| Project/Area Number |
15K16134
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Risk sciences of radiation and chemicals
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| Research Institution | Tokyo University of Agriculture and Technology |
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Principal Investigator |
MIZUKAWA Kaoruko 東京農工大学, (連合)農学研究科(研究院), 助教 (50636868)
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| Research Collaborator |
Takada Hideshige 東京農工大学
Stegeman John J. Woods Hole Oceanographic Institution
Goldstone Jed V. Woods Hole Oceanographic Institution
Salanga Matthew C. Arizona University
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2017: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000)
Fiscal Year 2016: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2015: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Keywords | PBDEs / 脱臭素化 / 魚類 / 異物代謝 / 甲状腺ホルモン / 脱ヨウ素酵素 / 微量汚染物質 / 種差 / ハゼ科 / ドジョウ亜科 / BDE99 / コイ目 |
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| Outline of Final Research Achievements |
Debromination of PBDEs by fish has been considered that it would be caused by deiodinase which is the enzyme for activation of thyroid hormones. The aim of the study is to compare species specific debromination of PBDEs and reveal the factor. It is important knowledge for metabolic sensitivity of xenobiotics. BDE99 is the most debrominatable congener of PBDE. To compare accumulation of BDE99 in muscle tissues and debromination ability of BDE99 by hepatic microsome among many kinds of fishes, wild fishes were collected from Tama River and coastal area of Tokyo Bay, Japan. Some fishes had no BDE99 accumulation in their muscle tissues and had debromination ability of BDE99 by hepatic microsome. Especially the all 12 Cyprinidae indicated the relationships throughout the family. However there are no consistent relationships among 6 Gobidae. It is suggested that the difference of the debromination velocity of BDE99 among species are due to enzymatic structures of deiodinase.
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