| Autor: |
Yakubu UM; Department of Microbiology and Molecular Genetics, McGovern Medical School at UTHealth, Houston, TX USA.; MD Anderson UTHealth Graduate School at UTHealth, Houston, TX USA., Catumbela CSG; MD Anderson UTHealth Graduate School at UTHealth, Houston, TX USA.; Mitchell Center for Alzheimer's Disease and Related Brain Disorders, Department of Neurology, McGovern Medical School at UTHealth, Houston, TX USA., Morales R; Mitchell Center for Alzheimer's Disease and Related Brain Disorders, Department of Neurology, McGovern Medical School at UTHealth, Houston, TX USA.; Centro integrativo de biología y química aplicada (CIBQA), Universidad Bernardo O'Higgins, Santiago, Chile., Morano KA; Department of Microbiology and Molecular Genetics, McGovern Medical School at UTHealth, Houston, TX USA. |
| Abstrakt: |
Several neurodegenerative diseases of humans and animals are caused by the misfolded prion protein (PrP Sc ), a self-propagating protein infectious agent that aggregates into oligomeric, fibrillar structures and leads to cell death by incompletely understood mechanisms. Work in multiple biological model systems, from simple baker's yeast to transgenic mouse lines, as well as in vitro studies, has illuminated molecular and cellular modifiers of prion disease. In this review, we focus on intersections between PrP and the proteostasis network, including unfolded protein stress response pathways and roles played by the powerful regulators of protein folding known as protein chaperones. We close with analysis of promising therapeutic avenues for treatment enabled by these studies. |
