کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1915962 | 1535198 | 2008 | 8 صفحه PDF | دانلود رایگان |

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 (PrPSc) 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 (PrPC) is much less clear. It is intriguing that PrPc 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 PrPC in the nervous system, as well as in lymphoid organs.
Journal: Journal of the Neurological Sciences - Volume 264, Issues 1–2, 15 January 2008, Pages 1–8