| Project/Area Number |
17380041
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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 |
Applied entomology
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| Research Institution | The Institute of Physical and Chemical Research |
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Principal Investigator |
MATSUMOTO Shogo The Institute of Physical and Chemical Research, Molecular Entomology Laboratory, Chief Scientist (60134516)
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| Co-Investigator(Kenkyū-buntansha) |
MOTO Ken'ichi RIKEN, Molecular Entomology Laboratory, Senior Research Scientist (90333335)
HULL J.Joe RIKEN, Molecular Entomology Laboratory, Contract Researcher (70415181)
OHNISHI Atsushi RIKEN, Molecular Entomology Laboratory (50342762)
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| Project Period (FY) |
2005 – 2007
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| Project Status |
Completed (Fiscal Year 2007)
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| Budget Amount *help |
¥17,080,000 (Direct Cost: ¥15,700,000、Indirect Cost: ¥1,380,000)
Fiscal Year 2007: ¥5,980,000 (Direct Cost: ¥4,600,000、Indirect Cost: ¥1,380,000)
Fiscal Year 2006: ¥4,600,000 (Direct Cost: ¥4,600,000)
Fiscal Year 2005: ¥6,500,000 (Direct Cost: ¥6,500,000)
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| Keywords | silkmoth / pheromone / lipid droplet / lipolysis / G-protein coupled receptor / RNAi / PBAN receptor / acvl-CoA binding protein / 昆虫 / 生合性酵素遺伝子 / シグナル伝達 / リン酸化 / ESTデータベース / リパーゼ |
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| Research Abstract |
The neurohormone PBAN (pheromone biosynthesis activating neuropeptide) regulates pheromone (bombykol) biosynthesis in the silkmoth, Bombyx marl, by binding to its cognate PBAN receptor, which is located in the pheromone gland (PG) cells of female moths. While extracellular Ca^<2+> had been shown to be essential for sex pheromone biosynthesis in all species studied to date, there had been no direct demonstration of this crucial event. To address this, we used fluorescent Ca^<2+> imaging techniques with isolated PGs to directly demonstrate that PBAN specifically triggers an influx of extracellular Ca^<2+>. Despite the efforts of numerous groups to understand the molecular mechanisms underlying bombykol production, little is known regarding how the external PBAN signal is converted to the calcium signal that drives bombykol production and release. To address this issue, we have taken advantage of the genome information in B. mori and characterized PG-specific genes[i.e. PG fatty acyl reductase (pgFAR), B. mori PG Z11/Δ10, 12 desaturase (Bmpgdesatl), PG acyl-CoA-binding protein (pgilCB1), midgut ACBP (mgACBI), and PBAN receptor (PBANR)] and successfully demonstrated their specific roles in bombykol biosynthesis in vivo by using an RNA interference-mediated loss-of-function approach.
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