Laboratory of Biometabolic Chemistry, School of Health Sciences, Faculty of Medicine, University of the Ryukyus, 207 Uehara, Nishihara, Okinawa 903-0215, Japan.
Biochem Biophys Res Commun. 2011 Jan 7;404(1):523-7. doi: 10.1016/j.bbrc.2010.12.016. Epub 2010 Dec 7.
A prion protein (PrP)-like protein, Doppel (Dpl) is a homologue of cellular PrP (PrP(C)). Immunoblotting revealed heterogeneous glycosylation patterns of Dpl and PrP(C) in several cell lines and tissues, including brain and testis. To investigate whether the glycosylation and modification of Dpl and PrP(C) could influence each other, PrP gene (Prnp)-deficient neuronal cells, transfected with Prnp and/or the Dpl gene (Prnd), were analyzed by deglycosylation with peptide N-glycosidase F. The modification of Dpl was not influenced by PrP(C), whereas an N-terminally truncated fragment of PrP(C) was reduced by Dpl expression. These results indicated that Dpl was glycosylated in a cell type- and tissue-specific manner regardless of PrP(C), while PrP(C) endoproteolysis was modulated by Dpl expression.
一种朊病毒蛋白（PrP）样蛋白，双调蛋白（Dpl）是细胞朊病毒蛋白（PrP（C））的同源物。免疫印迹显示 Dpl 和 PrP（C）在几种细胞系和组织中的糖基化模式存在异质性，包括脑和睾丸。为了研究 Dpl 和 PrP（C）的糖基化和修饰是否会相互影响，用肽 N-糖苷酶 F 对转染了 Prnp 和/或 Dpl 基因（Prnd）的 Prnp 基因（Prnp）缺陷神经元细胞进行了去糖基化分析。Dpl 的修饰不受 PrP（C）的影响，而 PrP（C）的 N 端截断片段则被 Dpl 表达减少。这些结果表明，Dpl 的糖基化方式在细胞类型和组织特异性方面不受 PrP（C）的影响，而 PrP（C）的内切蛋白酶活性则受 Dpl 表达的调节。
