Functional Roles of Amyloid Precursor Protein as Signaling Molecule of Histone Modification in Alzheimer's Disease
Alzheimer’s disease (AD) is a progressive neurodegenerative disorder. It was hypothesized that the abnormal
cleavage of amyloid precursor proteins (APP) to highly insoluble beta amyloid peptides (Αβ) form plaques in the brain,
causing neurodegeneration. Recently, it has been shown that epigenetic changes such as histone modification is associated
with the APP pathway in AD. Therefore, the present study aimed to determine protein expression of different histone
modifications in APP-overexpressing human embryonic kidney cells 293 (HEK293T cells).HEK293T cells were transfected
with hAPP plasmid to overexpress APP. Dot blot was performed using the APP-overexpressed cells to determine the protein
expression of acetylated and total histones (H2A, H2B, H3 and H4).Results show a significant decrease of acetyl-histone
H2A (Lys 5) in APP-overexpressed HEK293T cells when compared to its control group. The finding suggests that acetylhistone
H2A (Lys 5) is involved in an AD-associated APP pathway.
Keywords - Alzheimer’s Disease, Amyloid Precursor Protein, Histone Modification.