Full metadata record
DC Field | Value | Language |
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dc.contributor.author | 이영한 | - |
dc.date.accessioned | 2021-01-20T05:24:33Z | - |
dc.date.available | 2021-01-20T05:24:33Z | - |
dc.date.issued | 2002-04 | - |
dc.identifier.citation | JOURNAL OF BIOLOGICAL CHEMISTRY, v. 277, issue. 4, page. 12334-12342 | en_US |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | https://www.sciencedirect.com/science/article/pii/S0021925818520627?via%3Dihub | - |
dc.identifier.uri | https://repository.hanyang.ac.kr/handle/20.500.11754/157249 | - |
dc.description.abstract | α-Synuclein has been implicated in the pathogenesis of many neurodegenerative diseases, including Parkinson's disease and Alzheimer's disease. Although the function of α-synuclein remains largely unknown, recent studies have demonstrated that this protein can interact with phospholipids. To address the role of α-synuclein in neurodegenerative disease, we have investigated whether it binds phospholipase D (PLD) and affects PLD activity in human embryonic kidney (HEK)-293 cells overexpressing wild type α-synuclein or the mutant forms of α-synuclein (A53T, A30P) associated with Parkinson's disease. Tyrosine phosphorylation of α-synuclein appears to play a modulatory role in the inhibition of PLD, because mutation of Tyr125 to Phe slightly increases inhibitory effect of α-synuclein on PLD activity. Treatment with pervanadate or phorbol myristate acetate inhibits PLD more in HEK 293 cells overexpressing α-synuclein than in control cells. Binding of α-synuclein to PLD requires phox and pleckstrin homology domain of PLD and the amphipathic repeat region and non-Aβ component of α-synuclein. Although biologically important, co-transfection studies indicate that the interaction of α-synuclein with PLD does not influence the tendency of α-synuclein to form pathological inclusions. These results suggest that the association of α-synuclein with PLD, and modulation of PLD activity, is biologically important, but PLD does not appear to play an essential role in the pathophysiology of α-synuclein. | en_US |
dc.language.iso | en_US | en_US |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | en_US |
dc.title | α-Synuclein Interacts with Phospholipase D Isozymes and Inhibits Pervanadate-induced Phospholipase D Activation in Human Embryonic Kidney-293 Cells | en_US |
dc.type | Article | en_US |
dc.identifier.doi | 10.1074/jbc.M110414200 | - |
dc.relation.journal | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.contributor.googleauthor | Ahn, Bong-Hyun | - |
dc.contributor.googleauthor | Rhim, Hyangshuk | - |
dc.contributor.googleauthor | Kim, Shi Yeon | - |
dc.contributor.googleauthor | Sung, Young-Mo | - |
dc.contributor.googleauthor | Lee, Mun-Yong | - |
dc.contributor.googleauthor | Choi, Ju-Youn | - |
dc.contributor.googleauthor | Wolozine, Benjamin | - |
dc.contributor.googleauthor | Chang, Jong-Soo | - |
dc.contributor.googleauthor | Lee, Young Han | - |
dc.contributor.googleauthor | Kwon, Taeg Kyu | - |
dc.contributor.googleauthor | Chung, KwangChul | - |
dc.contributor.googleauthor | Yoon, Shin-Hee | - |
dc.contributor.googleauthor | Hahn, Sang June | - |
dc.contributor.googleauthor | Kim, Myung-Suk | - |
dc.contributor.googleauthor | Joa, Yang-Hyeok | - |
dc.contributor.googleauthor | Min, Do Sik | - |
dc.relation.code | 2009204730 | - |
dc.sector.campus | E | - |
dc.sector.daehak | COLLEGE OF SCIENCE & TECHNOLOGY[E] | - |
dc.sector.department | DIVISION OF MOLECULAR & LIFE SCIENCE | - |
dc.identifier.pid | younghan | - |
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