Lake Forest College, Lake Forest, IL 60045
Parkinson’s Disease (PD) is a neurodegenerative disease characterized by the loss of midbrain neurons. The misfolding and aggregation of α-synuclein is thought to kill these neurons. Thus, finding ways to curb or prevent α-synuclein misfolding may have therapeutic potential in treating PD. Chaperones are proteins that help other proteins fold and heat shock proteins (Hsp) are specific stress-activated chaperones. An attractive hypothesis is that Hsps can prevent α-synuclein misfolding, and therefore, toxicity. I focused on two members of this large and diverse family, Hsp26 and Hsp42. I used yeast as the model system to evaluate if the absence of either of these chaperones would increase α-synuclein aggregation and/or toxicity. My results indicate that absence of Hsp26 increased α-synuclein-dependent toxicity without increasing aggregation, but this toxicity was specific to only one mutant, and not all forms, of α-synuclein. In the future, I plan to test the effects of other chaperones on α-synuclein aggregation and toxicity in PD.
N.Wang’s research was funded by Lake Forest College Richter apprentice scholar fund and a NIH R15 AREA grant.
[Abstract (DOC)]