Novel nutritional function of sphingolipids via secreted exosomes
| Project/Area Number |
23617005
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Integrated Nutrition Science
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| Research Institution | Tokyo University of Agriculture and Technology |
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Principal Investigator |
MIURA Yutaka 東京農工大学, (連合)農学研究科(研究院), 教授 (10219595)
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| Project Period (FY) |
2011 – 2013
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2013: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2012: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2011: ¥2,860,000 (Direct Cost: ¥2,200,000、Indirect Cost: ¥660,000)
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| Keywords | スフィンゴミエリン / エキソソーム / miRNA / 脂質栄養学 / 肝癌細胞 / 筋管細胞 / ガングリオシド |
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| Research Abstract |
The possible new nutritional functions of sphingolipids are proposed in this study, by analyzing the composition of exosomes prepared from sphingomyelin (SPM)-treated hepatoma cells or SPM-intubated rat sera. The treatment with SPM of human hepatoma cells resulted in the decrease of proliferation. The conditioned media of SPM-treated hepatoma showed an anti-proliferative effect on hepatoma cells. SPM treatment caused the change in miRNA composition of secreted exosome, thus suppressed the proliferation of surrounding cells. The exosomes prepared from SPM-intubated rat sera significantly promoted the glucose uptake of cultured muscle cells. This result suggests the possibility that orally-intubated SPM affects the composition of serum exosomes and shows some physiological effects in vivo.
These results clearly show the possibility that sphingolipids can affect the composition of exosomes secreted from cells or into sera, thus suggesting novel nutritional functions of sphingolipids.
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Report
(4 results)
Research Products
(19 results)
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[Journal Article] Splicing factor 2-associated protein p32 participates in ribosome biogenesis by regulating the binding of Nop52 and fibrillarin to preribosome particles.2011
Author(s)
Yoshikawa H, Komatsu W, Hayano T, Miura Y, Homma K, Izumikawa K, Ishikawa H, Miyazawa N, Tachikawa H, Yamauchi Y, Isobe T, and Takahashi N
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Journal Title
Mol. Cell. Proteomics
Volume: 10
Related Report
Peer Reviewed
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