Prion proteins: physiological functions and role in neurological disorders.
Stanley Prusiner was the first to promote the concept of misfolded proteins as a cause for neurological disease. It has since been shown by him and other investigators that the scrapie isoform of prion protein (PrP(Sc)) functions as an infectious agent in numerous human and non-human disorders of the central nervous system (CNS). Interestingly, other organ systems appear to be less affected, and do not appear to lead to major co-morbidities. The physiological function of the endogenous cellular form of the prion protein (PrP(C)) is much less clear. It is intriguing that PrP(c) is expressed on most tissues in mammals, suggesting not only biological functions outside the CNS, but also a role other than the propagation of its misfolded isotype. In this review, we summarize accumulating in vitro and in vivo evidence regarding the physiological functions of PrP(C) in the nervous system, as well as in lymphoid organs.
Hu
Wei
W
Department of Neurology, University of Texas Southwestern Medical Center at Dallas, TX 75390-9036, United States.
Kieseier
Bernd
B
Frohman
Elliot
E
Eagar
Todd N
TN
Rosenberg
Roger N
RN
Hartung
Hans-Peter
HP
Stüve
Olaf
O
D000818:Animals; D001928:Brain Diseases, Metabolic / Q000378:metabolism / Q000503:physiopathology; D002490:Central Nervous System / Q000378:metabolism* / Q000503:physiopathology; D006801:Humans; D007107:Immune System / Q000378:metabolism / Q000503:physiopathology; D007154:Immune System Diseases / Q000276:immunology / Q000378:metabolism / Q000503:physiopathology; D019636:Neurodegenerative Diseases / Q000378:metabolism* / Q000503:physiopathology; D018621:PrPC Proteins / Q000378:metabolism; D018620:PrPSc Proteins / Q000378:metabolism; D017096:Prion Diseases / Q000378:metabolism* / Q000503:physiopathology; D011328:Prions / Q000378:metabolism*
D018621:PrPC Proteins; D018620:PrPSc Proteins; D011328:Prions