Journal
PRION
Volume 1, Issue 2, Pages 83-93Publisher
TAYLOR & FRANCIS INC
DOI: 10.4161/pri.1.2.4346
Keywords
transmissible spongiform encephalopathy; amyloid; PrP
Categories
Funding
- Ellison Medical Research Foundation
- U. S. Department of Defense
- NIH
- European Union (TSEUR)
- Swiss National Foundation
- Ernst-Jung Foundation
- National Competence Center for Research on Neural Plasticity and Repair
Ask authors/readers for more resources
The key pathogenic event in prion disease involves misfolding and aggregation of the cellular prion protein (PrP). Beyond this fundamental observation, the mechanism by which PrP misfolding in neurons leads to injury and death remains enigmatic. Prion toxicity may come about by perverting the normal function of PrP. If so, understanding the normal function of PrP may help to elucidate the molecular mechansim of prion disease. Ablation of the Prnp gene, which encodes PrP, was instrumental for determining that the continuous production of PrP is essential for replicating prion infectivity. Since the structure of PrP has not provided any hints to its possible function, and there is no obvious phenotype in PrP KO mice, studies of PrP function have often relied on intuition and serendipity. Here, we enumerate the multitude of phenotypes described in PrP deficient mice, many of which manifest themselves only upon physiological challenge. We discuss the pleiotropic phenotypes of PrP deficient mice in relation to the possible normal function of PrP. The critical question remains open: which of these phenotypes are primary effects of PrP deletion and what do they tell us about the function of PrP?
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available