College of Arts & Sciences
Th e Interactions between Calcineurin and APP In January of 2011, President Barack Obama signed into law NAPAA, or the National Plan to Address Alzheimer’s Act, as a nationwide initiative to tackle the growing Alzheimer’s epidemic. Alzheimer’s Disease (AD) is a neurodegenerative disorder and the most common form of dementia. The disease manifests itself in the progressive deterioration of cognitive function. AD pathology is characterized by the accumulation of neurofibrillary tangles and amyloid-beta (A") plaques in the brains of affected patients. The amyloid cascade hypothesis suggests that processing of the amyloid precursor protein (APP) leads to the production of A" peptides, which then amass into oligomers and plaques. Consequently, the metabolism of APP has been the focus of intense research. Studies have shown that the protein phosphatase Calcineurin (CaN) affects certain AD phenotypes. Recently, our lab had found that the inhibition of CaN affects the phosphorylation state of APP and rescues certain AD phenotypes in transgenic fly models. In this study, we will further investigate the interaction between CaN and APP. Through the mutagenesis of phosphorylated residues and proposed CaN binding sites on APP, we will investigate the changes in phosphorylation and the subsequent effects on APP processing. 37
Da nielle Verghese COAS Biological Sciences
Dr . Alei st er Sa unders Faculty Mentor Biology
Poster Session B