کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1940649 | 1050785 | 2006 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Prion protein-related proteins from zebrafish are complex glycosylated and contain a glycosylphosphatidylinositol anchor
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موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
A hallmark of prion diseases in mammals is a conformational transition of the cellular prion protein (PrPC) into a pathogenic isoform termed PrPSc. PrPC is highly conserved in mammals, moreover, genes of PrP-related proteins have been recently identified in fish. While there is only little sequence homology to mammalian PrP, PrP-related fish proteins were predicted to be modified with N-linked glycans and a C-terminal glycosylphosphatidylinositol (GPI) anchor. We biochemically characterized two PrP-related proteins from zebrafish in cultured cells and show that both zePrP1 and zeSho2 are imported into the endoplasmic reticulum and are post-translationally modified with complex glycans and a C-terminal GPI anchor.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 341, Issue 1, 3 March 2006, Pages 218–224
Journal: Biochemical and Biophysical Research Communications - Volume 341, Issue 1, 3 March 2006, Pages 218–224
نویسندگان
Margit Miesbauer, Theresa Bamme, Constanze Riemer, Birgit Oidtmann, Konstanze F. Winklhofer, Michael Baier, Jörg Tatzelt,