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.
","abstract_html":"<p>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.</p>","abstract_has_math":false,"creators":["Mitsumori, Michael S."],"institution":null,"degree_name":"Master of Science","degree_level":"Master's Thesis","degree_discipline":"Biological Sciences","degree_department":null,"school":null,"contributors":["Varghese John, PhD","Clare Peters-Libeu, PhD","Maria Carranza, PhD"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-05-01T07:00:00Z","date_published":"2015-05-01T07:00:00Z","updated_at":"2026-07-24T02:04:35Z","subjects":["Alzheimer's","Amyloid","Mutation","Amyloid-β Precursor Protein","APP","late onset alzheimer's disease","Biology"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://scholar.dominican.edu/masters-theses/179","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Varghese John, PhD","Clare Peters-Libeu, PhD","Maria Carranza, PhD"]},{"key":"dc:creator","label":"Author","values":["Mitsumori, Michael S."]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["1970-01-01T08:00:00Z"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biological Sciences"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Master's Thesis"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Master of Science"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Alzheimer's","Amyloid","Mutation","Amyloid-β Precursor Protein","APP","late onset alzheimer's disease","Biology"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://scholar.dominican.edu/masters-theses/179"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["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.
"]},{"key":"dc:title","label":"Title","values":["Ectodomain Mutations Alter the Proteolysis of the Amyloid-β Precursor Protein (APP)"]}]}],"canonical_facts":{"dc:contributor":["Varghese John, PhD","Clare Peters-Libeu, PhD","Maria Carranza, PhD"],"dc:creator":["Mitsumori, Michael S."],"dc:date.available":["1970-01-01T08:00:00Z"],"dc:description.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.
"],"dc:identifier":["https://scholar.dominican.edu/masters-theses/179"],"dc:subject":["Alzheimer's","Amyloid","Mutation","Amyloid-β Precursor Protein","APP","late onset alzheimer's disease","Biology"],"dc:title":["Ectodomain Mutations Alter the Proteolysis of the Amyloid-β Precursor Protein (APP)"],"thesis:degree_discipline":["Biological Sciences"],"thesis:degree_level":["Master's Thesis"],"thesis:degree_name":["Master of Science"]},"updated_at":"2026-07-24T02:04:35Z"}