Okadaic acid stimulates the formation of α-synuclein aggregates through calcium- and transglutaminase-associated signaling pathway
- Okadaic acid stimulates the formation of α-synuclein aggregates through calcium- and transglutaminase-associated signaling pathway
- OH, Y; Im, E; 임혜원; Kim, Y; 정광철
- α-synuclein; okadaic acid; aggregate
- Issue Date
- 40th Annual Meeting Neuroscience 2010
- Parkinson's disease (PD) is characterized by the specific loss of dopaminergic neurons from the substantia nigra, and the formation of filamentous inclusion bodies called Lewy bodies. One of the PD-associated genes, α-synuclein (α-Syn), is an unstructured soluble protein that can aggregate to form insoluble fibrils in pathological conditions. In the present study we found that α-Syn aggregate formation is highly induced by a specific inhibitor of phosphoserine/threonine protein phosphatase 1 and 2a, okadaic acid (OA), in a dose- and time-dependent manner. Interestingly, OA-induced α-Syn aggregate formation was not altered by the mutation of various phosphorylation sites within α-Synuclein. In addition, OA-induced aggregate formation of α-Syn was enhanced by transglutaminase or calcium ionophore A23187. Taken together, these data suggest that OA induces enhanced α-Syn aggregation through calcium and/or transglutaminase-associated signaling pathway. However, this effect seems not to be dependent upon the phosphorylation state of α-Syn or via calcium/calmodulin-dependent protein kinase II (CaMKII) pathway. The detailed data will be presented at the meeting.
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