Effect of a serine protease on neurodegeneration using Alzheimer’s fly model
Presentation Type
Poster
Full Name of Faculty Mentor
Fang Ju Lin, Biology
Major
Biochemistry
Presentation Abstract
Alzheimer’s is a disease that leads to memory impairment and eventually the inability to carry-out daily tasks. Drosophila melanogaster, or fruit flies, are used in this study as their genome is 60% homologous to that of humans, and about 75% of the genes responsible for human genes have homologs in flies. This allows fruit flies to be eligible in the study of complex pathways relevant in biomedical research. This study utilized Amyloid-β peptides which are the makeup of plaques that clump between the neurons and disrupt cell signaling. The peptides form from a cleavage of larger peptides, human Amyloid-β peptide 42 (Aβ 42), was produced in transgenic flies. This study analyzed the phenotypes of transgenic Drosophila model of amyloid β (Aβ) toxicity. This was tested through trials of climbing assays and lifespan of the flies. Our preliminary data showed that knockdown of a serine protease rescued the behavioral phenotype. In addition, the morphology of the Alzheimer’s fly brains was documented using histological techniques to assess degree of neurodegeneration.
Start Date
12-4-2023 4:00 PM
End Date
12-4-2023 6:00 PM
Disciplines
Biochemistry | Biology
Recommended Citation
Brown, Mallorie; McCrea, Elizabeth; and McCutcheon, Hannah, "Effect of a serine protease on neurodegeneration using Alzheimer’s fly model" (2023). Undergraduate Research Competition. 86.
https://digitalcommons.coastal.edu/ugrc/2023/fullconference/86
Effect of a serine protease on neurodegeneration using Alzheimer’s fly model
Alzheimer’s is a disease that leads to memory impairment and eventually the inability to carry-out daily tasks. Drosophila melanogaster, or fruit flies, are used in this study as their genome is 60% homologous to that of humans, and about 75% of the genes responsible for human genes have homologs in flies. This allows fruit flies to be eligible in the study of complex pathways relevant in biomedical research. This study utilized Amyloid-β peptides which are the makeup of plaques that clump between the neurons and disrupt cell signaling. The peptides form from a cleavage of larger peptides, human Amyloid-β peptide 42 (Aβ 42), was produced in transgenic flies. This study analyzed the phenotypes of transgenic Drosophila model of amyloid β (Aβ) toxicity. This was tested through trials of climbing assays and lifespan of the flies. Our preliminary data showed that knockdown of a serine protease rescued the behavioral phenotype. In addition, the morphology of the Alzheimer’s fly brains was documented using histological techniques to assess degree of neurodegeneration.