sciencesconf.org:neurophdmeeting:97106

Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease characterized by the selective degeneration of both upper and lower motor neurons. Causes of disease remain still unknown, although protein aggregate formation in motor neurons is a neuropathological hallmark. These aggregates contain several different proteins, but transactivation response (TAR) DNA-binding protein (TDP-43) is considered the major component. Recent evidences showed that TDP-43 is degraded not only by the ubiquitin proteasome system (UPS) and macroautophagy, but also by the chaperone-mediated autophagy (CMA) through an interaction between the cytosolic chaperone heat shock cognate 70 (Hsc70, also known as HSPA8) and ubiquitylated TDP-43. We assessed the two principal parameters of CMA in easily accessible cells like peripheral blood mononuclear cells (PBMCs) obtained from 30 sporadic ALS patients (sALS), 9 ALS patients carrying mutations in…


Link to Full Article: sciencesconf.org:neurophdmeeting:97106

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