Regulation of APP Traffic and Processing by Arfs and MINTs
Richard Kahn, Ph.D.
Emory University
Atlanta, Georgia
2003 Investigator-Initiated Research Grant
The prime suspect in Alzheimer’s disease is the protein fragment beta-amyloid, clipped from the longer amyloid precursor protein (APP). Scientists are just now beginning to find clues to the role that APP normally plays in cells. Recent evidence suggests that APP may regulate the packaging of proteins at the Golgi complex, a cellular site where newly constructed proteins are given their final shape before transport to their appropriate cell destinations. APP, together with two proteins called MINT and Arf, appears to help package proteins into “delivery sacks.”
Richard Kahn and his colleagues will selectively interfere with MINT and Arf to find out how this affects the process of packaging proteins at the Golgi complex, and, by extension, what role APP plays in this process. In the first phase, experiments will be performed in connective tissue cells, which are simpler and easier to work with than brain cells. Any results from these cells will then be tested in brain cells. Understanding the normal role of APP is critical to ensure that any therapies designed to interfere with the beta-amyloid fragment do not also disrupt critical cell functions of APP.













