Tissue- and cell type-specific modification of prion protein (PrP)-like protein Doppel, which affects PrP endoproteolysis |
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Authors: | Sakudo Akikazu Onodera Takashi |
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Institution: | aLaboratory of Biometabolic Chemistry, School of Health Sciences, Faculty of Medicine, University of the Ryukyus, 207 Uehara, Nishihara, Okinawa 903-0215, Japan;bDepartment of Molecular Immunology, School of Agricultural and Life Sciences, University of Tokyo, Bunkyo-ku, Tokyo 113-8657, Japan |
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Abstract: | A prion protein (PrP)-like protein, Doppel (Dpl) is a homologue of cellular PrP (PrPC). Immunoblotting revealed heterogeneous glycosylation patterns of Dpl and PrPC in several cell lines and tissues, including brain and testis. To investigate whether the glycosylation and modification of Dpl and PrPC 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 PrPC, whereas an N-terminally truncated fragment of PrPC was reduced by Dpl expression. These results indicated that Dpl was glycosylated in a cell type- and tissue-specific manner regardless of PrPC, while PrPC endoproteolysis was modulated by Dpl expression. |
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Keywords: | Prion Doppel Gene targeting Glycosylation Proteolysis |
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