Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE
Volume 1772, Issue 6, Pages 629-644Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbadis.2007.02.011
Keywords
prion; neurodegeneration; apoptosis; oxidative stress; copper; bax
Funding
- NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE [R01NS052526, R01NS040975] Funding Source: NIH RePORTER
- NINDS NIH HHS [R01 NS040975, NS052526, R01 NS040975-07, R01 NS052526-02, NS04691003, NS040975, R01 NS052526] Funding Source: Medline
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Prion diseases are caused by conversion of a normal cell-surface glycoprotein (PrPC) into a conformationally altered isoform (PrPSc) that is infectious in the absence of nucleic acid. Although a great deal has been learned about PrPSc and its role in prion propagation, much less is known about the physiological function of PrPC. In this review, we will summarize some of the major proposed functions for PrPC, including protection against apoptotic and oxidative stress, cellular uptake or binding of copper ions, transmembrane signaling, formation and maintenance of synapses, and adhesion to the extracellular matrix. We will also outline how loss or subversion of the cytoprotective or neuronal survival activities of PrPC might contribute to the pathogenesis of prion diseases, and how similar mechanisms are probably operative in other neurodegenerative disorders. (c) 2007 Elsevier B.V. All rights reserved.
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