Graduation Date

5-2015

Document Type

Master's Thesis

Degree Name

Master of Science

Department or Program

Biological Sciences

Department or Program Chair

Maggie Louie, Ph.D.

First Reader

Varghese John, Ph.D.

Second Reader

Clare Peters-Libeu, Ph.D.

Third Reader

Maria Carranza, Ph.D.

Abstract

Alzheimer’s disease (AD) is the most common form of dementia, affecting over 5 million Americans. In AD patients there is a buildup of amyloid plaque in the brain, which contributes to AD symptoms. The main component of plaques is Amyloid-β (Aβ), a 40-42 length peptide formed from Amyloid-β Precursor Protein (APP) proteolysis. APP proteolysis can result in either anti-trophic or trophic peptides. Several APP polymorphisms exist that cause or protect against AD by altering APP proteolysis. Recently, more polymorphisms in the APP ectodomain have been discovered in patients with late onset AD (LOAD). The proteolysis of APP may be affected by these mutations, and we aim to determine their effect by measuring the levels of trophic and anti-trophic peptides produced in protein assays, Chinese Hamster Ovary (CHO) cells, and Human Embryonic Kidney (HEK) cells. We discovered that the N585Y APP polymorphism is likely to cause onset of LOAD through increased levels of anti-trophic peptides and decreased levels of trophic peptides.

Included in

Biology Commons

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