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Mannitol Reduces α‐Synuclein Aggregation in a Yeast Model of Parkinson’s Disease
Author(s) -
Pacheco Alissa Mercedes
Publication year - 2020
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2020.34.s1.03752
Subject(s) - alpha synuclein , protein aggregation , parkinson's disease , yeast , saccharomyces cerevisiae , microbiology and biotechnology , dopamine , programmed cell death , cell , disease , chemistry , biology , neuroscience , biochemistry , medicine , apoptosis
Parkinson’s Disease (PD) is an incurable, neurodegenerative disorder. This disorder is the second most common of its type and occurs by the accumulation of abnormal proteins called Lewy Bodies (LBs). LBs are found within the neurons of PD patients and trigger cell death. As a result of both damages and decreased neurons, dopamine levels decrease triggering common symptoms of the disease such as muscle stiffness, tremors, and slowed movements. Previous studies have revealed that the human protein alpha‐synuclein is one of the major components of Lewy Bodies. In the effort to better understand the relationship between both protein aggregation and cell death, a mechanism that overexpresses human alpha‐synuclein fused to GFP in the budding yeast Saccharomyces was derived. Our preliminary data suggests that the localization of the alpha synuclein protein is found in the cell membrane. Based upon other data, mannitol may alleviate the aggregation of alpha‐synuclein within the cell membrane of the yeast cells, suggesting a possible pharmacological intercession that may lower the amount of protein aggregation in PD.