Publication Date
2016
Document Type
Thesis
Committee Members
Paula Bubulya (Committee Member), Shulin Ju (Advisor), Mill Miller (Committee Member), Quan Zhong (Committee Member)
Degree Name
Master of Science (MS)
Abstract
Amyotrophic Lateral Sclerosis (ALS) is a neurodegenerative disorder that occurs due to the death of motor neurons and leads to paralysis and death within three to five years after symptoms present (Byrne et al., 2013). Superoxide Dismutase 1 (SOD1) was first identified to be associated with ALS in 1993. The objective of this study is to determine which proteins interact with wild type and mutant SOD1 and find any similarities or differences between them. ALS is attributed to a gain of toxicity, therefore abnormal protein interactions in mutant SOD1 are important. The results of this study will provide insight on the protein-protein interactions of SOD1, as well as how important these interactions are in association with ALS. Initially, the plan was to use yeast two-hybrid screening (Y2H) to identify the protein-protein interactions, then confirm the interactions with a pull down assay (immunoprecipitation). However, the Y2H was unable to obtain results. Instead, a combination of a pull-down assay and mass spectrometry were used to identify protein-protein interactions. Fifty one proteins were identified to interact exclusively with wild type SOD1 and thirteen proteins interacted with both wild type and A4V SOD1.
Page Count
72
Department or Program
Department of Biological Sciences
Year Degree Awarded
2016
Copyright
Copyright 2016, all rights reserved. My ETD will be available under the "Fair Use" terms of copyright law.
