Date of Award


Publication Type

Master Thesis

Degree Name



Chemistry and Biochemistry


Chemistry, Biochemistry.




Protein disulfide isomerase (PDI) is a multifunctional protein most well characterized for its ability to form and exchange disulfide bonds (Darby et al., 1996). The localization of PDI in differentiated human neuroblastoma SH-SY5Y cells was probed by the development of a recombinant fusion protein between green fluorescent protein GFP and PDI. SH-SY5Y cells expressing the recombinant reporter protein were also exposed to oxidative and ischemic stress, and examined for characteristics of apoptosis. These cells demonstrated that PDI provides a significant decrease in apoptotic traits as compared to the control cells. It was observed that there was reduced nuclear condensation, and maintenance of mitochondrial membrane potential. Cells containing the recombinant protein also showed an increased number of viable cells when exposed to hypoxic stress. These results suggest that PDI plays a role in the protective mechanism towards cellular stress. Excessive neuronal loss induced by oxidative stress is often seen in patients due to aging, strokes, and neurodegenerative diseases. (Abstract shortened by UMI.)Dept. of Chemistry and Biochemistry. Paper copy at Leddy Library: Theses & Major Papers - Basement, West Bldg. / Call Number: Thesis2005 .S47. Source: Masters Abstracts International, Volume: 44-03, page: 1370. Thesis (M.Sc.)--University of Windsor (Canada), 2005.