Tissue Transglutaminase is Not Involved in the Aggregate Formation of Stably Expressed $alpha$-Synuclein in SH-SY5Y Human Neuroblastoma Cells

Suh, Myung-Duk; Park, Chang-Ha; Kim, Sung-Soo; Kil, Myeng-Og; Lee, Geon-Hee; Johnson, Gail V. W.; Chun, Wan-Joo

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자료유형: 학술저널

저자정보: Suh, Myung-Duk (Department of Pharmacology, College of Medicine, Kangwon National University) Park, Chang-Ha (Department of Pharmacology, College of Medicine, Kangwon National University) Kim, Sung-Soo (Department of Pharmacology, College of Medicine, Kangwon National University) Kil, Myeng-Og (Department of Pharmacology, College of Medicine, Kangwon National University) Lee, Geon-Hee (Department of Pharmacology, College of Medicine, Kangwon National University) Johnson, Gail V. W. (Department of Pharmacology, College of Medicine, Kangwon National University) Chun, Wan-Joo (Department of Psychiatry, University of Alabama at Birmingham)

저널정보: 대한약학회 Archives of pharmacal research : a publication of the Pharmaceutical Society of Korea Archives of pharmacal research : a publication of the Pharmaceutical Society of Korea 제27권 제8호

발행연도: 2004.1

수록면: 850 - 856 (7page)

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Intraneuronal deposition containing $\alpha$-synuclein is implicated in the pathogenesis of synuclein-opathies including Parkinsons disease (PD). Although it has been demonstrated that cytoplas-mic inclusions of wild type $\alpha$-synuclein are observed in the brain of PD patients and that $\alpha$-synuclein mutations such as A30P and A53T accelerate aggregate formation, the exact mech-anism by which $\alpha$-synuclein forms insoluble aggregates is still controversial. In the present study, to understand the possible involvement of tissue transglutaminase (tTG) in aggregate formation of $\alpha$-synuclein, SH-SY5Y cell lines stably expressing wild type or mutant (A30P or A53T) $\alpha$-synuclein were created and aggregate formation of $\alpha$-synuclein was observed upon activation of tTG. The data demonstrated that $\alpha$-synuclein negligibly interacted with tTG and that activation of tTG did not result in the aggregate formation of $\alpha$-synuclein in SH-SY5Y cells overexpressing either wild type or mutant $\alpha$-synuclein. In addition, $\alpha$-synuclein was not modi-fied by activated tTG in situ. These data suggest that tTG is unlikely to be a contributing factor to the formation of aggregates of $\alpha$-synuclein in a stable cell model.

#Tissue transglutaminase #tTG #${alpha}-Synuclein #Inclusion$ #A30P #A53T #SH-SY5Y human neuroblastoma

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