| Project/Area Number |
15K06981
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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 |
Structural biochemistry
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| Research Institution | Wakayama Medical University |
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Principal Investigator |
Ihara Yoshito 和歌山県立医科大学, 医学部, 教授 (70263241)
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| Co-Investigator(Kenkyū-buntansha) |
井内 陽子 和歌山県立医科大学, 医学部, 助教 (20316087)
池崎 みどり 和歌山県立医科大学, 医学部, 助教 (40549747)
南方 志帆 和歌山県立医科大学, 医学部, 特別研究員 (90508574)
眞鍋 史乃 国立研究開発法人理化学研究所, 伊藤細胞制御化学研究室, 専任研究員 (60300901)
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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 |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2017: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2016: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2015: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | 糖タンパク質 / C-マンノシル化 / 細胞接着分子 / E-カドヘリン |
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| Outline of Final Research Achievements |
C-Mannosylation is a unique sugar modification on tryptophan residues in proteins. We found that chemically synthesized C-mannosyl peptides (i.e., C-Man-Trp-Ser-Pro-Trp) suppress the formation of adherens-junction structure in epithelial-like A549 cells. In the presence of C-mannosyl peptides, degradation of E-cadherin was accelerated in the cells. C-Mannosyl peptides also suppressed the complex formation between E-cadherin and β-catenin, through the interaction to α-actinin 4 or myosin-1c but not to E-cadherin. This study indicates that the C-mannosyl peptide is a bioactive glycopeptide, and exerts a novel role for the regulation of epithelial-cell adhesion.
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