小細胞肺癌および非小細胞肺癌細胞由来の細胞外小胞におけるN結合型糖鎖構造の違いの同定

• Material Type: 博士論文
• Title: 小細胞肺癌および非小細胞肺癌細胞由来の細胞外小胞におけるN結合型糖鎖構造の違いの同定
• Author/Editor: 近藤, 清貴
• Author Heading: 近藤, 清貴
• Publication, Distribution, etc.: American Society for Biochemistry and Molecular Biology
• Publication Date: 2022-11-17
• Publication Date (W3CDTF): 2022-11-17
• Alternative Title: Identification of distinct N-glycosylation patterns on extracellular vesicles from small-cell and non-small-cell lung cancer cells
• Degree grantor/type: 鹿児島大学
• Date Granted: 2022-11-17
• Date Granted (W3CDTF): 2022-11-17
• Dissertation Number: 甲総研第676号
• Degree Type: 博士(医学); Doctor of Philosophy in Medical Science
• Text Language Code: eng
• Subject Heading: exosome (vesicle); extracellular vesicles; glycomics; glycosylation; integrins; lung cancers
• NDC: 490
• Target Audience: 一般
• Note (General): 博士論文全文, 博士論文要旨, 最終試験結果の要旨, 論文審査の要旨; Asparagine-linked glycosylation (N-glycosylation) of proteins in the cancer secretome has been gaining increasing attention as a potential biomarker for cancer detection and diagnosis. Small extracellular vesicles (sEVs) constitute a large part of the cancer secretome, yet little is known about whether their N-glycosylation status reflects known cancer characteristics. Here, we investigated the N-glycosylation of sEVs released from small-cell lung carcinoma (SCLC) and non–small-cell lung carcinoma (NSCLC) cells. We found that the N-glycans of SCLC-sEVs were characterized by the presence of structural units also found in the brain N-glycome, while NSCLC-sEVs were dominated by typical lung-type N-glycans with NSCLC-associated core fucosylation. In addition, lectin-assisted N-glycoproteomics of SCLC-sEVs and NSCLC-sEVs revealed that integrin αV was commonly expressed in sEVs of both cancer cell types, while the epithelium-specific integrin α6β4 heterodimer was selectively expressed in NSCLC-sEVs. Importantly, N-glycomics of the immunopurified integrin α6 from NSCLC-sEVs identified NSCLC-type N-glycans on this integrin subunit. Thus, we conclude that protein N-glycosylation in lung cancer sEVs may potentially reflect the histology of lung cancers.Kiyotaka Kondo, Yoichiro Harada, Miyako Nakano, Takehiro Suzuki, Tomoko Fukushige, Ken Hanzawa, Hirokazu Yagi, Koichi Takagi, Keiko Mizuno, Yasuhide Miyamoto, Naoyuki Taniguchi, Koichi Kato, Takuro Kanekura, Naoshi Dohmae, Kentaro Machida, Ikuro Maruyama, Hiromasa InoueIdentification of distinct N-glycosylation patterns on extracellular vesicles from small-cell and non–small-cell lung cancer cellsJournal of Biological Chemistry (2022) 298(6) 101950https://doi.org/10.1016/j.jbc.2022.101950
• Persistent ID (NDL): info:ndljp/pid/12651730; https://dl.ndl.go.jp/pid/12651730
• Collection: 障害者向け資料
• Collection (Materials For Handicapped People:1): テキストデータ
• Collection (particular): 国立国会図書館デジタルコレクション > デジタル化資料 > 博士論文; https://dl.ndl.go.jp/collections/A00014
• Acquisition Basis: 博士論文（自動収集）
• Date Accepted (W3CDTF): 2023-03-02T11:18:11+09:00
• Format (IMT): application/pdf
• Access Restrictions: 国立国会図書館内限定公開
• Service for the Digitized Contents Transmission Service: 図書館・個人送信対象外
• Availability of remote photoduplication service: 可
• Periodical Title (URI): http://hdl.handle.net/10232/00032152
• Data Provider (Database): 国立国会図書館 : 国立国会図書館デジタルコレクション; https://dl.ndl.go.jp

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