Studies on the mechanism of activation of phospholipase D
| Project/Area Number |
11470041
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| Research Category |
Grant-in-Aid for Scientific Research (B).
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Pathological medical chemistry
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| Research Institution | Kobe University |
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Principal Investigator |
NAKAMURA Shun-ichi Kobe University, School of Medicine, Biochemistry, Professor, 医学部, 教授 (40155833)
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| Co-Investigator(Kenkyū-buntansha) |
OKADA Taro Kobe University, School of Medicine, Research Associate, 医学部, 助手 (80304088)
MIWA Noriko Kobe University, School of Medicine, Research Associate, 医学部, 助手 (50202354)
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| Project Period (FY) |
1999 – 2000
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| Project Status |
Completed (Fiscal Year 2000)
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| Budget Amount *help |
¥14,900,000 (Direct Cost: ¥14,900,000)
Fiscal Year 2000: ¥4,200,000 (Direct Cost: ¥4,200,000)
Fiscal Year 1999: ¥10,700,000 (Direct Cost: ¥10,700,000)
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| Keywords | Signal transduction / Phospholipase D / G_<M2> activator / G-protein / ADP-ribosvlation factor |
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| Research Abstract |
We have recently reported that an important factor for ganglioside metabolism known as GM2 activator is involved in the regulation of phospholipase D (PLD) activation.
In an in vitro study recombinant GM2 activator activated PLD1 and PLD2 in a dose-dependent manner. GM2 activator stimulated PLD1 synergistically with ARF.In contrast to the concerted activation of activators, PLD2 was stimulated by GM2 activator acting almost solely.
In GM2 activator-deficient fibroblasts PLD activation by PMA was almost normal compared with the stimulation pattern in wild-type cells. In the cells stably expressing dominant-negative GM2 activator, PLD activation by PMA was remarkably suppressed. Taken together, these data strongly suggest that similar factors to GM2 activator redundantly regulate PLD activity in the cells. Identification of these factors is essential for the understanding of the mechanism of receptor-mediated PLD activation.
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Report
(3 results)
Research Products
(5 results)
