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This first demonstration of sialidase involvement in invasive potential of gliolastoma cells may point to NEU3 as an attractive treatment target of human gliomas
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effect of overexpression on EGFR downstream pathway activation and TKI targeted therapies sensitivity in non-small cell lung cancer cell lines
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The most potent compound tested targeted the human Neu4 isoenzyme, and was able to substantially reduce the rate of cell migration. We found that the lateral mobility of integrins was reduced by treatment of cells with Neu3, suggesting that Neu3 enzyme activity resulted in changes to integrin-co-receptor or integrin-cytoskeleton interactions
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NEU3 possesses the ability to interact with specific proteins, many of which are different in each cell compartment, supporting NEU3 involvement in the cell stress response, protein folding, and intracellular trafficking.
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findings identify NEU3 as a participant in head and neck squamous cell carcinoma progression
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Besides the already reported indirect EGFR activation through GM3, sialidase NEU3 could also play a role on EGFR activation through its desialylation.
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NEU3 promotes anchorage-independent growth and in vivo tumorigenicity.
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In the plasma membrane, NEU3 has a role in endocytosis and protein binding at the cell surface.
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Results indicate an essential contribution of NEU3 to tumorigenic potential through maintenance of stem-like characteristics of colon cancer cells by regulating Wnt signaling at the receptor level.
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The results provide strong evidence that the serum sialidase is, in fact, NEU3, and this subtype may, therefore, be a potential utility for novel diagnosis of human cancers
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Studies indicate that ganglioside-specific sialidase NEU3 cleaves sialic acids preferentially from gangliosides.
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Weak anchorage of NEU1 and NEU3 to the plasma membrane and their loss during erythrocyte life could be a tool to preserve the cellular sialic acid content to avoid early aging of erythrocyte and processes of cell aggregation in the capillaries.
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NEU3 is a key regulator of the beta1 integrin-recycling pathway and FAK/AKT signaling and demonstrate its crucial role in renal cell carcinomas malignancy.
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Data indicate that sialidases Neu1 and Neu3 are present on sperm, and their activity is required for capacitation and zona pellucida binding.
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Data show that NEU1 was immunolocalized to both the plasma membrane and the perinuclear region, and NEU3 was detected both in the cytosol and nucleus.
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These data suggest that NEU3 regulates tumor progression through AR signaling, and thus be a potential tool for diagnosis and therapy of androgen-independent prostate cancer.
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NEU3 is highly expressed to enhance malignant phenotypes including apoptosis inhibition in malignant melanomas.
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observed that trisaccharides with incorporated azide groups in the Neu5Ac residue at either C9 or the N5-Ac position were substrates, and in the case of the N5-azidoacetyl derivative, the activity was superior to that of GM3
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Truncations at the N- or C-terminus of more than 10 residues abolished enzyme activity.
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NEU3 expression is diversely regulated by Sp1/Sp3 transcription factors binding to alternative promoters, which might account for multiple modulation of gene expression.
