Alzheimer’s disease is the most common cause of dementia, characterized by the progressive loss of memory. Learning about the pathology on a molecular level allowed me to further empathize with individuals that struggle with AD. The main culprits of AD are intracellular neurofibrillary tangles (NFTs ), composed of abnormally hyperphosphorylated Tau protein and extracellular senile plaques, consisting of amyloid-β (Aβ) peptides. The results of the disease are truly debilitating and eventually lethal.
Working with Dr. Shen ultimately taught me how to conduct and review elaborate research utilizing immunohistological staining methods to illustrate drug efficacy. If I continued to pursue the study, I would focus on the mechanism responsible for activation of passive immunization with monoclonal antibody 43D to gain a better understanding of how microglial cells can aid in eradicating Aβ pathology. It is also essential to study the intracellular interaction among Tau against 43D antibody so that the possible mechanism by which Tau pathology affects Aβ pathology may be further explained. Studies indicate that hyperphosphorylated Tau enhances the Aβ plaque load via a prion-like mechanism. Other research states that Aβ plaque load induces intracellular Tau accumulation. The study of extracellular Tau provides a conceivable treatment as well as a means to explore the mechanism behind inhibiting pathogenesis in AD.
Possible future work can also run similar experiments, ideally using more mice along with collecting and analyzing cerebrospinal-fluid to speculate whether the inhibition of Tau pathology observed by immunization with 43D was due to clearance of only extracellular or both intracellular and extracellular Tau. Ultimately, immunization with 43D prevents the seeding and propagation of Tau pathology as well as inhibits the promotion of Aβ pathology in 3 × Tg-AD mice.
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