface and within a variety of cells. Its conformation change is thought to be essential for the proliferation of prion neurodegenerative diseases. Using the yeast two-hybrid assay we identified an interaction between prion protein and clusterin, a chaperone glycoprotein. This interaction was confirmed in a mammalian system by in vivo co-immunoprecipitation and in vitro by circular dichroism analysis. Through deletion mapping analysis we demonstrated that the α subunit, but not the β subunit, of clusterin binds to prion and that the C-terminal 62 amino acid segment of the putative α helix region of clusterin is essential for the binding interaction. The full prion protein as well as the N-terminal section (aa 23–95) and C-terminal (aa 96–231) were shown to interact with clusterin. These findings provide new insights into the molecular mechanisms of interaction between prion and clusterin protein and contribute to the understanding of prion protein's physiological function.
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease - Volume 1782, Issue 11, November 2008, Pages 615–620