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Eukaryon

Class Year

Arun George Paul '05

Ruja Shrestha '07

Keywords

Parkinson's Disease, α-synuclein misfolding

Abstract

Parkinson disease (PD) is caused by α-synuclein misfolding in the substantia nigra par compacta cells of the brain. A recent study (Willingham et. al., 2003) demonstrated that over-expression of wild type (WT) α-synuclein in STP2 deletion (STP2Δ) S. cerevisiae strains is toxic. Surprisingly, we did not observe any toxicity in 4741 (parent strain) and STP2Δ strains over-expressing WT α-synuclein or its mutant forms. Moreover, GFP microscopy of α-synuclein in STP2Δ strains showed phenotypes observed in strains with STP2. We observed halos for strains over-expressing WT α-synuclein and the A53T mutant. α-Synuclein was cytoplasmic for strains with the A30P mutant and the A30P/A53T double mutant. Western analysis demonstrated that neither the levels of α-synuclein expression nor the levels of GAPDH, a pro-apoptotic protein changed in STP2Δ strains. Furthermore, genetic deletion of GAPDH did not show any enhanced growth in strains that overexpressed α-synuclein. The lack of α-synuclein toxicity in STP2Δin our study may be due to our use of a different overexpression system, which did not yield amounts high enough to overwhelm protein quality-control systems and yield the toxicity that underlies PD pathogenesis (Berke, 2003) of the cell.

ArunPaul.pps (3197 kB)
PowerPoint Seminar

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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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