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Identification of Glycan Structure Alterations on Cell Membrane Proteins in Desoxyepothilone B Resistant Leukemia Cells

https://hiroshima.repo.nii.ac.jp/records/2007717
https://hiroshima.repo.nii.ac.jp/records/2007717
8567e160-699c-4fa4-bd64-c8415855f691
名前 / ファイル ライセンス アクション
MolCellProteomics_10-11_M111.009001.pdf MolCellProteomics_10-11_M111.009001.pdf (3.1 MB)
Item type デフォルトアイテムタイプ_(フル)(1)
公開日 2023-03-18
タイトル
タイトル Identification of Glycan Structure Alterations on Cell Membrane Proteins in Desoxyepothilone B Resistant Leukemia Cells
言語 en
作成者 Nakano, Miyako

× Nakano, Miyako

en Nakano, Miyako

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Saldanha, Rohit

× Saldanha, Rohit

en Saldanha, Rohit

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Göbel, Anja

× Göbel, Anja

en Göbel, Anja

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Kavallaris, Maria

× Kavallaris, Maria

en Kavallaris, Maria

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Packer, Nicolle H.

× Packer, Nicolle H.

en Packer, Nicolle H.

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アクセス権
アクセス権 open access
アクセス権URI http://purl.org/coar/access_right/c_abf2
権利情報
権利情報 This research was originally published in Molecular & Cellular Proteomics. Miyako Nakano, Rohit Saldanha, Anja Göbel, Maria Kavallaris, Nicolle H. Packer. Identification of Glycan Structure Alterations on Cell Membrane Proteins in Desoxyepothilone B Resistant Leukemia Cells. Mol Cell Proteomics. 2011; 10(11):M111.009001. © the American Society for Biochemistry and Molecular Biology.
内容記述
内容記述 Resistance to tubulin-binding agents used in cancer is often multifactorial and can include changes in drug accumulation and modified expression of tubulin isotypes. Glycans on cell membrane proteins play important roles in many cellular processes such as recognition and apoptosis, and this study investigated whether changes to the glycan structures on cell membrane proteins occur when cells become resistant to drugs. Specifically, we investigated the alteration of glycan structures on the cell membrane proteins of human T-cell acute lymphoblastic leukemia (CEM) cells that were selected for resistance to desoxyepothilone B (CEM/dEpoB). The glycan profile of the cell membrane glycoproteins was obtained by sequential release of N- and O-glycans from cell membrane fraction dotted onto polyvinylidene difluoride membrane with PNGase F and β-elimination respectively. The released glycan alditols were analyzed by liquid chromatography (graphitized carbon)-electrospray ionization tandem MS. The major N-glycan on CEM cell was the core fucosylated α2–6 monosialo-biantennary structure. Resistant CEM/dEpoB cells had a significant decrease of α2–6 linked sialic acid on N-glycans. The lower α2–6 sialylation was caused by a decrease in activity of β-galactoside α2–6 sialyltransferase (ST6Gal), and decreased expression of the mRNA. It is clear that the membrane glycosylation of leukemia cells changes during acquired resistance to dEpoB drugs and that this change occurs globally on all cell membrane glycoproteins. This is the first identification of a specific glycan modification on the surface of drug resistant cells and the mechanism of this downstream effect on microtubule targeting drugs may offer a route to new interventions to overcome drug resistance.
言語 en
内容記述
内容記述タイプ Other
内容記述 This research was supported by a Cancer Institute of New South Wales Infrastructure Award, Children’s Cancer Institute Australia for Medical Research, which is affiliated with the University of New South Wales and the Sydney Children’s Hospital and grants from the New South Wales Cancer Council and a National Health and Medical Research Council Senior Fellowship (M. Kavallaris).
出版者
出版者 The American Society for Biochemistry and Molecular Biology, Inc.
言語
言語 eng
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
資源タイプ journal article
出版タイプ
出版タイプ VoR
出版タイプResource http://purl.org/coar/version/c_970fb48d4fbd8a85
関連情報
識別子タイプ DOI
関連識別子 10.1074/mcp.M111.009001
関連情報
識別子タイプ DOI
関連識別子 https://doi.org/10.1074/mcp.M111.009001
収録物識別子
収録物識別子タイプ ISSN
収録物識別子 1535-9476
収録物識別子
収録物識別子タイプ ISSN
収録物識別子 1535-9484
開始ページ
開始ページ M111.009001
書誌情報 Molecular & Cellular Proteomics
Molecular & Cellular Proteomics

巻 10, 号 11, p. M111.009001, 発行日 2011-08-22
旧ID 48595
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