| Autor: |
Choi, Yeon Joo, Yeo, Hyeon Ji, Shin, Min Jea, Youn, Gi Soo, Park, Jung Hwan, Yeo, Eun Ji, Kwon, Hyun Jung, Lee, Lee Re, Kim, Na Yeon, Kwon, Su Yeon, Kim, Su Min, Kim, Dae Won, Jung, Hyo Young, Kwon, Oh-Shin, Lee, Chan Hee, Park, Jong Kook, Lee, Keun Wook, Han, Kyu Hyung, Park, Jinseu, Eum, Won Sik |
| Předmět: |
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| Zdroj: |
Biomedicines; Mar2023, Vol. 11 Issue 3, p836, 12p |
| Abstrakt: |
Glutathione S-transferase pi (GSTpi) is a member of the GST family and plays many critical roles in cellular processes, including anti-oxidative and signal transduction. However, the role of anti-oxidant enzyme GSTpi against dopaminergic neuronal cell death has not been fully investigated. In the present study, we investigated the roles of cell permeable Tat-GSTpi fusion protein in a SH-SY5Y cell and a Parkinson's disease (PD) mouse model. In the 1-methyl-4-phenylpyridinium (MPP+)-exposed cells, Tat-GSTpi protein decreased DNA damage and reactive oxygen species (ROS) generation. Furthermore, this fusion protein increased cell viability by regulating MAPKs, Bcl-2, and Bax signaling. In addition, Tat-GSTpi protein delivered into the substantia nigra (SN) of mice brains protected dopaminergic neuronal cell death in the 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)-induced PD animal model. Our results indicate that the Tat-GSTpi protein inhibited cell death from MPP+- and MPTP-induced damage, suggesting that it plays a protective role during the loss of dopaminergic neurons in PD and that it could help to identify the mechanism responsible for neurodegenerative diseases, including PD. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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