Asparagine-linked glycosylation of the scrapie and cellular prion proteins☆
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Intercommunication between metal ions and amyloidogenic peptides or proteins in protein misfolding disorders
2023, Coordination Chemistry ReviewsAn optimized Western blot assay provides a comprehensive assessment of the physiological endoproteolytic processing of the prion protein
2023, Journal of Biological ChemistryThe role of membranes in function and dysfunction of intrinsically disordered amyloidogenic proteins
2022, Advances in Protein Chemistry and Structural BiologyCitation Excerpt :These two domains are connected by a conserved hydrophobic core (HC) region (residues 105–126) that make contacts with the biological membrane. PrPc can be glycosylated at two highly conserved amino acid positions (N180 and N196 in mice) and form diglycosylated, monoglycosylated at N180, monoglycosylated at N196, and unglycosylated PrPc (Haraguchi et al., 1989). Prions are attached to the membrane by a glycosyl-phosphatidyl inositol (GPI) anchor.
Treatment of microglia with Anti-PrP monoclonal antibodies induces neuronal apoptosis in vitro
2021, HeliyonCitation Excerpt :Prion diseases are a group of fatal neurodegenerative diseases characterized by the conversion of the α-helices-rich cellular prion protein, PrPC and deposition in the central nervous system (CNS) of humans and animals of a disease specific isoform, PrPSc that is rich in β-sheet structure and partially proteinase-resistant (Prusiner and DeArmond, 1994; Tayebi and Hawke, 2006). The majority of PrP molecules carry bi-, tri- and tetra-antennary neutral and N-linked sialylated oligosaccharides at two sites (Endo et al., 1989; Haraguchi et al., 1989). A disulfide bond links the only two cysteines in the mature prion protein (Turk et al., 1988).
Multisite interactions of prions with membranes and native nanodiscs
2021, Chemistry and Physics of LipidsCitation Excerpt :Smaller amounts of two alternative topologic forms called Ntm- and Ctm-PrP can be generated within the biosynthetic pathway of the ER; they share the same membrane spanning region derived from PrP's central tract of hydrophobic residues, but they are oriented in opposite ways (Yost et al., 1990). Two asparagine residues are the sites of addition of heterogeneous antennary glycosyl structures (Haraguchi et al., 1989). A further form of PrP is shed from cell, resulting from the action of ADAM10, a metalloprotease sheddase.
Neurodegeneration meets immunology – A chemical biology perspective
2019, Bioorganic and Medicinal ChemistryCitation Excerpt :Two main N-glycoforms of PrP exist, mono- and di-glycosylated PrP. Haraguchi and coworkers laid the foundation for characterizing the glycosylation pattern of PrPC and PrPSc via treating purified PrP with N-glycosidase F.176 Subsequent publications using combinations of biochemical methods and mass spectrometry by two different groups showed that N-glycoforms of PrP are highly heterogeneous.177,178 Over 50 glycoforms of PrPC and PrPSc could be characterized with an increased number of tri- and tetra-antennary glycans found on PrPSc using hydrazinolysis, fluorescence labeling or acetylation of glycans and glycosidase digestion followed by mass spectrometry.
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This work was supported by research grants from the National Institutes of Health (AG02132 and NS14069), the Senator Jacob Javits Center of Excellence in Neuroscience (NS22786), the Swedish Medical Research Council (4515), and the State of California, Department of Health Services (8792062), as well as by gifts from the Sherman Fairchild Foundation and RJR/Nabisco, Inc.