title: Prion protein biosynthesis and its emerging role in neurodegeneration.
abstract: Various fatal neurodegenerative disorders are caused by altered metabolism of the prion protein (PrP). These diseases are typically transmissible by an unusual 'protein-only' mechanism in which a misfolded isomer, PrP(Sc), confers its aberrant conformation onto normal cellular PrP. An impressive range of studies has investigated nearly every aspect of this fascinating event; yet, our understanding of how PrP(Sc) accumulation might lead to cellular dysfunction and neurodegeneration is trifling. Recent advances in our understanding of normal PrP biosynthesis and degradation might have unexpectedly shed new light on this complex problem. Indeed, our current understanding of normal PrP cell biology, coupled with a growing appreciation of its complex metabolism, is providing new hypotheses for PrP-mediated neurodegeneration.
authors.affiliation: Cell Biology and Metabolism Program, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.
authors.forename: Oishee
authors.initials: O
authors.lastname: Chakrabarti
authors.forename: Aarthi
authors.initials: A
authors.lastname: Ashok
authors.forename: Ramanujan S
authors.initials: RS
authors.lastname: Hegde
mesh_terms: D000818:Animals; D006801:Humans; D051379:Mice; D008822:Mice, Transgenic; D008954:Models, Biological; D008962:Models, Theoretical; D009410:Nerve Degeneration / Q000378:metabolism; D019636:Neurodegenerative Diseases / Q000378:metabolism* / Q000503:physiopathology; D018620:PrPSc Proteins / Q000096:biosynthesis* / Q000737:chemistry*; D017096:Prion Diseases / Q000503:physiopathology / Q000635:transmission; D011328:Prions / Q000737:chemistry; D014176:Protein Biosynthesis; D020033:Protein Isoforms
chemical_list: D018620:PrPSc Proteins; D011328:Prions; D020033:Protein Isoforms