Prion protein glycosylation
نویسندگان
چکیده
منابع مشابه
Prion protein glycosylation is not required for strain-specific neurotropism.
In this study, we tested the hypothesis that the glycosylation of the pathogenic isoform of the prion protein (PrP(Sc)) might encode the selective neurotropism of prion strains. We prepared unglycosylated cellular prion protein (PrP(C)) substrate molecules from normal mouse brain by treatment with PNGase F and used reconstituted serial protein cyclic misfolding amplification reactions to produc...
متن کاملGlycosylation differences between the normal and pathogenic prion protein isoforms.
Prion protein consists of an ensemble of glycosylated variants or glycoforms. The enzymes that direct oligosaccharide processing, and hence control the glycan profile for any given glycoprotein, are often exquisitely sensitive to other events taking place within the cell in which the glycoprotein is expressed. Alterations in the populations of sugars attached to proteins can reflect changes cau...
متن کاملDistance of sequons to the C-terminus influences the cellular N-glycosylation of the prion protein.
Cell-specific differences in the utilization of the two N-glycosylation sequons (Asn180-Ile-Thr and Asn196-Phe-Thr) of the prion protein (PrP) have been proposed to influence the aetiology of the neurodegenerative prion diseases. As the N-glycosylation of PrP is ablated by deletion of the C-terminal glycosyl-phosphatidylinositol (GPI) anchor signal sequence, we have investigated the determinant...
متن کاملBlockade of glycosylation promotes acquisition of scrapie-like properties by the prion protein in cultured cells.
The conformational conversion of the prion protein, a sialoglycoprotein containing two N-linked oligosaccharide chains, from its normal form (PrPC) to a pathogenic form (PrPSc) is the central causative event in prion diseases. Although PrPSc can be generated in the absence of glycosylation, there is evidence that oligosaccharide chains may modulate the efficiency of the conversion process, and ...
متن کاملGlycosylation modification of human prion protein provokes apoptosis in HeLa cells in vitro.
We investigate the correlation between the glycosylation modified prion proteins and apoptosis. The wild-type PRNP gene and four PRNP gene glycosylated mutants were transiently expressed in HeLa cells. The effect of apoptosis induced by PrP mutants was confirmed by MTT assay, Hochest staining, Annexin-V staining and PI staining. ROS test detected ROS generation within the cells. The mitochondri...
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ژورنال
عنوان ژورنال: Journal of Neurochemistry
سال: 2005
ISSN: 0022-3042,1471-4159
DOI: 10.1111/j.1471-4159.2005.03104.x