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Existence of NEU1 sialidase on mouse thymocytes whose natural substrate is CD5

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Title: Existence of NEU1 sialidase on mouse thymocytes whose natural substrate is CD5
Authors: Ochiai, Shigeko1 Browse this author →KAKEN DB
Matsumoto-Mizuno, Tokuko Browse this author
Kamimura, Daisuke Browse this author →KAKEN DB
Murakami, Masaaki Browse this author →KAKEN DB
Kobayashi, Miwako Browse this author →KAKEN DB
Matsuoka, Ichiro Browse this author →KAKEN DB
Ochiai, Hiroshi Browse this author →KAKEN DB
Ishida, Hideharu Browse this author →KAKEN DB
Kiso, Makoto Browse this author →KAKEN DB
Kamimura, Keiko Browse this author
Koda, Toshiaki Browse this author →KAKEN DB
Authors(alt): Kijimoto, Shigeko1
Keywords: CD5
mRNA of 4 thymus-sialidases
NEU1 on thymocyte
NEU1-selective inhibitor
SM/J mouse
Issue Date: May-2018
Publisher: Oxford University Press
Journal Title: Glycobiology
Volume: 28
Issue: 5
Start Page: 306
End Page: 317
Publisher DOI: 10.1093/glycob/cwy009
Abstract: Membrane-bound sialidases in the mouse thymus are unique and mysterious because their activity at pH 6.5 is equal to or higher than that in the acidic region. The pH curve like this has never been reported in membrane-bound form. To clarify this enzyme, we studied the sialidase activities of crude membrane fractions from immature-T, mature-T and non-T cells from C57BU6 mice and from SM/J mice, a strain with a defect in NEU1 activity. Non-T cells from C57BL/6 mice had high activity at pH 6.5, but those from SM/J mice did not. Neu1 and Neu3 mRNA was shown by real-time PCR to be expressed in T cells and also in non-T cells, whereas Neu2 was expressed mainly in non-T cells and Neu4 was scarcely expressed. However, the in situ hybridization study on the localization of four sialidases in the thymus showed that Neu4 was clearly expressed. We then focused on a sialidase on the thymocyte surface because the possibility of the existence of a sialidase on thymocytes was suggested by peanut agglutinin (PNA) staining after incubation of the cells alone in PBS. This activity was inhibited by NEU1-selective sialidase inhibitor C9-butyl-amide-2-deoxy-2,3-dehydro-N-acetylneuraminic acid. The natural substrate for the cell surface sialidase was identified as clustered differentiation 5 (CD5) by PNA-blot analysis of anti-CD5 immunoprecipitate. We conclude that NEU1 exists on the cell surface of mouse thymocytes and CD5 is a natural substrate for it. Although this is not the main reaction of the membrane-bound thymus-sialidases, it must be important for the thymus.
Rights: This is a pre-copyedited, author-produced version of an article accepted for publication in Glycobiology following peer review. The version of record Glycobiology, Volume 28, Issue 5, 1 May 2018, Pages 306–317, is available online at:
Type: article (author version)
Appears in Collections:遺伝子病制御研究所 (Institute for Genetic Medicine) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 落合 滋子

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