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Eukaryon

Class Year

2004

Keywords

neurodegenerative disease, proteins

Abstract

Recent research of neurodegenerative diseases has called attention to abnormal protein aggregates found in brain lesions. Alzheimer's disease (AD) and frontotemporal dementia with parkinsonism linked to chromosome 17 (FTDP-17) are part of a collective group of neurodegenerative diseases termed taupathies and are characterized by abnormal filamentous tau inclusions. Aβ amyloid plaques and neurofibrillary tangles containing hyperphosphorylated tau are invariant features of AD. The role of tau in AD pathogenesis is controversial. However, multiple tau mutations discovered in FTDP-17 add significance to tau's role in neurodegeneration. To study AD, our lab has identified different sites that become abnormally phosphorylated in adult tau and the potential role for dysfunctional phosphatases. To model FTDP-17, we and other labs have created transgenic mice that either overexpress wild type tau or express mutant tau. These mice develop clear neurodegenerative phenotypes. Analogous to tau aggregates, cytoplasmic inclusions known as Lewy bodies are characteristic of Parkinson's disease (PD). α-Synuclein has been linked to both familial and sporadic PD. Following this discovery, our lab has demonstrated that aggregated α-synuclein appears in Lewy bodies of human patients. Transgenic mice and Drosophila models expressing α-synuclein are being used to identify suppressors and enhancers of disease. Investigating the role of tau and α-synuclein in neurodegenerative diseases can aid in the development of effective treatments.

Disclaimer

Eukaryon is published by students at Lake Forest College, who are solely responsible for its content. The views expressed in Eukaryon do not necessarily reflect those of the College. Articles published within Eukaryon should not be cited in bibliographies. Material contained herein should be treated as personal communication and should be cited as such only with the consent of the author.

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