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Visualization of sialidase activity in Mammalian tissues and cancer detection with a novel fluorescent sialidase substrate.


ABSTRACT: Sialidase removes sialic acid from sialoglycoconjugates and plays crucial roles in many physiological and pathological processes. Various human cancers express an abnormally high level of the plasma membrane-associated sialidase isoform.Visualization of sialidase activity in living mammalian tissues would be useful not only for understanding sialidase functions but also for cancer diagnosis. However, since enzyme activity of mammalian sialidase is remarkably weak compared with that of bacterial and viral sialidases, it has been difficult to detect sialidase activity in mammalian tissues. We synthesized a novel benzothiazolylphenol-based sialic acid derivative (BTP-Neu5Ac) as a fluorescent sialidase substrate. BTP-Neu5Ac can visualize sialidase activities sensitively and selectively in acute rat brain slices. Cancer cells implanted orthotopically in mouse colons and human colon cancers (stages T3-T4) were also clearly detected with BTP-Neu5Ac. The results suggest that BTP-Neu5Ac is useful for histochemical imaging of sialidase activities.

SUBMITTER: Minami A 

PROVIDER: S-EPMC3888388 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature

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Visualization of sialidase activity in Mammalian tissues and cancer detection with a novel fluorescent sialidase substrate.

Minami Akira A   Otsubo Tadamune T   Ieno Daisuke D   Ikeda Kiyoshi K   Kanazawa Hiroaki H   Shimizu Kosuke K   Ohata Ko K   Yokochi Tsunehiro T   Horii Yuuki Y   Fukumoto Hokuto H   Taguchi Risa R   Takahashi Tadanobu T   Oku Naoto N   Suzuki Takashi T  

PloS one 20140110 1


Sialidase removes sialic acid from sialoglycoconjugates and plays crucial roles in many physiological and pathological processes. Various human cancers express an abnormally high level of the plasma membrane-associated sialidase isoform.Visualization of sialidase activity in living mammalian tissues would be useful not only for understanding sialidase functions but also for cancer diagnosis. However, since enzyme activity of mammalian sialidase is remarkably weak compared with that of bacterial  ...[more]

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