Current Molecular Medicine

David W. Li  
College of Medicine
University of Nebraska Medical Center
Omaha, NE


Stressing Out the ER: A Role of the Unfolded Protein Response in Prion-Related Disorders

Author(s): Claudio A. Hetz and Claudio Soto

Affiliation: Harvard School of Public Health, Department of Immunology and Infectious Diseases, FXB Building, Room 205, 653 Huntington Avenue Boston, MA 02115, USA.

Keywords: Prion related disorders, apoptosis, PrPSC, proteasome, ER stress, glucose-regulated proteins, caspase-12, PrPSC-like, aggresomes


Transmissible Spongiform Encephalopathies are fatal and infectious neurodegenerative diseases characterized by extensive neuronal apoptosis and the accumulation of an abnormally folded form of the cellular prion protein (PrP), denoted PrPSC. Compelling evidence suggests the involvement of several signaling pathways in prion pathogenesis, including proteasome dysfunction, alterations in the protein maturation pathways and the unfolded protein response. Recent reports indicate that endoplasmic reticulum stress due to the PrP misfolding may be a critical factor mediating neuronal dysfunction in prion diseases. These findings have applications for developing novel strategies for treatment and early diagnosis of transmissible spongiform encephalopathies and other neurodegenerative diseases.

Order Reprints Order Eprints Rights & PermissionsPrintExport

Article Details

Page: [37 - 43]
Pages: 7
DOI: 10.2174/156652406775574578