Roles of GalNAc-disialyl Lactotetraosyl ...
Document type :
Article dans une revue scientifique
Permalink :
Title :
Roles of GalNAc-disialyl Lactotetraosyl Antigens in Renal Cancer Cells
Author(s) :
Tsuchida, Akiko [Auteur]
Nagoya University
Senda, Motohiro [Auteur]
Nagoya University
Ito, Akihiro [Auteur]
Tohoku University [Sendai]
Saito, Seiichi [Auteur]
University of the Ryukyus [Okinawa]
Kiso, Makoto [Auteur]
Gifu University
Ando, Takayuki [Auteur]
Harduin Lepers, Anne [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Matsuda, Akio [Auteur]
Furukawa, Keiko [Auteur]
Chubu University
Furukawa, Koichi [Auteur]
Chubu University
Nagoya University
Senda, Motohiro [Auteur]
Nagoya University
Ito, Akihiro [Auteur]
Tohoku University [Sendai]
Saito, Seiichi [Auteur]
University of the Ryukyus [Okinawa]
Kiso, Makoto [Auteur]
Gifu University
Ando, Takayuki [Auteur]
Harduin Lepers, Anne [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Matsuda, Akio [Auteur]
Furukawa, Keiko [Auteur]
Chubu University
Furukawa, Koichi [Auteur]
Chubu University
Journal title :
Scientific Reports
Abbreviated title :
Sci Rep
Volume number :
8
Pages :
7017
Publisher :
Nature Research
Publication date :
2018-12
ISSN :
2045-2322
HAL domain(s) :
Chimie/Chimie théorique et/ou physique
English abstract : [en]
GalNAc-disialyl Lc4 (GalNAc-DSLc4) was reported as a novel antigen that associated with malignant features of renal cell cancers (RCCs). To clarify roles of GalNAc-DSLc4 in malignant properties of RCCs, we identified ...
Show more >GalNAc-disialyl Lc4 (GalNAc-DSLc4) was reported as a novel antigen that associated with malignant features of renal cell cancers (RCCs). To clarify roles of GalNAc-DSLc4 in malignant properties of RCCs, we identified B4GalNAc-T2 as a responsible gene for the synthesis of GalNAc-DSLc4, and prepared stable transfectants of GalNAc-T2 cDNA using VMRC-RCW cells, resulting in the establishment of high expressants of GalNAc-DSLc4. They showed increased proliferation and invasion, and specific adhesion to laminin. In the transfectants, PI3K/Akt signals were highly activated by serum stimulation or adhesion to laminin. GalNAc-DSLc4 was co-localized in lipid rafts with integrin β1 and caveolin-1 in both immunoblotting of fractionated detergent extracts and immunocytostaining, particularly when stimulated with serum. Masking of GalNAc-DSLc4 with antibodies as well as PI3K inhibitor suppressed malignant properties of the transfectants. These results suggested that GalNAc-DSLc4 is involved in malignant properties of RCCs by forming a molecular complex with integrins in lipid rafts.Show less >
Show more >GalNAc-disialyl Lc4 (GalNAc-DSLc4) was reported as a novel antigen that associated with malignant features of renal cell cancers (RCCs). To clarify roles of GalNAc-DSLc4 in malignant properties of RCCs, we identified B4GalNAc-T2 as a responsible gene for the synthesis of GalNAc-DSLc4, and prepared stable transfectants of GalNAc-T2 cDNA using VMRC-RCW cells, resulting in the establishment of high expressants of GalNAc-DSLc4. They showed increased proliferation and invasion, and specific adhesion to laminin. In the transfectants, PI3K/Akt signals were highly activated by serum stimulation or adhesion to laminin. GalNAc-DSLc4 was co-localized in lipid rafts with integrin β1 and caveolin-1 in both immunoblotting of fractionated detergent extracts and immunocytostaining, particularly when stimulated with serum. Masking of GalNAc-DSLc4 with antibodies as well as PI3K inhibitor suppressed malignant properties of the transfectants. These results suggested that GalNAc-DSLc4 is involved in malignant properties of RCCs by forming a molecular complex with integrins in lipid rafts.Show less >
Language :
Anglais
Peer reviewed article :
Oui
Audience :
Internationale
Popular science :
Non
Comment :
Corrections apportées à l'article original, le 09 avril 2020.
An Author Correction to this article was published on 09 April 2020.
Administrative institution(s) :
CNRS
Université de Lille
Université de Lille
Research team(s) :
Régulation de la glycosylation terminale
Submission date :
2020-02-12T15:45:05Z
2021-04-30T08:14:53Z
2021-04-30T08:14:53Z
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- s41598-020-63112-6.pdf
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