title: Metabolism of minor isoforms of prion proteins: Cytosolic prion protein and transmembrane prion protein.
abstract: Transmissible spongiform encephalopathy or prion disease is triggered by the conversion from cellular prion protein to pathogenic prion protein. Growing evidence has concentrated on prion protein configuration changes and their correlation with prion disease transmissibility and pathogenicity. In vivo and in vitro studies have shown that several cytosolic forms of prion protein with specific topological structure can destroy intracellular stability and contribute to prion protein pathogenicity. In this study, the latest molecular chaperone system associated with endoplasmic reticulum-associated protein degradation, the endoplasmic reticulum resident protein quality-control system and the ubiquitination proteasome system, is outlined. The molecular chaperone system directly correlates with the prion protein degradation pathway. Understanding the molecular mechanisms will help provide a fascinating avenue for further investigations on prion disease treatment and prion protein-induced neurodegenerative diseases.
authors.affiliation: State Key Laboratory for Agrobiotechnology, National Animal Transmissible Spongiform Encephalopathy Laboratory, College of Veterinary Medicine, China Agricultural University, Beijing 100193, China.
authors.forename: Zhiqi
authors.initials: Z
authors.lastname: Song
authors.affiliation: State Key Laboratory for Agrobiotechnology, National Animal Transmissible Spongiform Encephalopathy Laboratory, College of Veterinary Medicine, China Agricultural University, Beijing 100193, China.
authors.forename: Deming
authors.initials: D
authors.lastname: Zhao
authors.affiliation: State Key Laboratory for Agrobiotechnology, National Animal Transmissible Spongiform Encephalopathy Laboratory, College of Veterinary Medicine, China Agricultural University, Beijing 100193, China.
authors.forename: Lifeng
authors.initials: L
authors.lastname: Yang
keywords: cytosolic form of prion protein; metabolism; molecular chaperone; molecular mechanism; neural regeneration; neurodegeneration; neuroregeneration; prion protein; protein degeneration; transmembrane form of prion protein; ubiquitination