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2006 Grant - Parent
Role of Cell Adhesion Molecules in Presenilin Animal Models
Angele Parent, Ph.D.
University of Chicago
2006 Investigator-Initiated Research Grant
Some rare, inherited forms of Alzheimer's disease are caused by mutations in a protein called presenilin, an enzyme that regulates production of a small protein fragment called beta-amyloid. Presenilin helps to chop beta-amyloid from its parent molecule, amyloid precursor protein. Because beta-amyloid is toxic to neurons, it is thought to be a major trigger in all types of Alzheimer's disease, inherited or not. However, presenilin chops up other proteins, too-a phenomenon that has led many researchers to question if those targets may also be related to the disease process.
Angele Parent, Ph.D., has proposed to examine the relationship between other targets of presenilin and Alzheimer's disease. Parent plans to focus on a group of presenilin targets called cell adhesion molecules. These are proteins that are present on the cell surface and that mediate cell-to-cell contact, or adhesion. In neurons, some of these proteins are concentrated in synapses, specialized junctions that facilitate communication between neurons. Failure of these synapses contributes to memory loss and is thought to be one of the earliest manifestations of Alzheimer's disease.
Parent will determine if presenilin is involved in the processing of cell adhesion molecules and if it plays any role in the regulation of synapse activity. These studies will lead to a fuller understanding of the role of presenilin and presenilin gene mutations in Alzheimer's disease, and the research findings could spur the development of new therapeutic strategies for treating the disease.