Molecular mechanisms linking lipid metabolism and thermoregulation
| Project/Area Number |
25293012
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Partial Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Biological pharmacy
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| Research Institution | Kyoto University |
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Principal Investigator |
Umeda Masato 京都大学, 工学(系)研究科(研究院), 教授 (10185069)
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| Co-Investigator(Renkei-kenkyūsha) |
HARA Yuji 京都大学, 大学院工学研究科, 准教授 (60362456)
NAGAO Kohjiro 京都大学, 大学院工学研究科, 助教 (40587325)
JUNI Naoto 京都大学, 大学院工学研究科, 研究員 (90572199)
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| Project Period (FY) |
2013-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥18,980,000 (Direct Cost: ¥14,600,000、Indirect Cost: ¥4,380,000)
Fiscal Year 2015: ¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2014: ¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2013: ¥8,060,000 (Direct Cost: ¥6,200,000、Indirect Cost: ¥1,860,000)
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| Keywords | 脂質 / 細胞膜 / 温度 / 細胞・組織 / 昆虫 / シグナル伝達 / 代謝疾患 |
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| Outline of Final Research Achievements |
Temperature is a universal and pervasive physical characteristic, which affects the physiology, behavior and evolution of organisms. Animals have thermoregulatory systems to adapt their physiological functions, such as energy utilization, growth, reproduction and locomotion, in response to the wide range of changes in ambient temperature. We have shown that thermoregulatory behavior of Drosophila melanogaster is highly dependent on the level of energy metabolism and identified that Δ-9 fatty acid desaturase (DESAT1), whose expression is highly dependent on environmental temperature, plays a pivotal role in controlling thermoregulatory behavior as well as lipid metabolism of Drosophila.
In this study, we elucidated the molecular mechanisms that regulate the expression of DESAT1 and identified the DESAT1-associated proteins. We also examined the effect of DESAT1 on mitochondrial function and the temperature-dependent control of body size.
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Report
(4 results)
Research Products
(26 results)
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[Journal Article] Evaluation of aegerolysins as novel tools to detect and visualize ceramide phosphoethanolamine, a major sphingolipid in invertebrates.2015
Author(s)
Bhat HB, Ishitsuka R, Inaba T, Murate M, Abe M, Makino A, Kohyama-Koganeya A, Nagao K, Kurahashi A, Kishimoto T, Tahara M, Yamano A, Nagamune K, Hirabayashi Y, Juni N, Umeda M, Fujimori F, Nishibori K, Yamaji-Hasegawa A, Greimel P, Kobayashi T.
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Journal Title
FASEB.J.
Volume: 29(9)
Pages: 3920-34
DOI
Related Report
Peer Reviewed / Open Access / Int'l Joint Research / Acknowledgement Compliant
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[Journal Article] Development of a novel tetravalent synthetic peptide that binds to phosphatidic acid.2015
Author(s)
Rina Ogawa, Kohjiro Nagao, Kentaro Taniuchi, Masaki Tsuchiya, Utako Kato, Yuji Hara, Takehiko Inaba, Toshihide Kobayashi, Yoshihiro Sasaki, Kazunari Akiyoshi, Miho Watanabe-Takahashi, Kiyotaka Nishikawa, Masato Umeda
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Journal Title
DOI
NAID
Related Report
Peer Reviewed / Open Access / Acknowledgement Compliant
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[Journal Article] Curvature engineering: positive membrane curvature induced by epsin N-terminal peptide boosts internalization of octaarginine.2013
Author(s)
Pujals S., Miyamae H., Afonin S., Murayama T., Hirose H., Nakase I., Taniuchi K., Umeda M., Sakamoto K., Ulrich AS., Futaki S.
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Journal Title
ACS Chem Biol.
Volume: 8
Pages: 1894-1899
DOI
Related Report
Peer Reviewed
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[Journal Article] The role of nadrin, a Rho GTPase-activating protein, in the morphological differentiation of astrocytes.2013
Author(s)
Kobayashi, Y., Harada, A., Furuta, B., Asou, H., Kato, U., Umeda, M.:
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Journal Title
J Biochem.
Volume: 153
Pages: 389-398
DOI
Related Report
Peer Reviewed
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[Journal Article] Furuta, B., Asou, H., Kato, U., Umeda, M.: The role of nadrin, a Rho GTPase-activating protein, in the morphological differentiation of astrocytes.2013
Author(s)
Kato, U., Inadome, H., Emoto, K., Kobayashi, T., Umeda, M.
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Journal Title
J Biol Chem.
Volume: 288
Pages: 389-398
DOI
Related Report
Peer Reviewed
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