C-Mannosylation is involved in the regulation of epithelial-cell adhesion.

2017 Fiscal Year Final Research Report

• Project/Area Number: 15K06981
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Structural biochemistry
• Research Institution: Wakayama Medical University
• Principal Investigator: Ihara Yoshito 和歌山県立医科大学, 医学部, 教授 (70263241)
• 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)
• Project Period (FY): 2015-04-01 – 2018-03-31
• 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

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.

Free Research Field

生物学