Interactions between Calcium and Alpha-Synuclein in Neurodegeneration
AbstractIn Parkinson’s disease and some atypical Parkinson’s syndromes, aggregation of the α-synuclein protein (α-syn) has been linked to neurodegeneration. Many triggers for pathological α-syn aggregation have been identified, including port-translational modifications, oxidative stress and raised metal ions, such as Ca2+. Recently, it has been found using cell culture models that transient increases of intracellular Ca2+ induce cytoplasmic α-syn aggregates. Ca2+-dependent α-syn aggregation could be blocked by the Ca2+ buffering agent, BAPTA-AM, or by the Ca2+ channel blocker, Trimethadione. Furthermore, a greater proportion of cells positive for aggregates occurred when both raised Ca2+ and oxidative stress were combined, indicating that Ca2+ and oxidative stress cooperatively promote α-syn aggregation. Current on-going work using a unilateral mouse lesion model of Parkinson’s disease shows a greater proportion of calbindin-positive neurons survive the lesion, with intracellular α-syn aggregates almost exclusively occurring in calbindin-negative neurons. These and other recent findings are reviewed in the context of neurodegenerative pathologies and suggest an association between raised Ca2+, α-syn aggregation and neurotoxicity. View Full-Text
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Rcom-H'cheo-Gauthier, A.; Goodwin, J.; Pountney, D.L. Interactions between Calcium and Alpha-Synuclein in Neurodegeneration. Biomolecules 2014, 4, 795-811.
Rcom-H'cheo-Gauthier A, Goodwin J, Pountney DL. Interactions between Calcium and Alpha-Synuclein in Neurodegeneration. Biomolecules. 2014; 4(3):795-811.Chicago/Turabian Style
Rcom-H'cheo-Gauthier, Alex; Goodwin, Jacob; Pountney, Dean L. 2014. "Interactions between Calcium and Alpha-Synuclein in Neurodegeneration." Biomolecules 4, no. 3: 795-811.