BYU

Abstract by Joseph Creery

Personal Infomation


Presenter's Name

Joseph Creery

Degree Level

Undergraduate

Co-Authors

Russell Denton
John C. Price

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). Comparing transgenic mice (C57BL/6), expressing one of the three isoforms of human ApoE, we can observe differences in relative concentrations of proteins that do not directly interact with ApoE on a protein-protein level. The differences in protein concentrations of these seemingly unrelated proteins have been observed by others as well as ourselves. We hypothesize that there are systematic responses to the ApoE isoform differences to compensate for a lack of control in the ApoE dominion or subsection of the system. From protein turnover data, using newly developed mass spectrometry programs and deuterium labeling, we can determine whether a synthesis or degradation response is controlling the change of protein concentration for each of the proteins in the proteome that are detected. By focusing on a systems ability to control variables in its natural processes we can understand better why unrelated proteins are seen changing in concentration due to a genetic modification of ApoE isoforms.