Abstract
Intraneuronal deposition containing α-synuclein is implicated in the pathogenesis of synucleinopathies including Parkinsons disease (PD). Although it has been demonstrated that cytoplasmic inclusions of wild type α-synuclein are observed in the brain of PD patients and that α-synuclein mutations such as A30P and A53T accelerate aggregate formation, the exact mechanism by which α-synuclein forms insoluble aggregates is still controversial. In the present study, to understand the possible involvement of tissue transglutaminase (tTG) in aggregate formation of a-synuclein, SH-SY5Y cell lines stably expressing wild type or mutant (A30P or A53T) a-synuclein were created and aggregate formation of α-synuclein was observed upon activation of tTG. The data demonstrated that a-synuclein negligibly interacted with tTG and that activation of tTG did not result in the aggregate formation of a-synuclein in SH-SY5Y cells overexpressing either wild type or mutant a-synuclein. In addition, a-synuclein was not modified by activated tTGin situ. These data suggest that tTG is unlikely to be a contributing factor to the formation of aggregates of α-synuclein in a stable cell model.
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Suh, MD., Park, CH., Kim, SS. et al. Tissue transglutaminase is not involved in the aggregate formation of stably expressed α-synuclein in sh-sy5y human neuroblastoma cells. Arch Pharm Res 27, 850–856 (2004). https://doi.org/10.1007/BF02980178
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DOI: https://doi.org/10.1007/BF02980178