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  1. C100 医学部/医学系研究科
  2. C100a 雑誌掲載論文
  3. 学術雑誌

N-acetylglucosaminyltransferase IVa promotes invasion of choriocarcinoma

http://hdl.handle.net/2237/26977
http://hdl.handle.net/2237/26977
b553ee37-ca0f-4545-aa3a-15cf1bf9c9cb
名前 / ファイル ライセンス アクション
OR-183799_Nishino.pdf OR-183799_Nishino.pdf ファイル公開:2018/01/01 (774.8 kB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2017-09-08
タイトル
タイトル N-acetylglucosaminyltransferase IVa promotes invasion of choriocarcinoma
言語 en
著者 Nishino, Kimihiro

× Nishino, Kimihiro

WEKO 73565

en Nishino, Kimihiro

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Yamamoto, Eiko

× Yamamoto, Eiko

WEKO 73566

en Yamamoto, Eiko

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Niimi, Kaoru

× Niimi, Kaoru

WEKO 73567

en Niimi, Kaoru

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Sekiya, Yoko

× Sekiya, Yoko

WEKO 73568

en Sekiya, Yoko

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Yamashita, Yoriko

× Yamashita, Yoriko

WEKO 73569

en Yamashita, Yoriko

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Kikkawa, Fumitaka

× Kikkawa, Fumitaka

WEKO 73570

en Kikkawa, Fumitaka

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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
抄録
内容記述タイプ Abstract
内容記述 Gestational trophoblastic neoplasia (GTN) results from the malignant transformation of placental trophoblasts which secrete human chorionic gonadotropin (hCG) as do normal placenta or hydatidiform mole. N-acetylglucosaminyltransferase IV (GnT-IV) is a glycosyltransferase which catalyses the formation of β1,4GlcNAc branches on the mannose core of N-glycans. Previous studies reported that β1,4GlcNAc branches on hCG were detected in GTN but not in normal pregnancy or hydatidiform mole. The aim of the present study was to understand the role of GnT-IVa in choriocarcinoma and find the target proteins for GnT-IVa glycosylation which contribute to the malignancy of choriocarcinoma. Immunohistochemistry showed that Griffonia simplicifolia lectin-II staining and GnT-IVa staining were intense in trophoblastic cells of invasive mole and choriocarcinoma. We established a choriocarcinoma cell line with GnT-IVa overexpression (Jar-GnT4a), and examined its malignant potential and target proteins for GnT-IVa glycosylation. GnT-IVa overexpression increased the cell migration and invasion (2.5- and 1.4-fold) as well as the ability to adhere to the extracellular matrix (ECM) components, including fibronectin and collagen type I and IV. The tumour formation potential of Jar-GnT4a in mice was significantly higher than that of control (P=0.0407), and the cumulative survival rate of mice with Jar-GnT4a was relatively lower than those with control. Immunoprecipitation studies showed that β1,4GlcNAc branches of N-glycans on integrin β1 in choriocarcinoma cells were increased by GnT-IVa overexpression. Nano-LC/MS/MS analysis suggested that lysosome-associated membrane glycoprotein 2 (LAMP-2) was a target protein for glycosylation by GnT-IVa. The increase in β1,4GlcNAc branches on LAMP-2 by GnT-IVa overexpression was confirmed by lectin blot analysis using whole cell lysate and conditioned medium. Our results suggest that highly branched N-glycans generated by the action of GnT-IVa are present in trophoblastic cells of GTN in proportion to GnT-IVa expression level, and that GnT-IVa may contribute to the malignancy of choriocarcinoma by promoting cell adhesion, migration and invasion through glycosylation of integrin β1 and LAMP-2.
言語 en
出版者
出版者 Spandidos Publications
言語 en
言語
言語 eng
資源タイプ
資源タイプresource http://purl.org/coar/resource_type/c_6501
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
DOI
関連タイプ isVersionOf
識別子タイプ DOI
関連識別子 https://doi.org/10.3892/or.2017.5661
ISSN
収録物識別子タイプ PISSN
収録物識別子 1021-335X
書誌情報 en : Oncology Letters

巻 38, 号 1, p. 440-448, 発行日 2017-07
著者版フラグ
値 publisher
URI
識別子 https://doi.org/10.3892/or.2017.5661
識別子タイプ DOI
URI
識別子 http://hdl.handle.net/2237/26977
識別子タイプ HDL
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