BYU

Abstract by Joseph Creery

Personal Infomation


Presenter's Name

Joseph Creery

Co-Presenters

None

Degree Level

Undergraduate

Co-Authors

None

Abstract Infomation


Department

Chemistry and Biochemistry

Faculty Advisor

John Price

Title

Identifying ApoE isoform dependent changes for protein turnover in the brain

Abstract

It is known that a significant contributor to proteopathy in late-onset Alzheimer’s disease (AD) is the genetic variation of Apolipoprotein E (ApoE). Although this is known that many specific protein-protein interactions contribute to proteopathy in AD, there is no clear picture of total protein homeostasis and turnover in the presence of the different isoforms of ApoE. For AD, being an age-related disease, this is critical information. Labeling transgenic mice with deuterated water, expressing one of the three isoforms of human ApoE, we can see the effects APOE has on protein turnover within the brain tissue. We are progressing toward an overall proteopathy picture, tissue wide, of protein turnover and homeostasis in the presence of ApoE isoform differences.