Okadaic acid stimulates the formation of α-synuclein aggregates through calcium- and transglutaminase-associated signaling pathway

Title
Okadaic acid stimulates the formation of α-synuclein aggregates through calcium- and transglutaminase-associated signaling pathway
Authors
OH, YIm, E임혜원Kim, Y정광철
Keywords
α-synuclein; okadaic acid; aggregate
Issue Date
2010-11
Publisher
40th Annual Meeting Neuroscience 2010
Abstract
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.
URI
http://pubs.kist.re.kr/handle/201004/39114
Appears in Collections:
KIST Publication > Conference Paper
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