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  • Differential Carbohydrate Binding and Cell Surface Glycosylation of Human Cancer Cell Lines

    Author(s)
    Arndt, Nadia X
    Tiralongo, Joe
    Madge, Paul D
    von Itzstein, Mark
    Day, Christopher J
    Griffith University Author(s)
    von Itzstein, Mark
    Day, Christopher J.
    Tiralongo, Joe
    Year published
    2011
    Metadata
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    Abstract
    Currently there is only a modest level knowledge of the glycosylation status of immortalised cell lines that are commonly used in cancer biology as well as their binding affinities to different glycan structures. Through use of glycan and lectin microarray technology, this study has endeavoured to define the different bindings of cell surface carbohydrate structures to glycan-binding lectins. The screening of breast cancer MDA-MB435 cells, cervical cancer HeLa cells and colon cancer Caco-2, HCT116 and HCT116-FM6 cells was conducted to determine their differential bindings to a variety of glycan and lectin structures printed ...
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    Currently there is only a modest level knowledge of the glycosylation status of immortalised cell lines that are commonly used in cancer biology as well as their binding affinities to different glycan structures. Through use of glycan and lectin microarray technology, this study has endeavoured to define the different bindings of cell surface carbohydrate structures to glycan-binding lectins. The screening of breast cancer MDA-MB435 cells, cervical cancer HeLa cells and colon cancer Caco-2, HCT116 and HCT116-FM6 cells was conducted to determine their differential bindings to a variety of glycan and lectin structures printed on the array slides. An inverse relationship between the number of glycan structures recognised and the variety of cell surface glycosylation was observed. Of the cell lines tested, it was found that four bound to sialylated structures in initial screening. Secondary screening in the presence of a neuraminidase inhibitor (4-deoxy-4-guanidino- Neu5Ac2en) significantly reduced sialic acid binding. The array technology has proven to be useful in determining the glycosylation signatures of various cell-lines as well as their glycan binding preferences. The findings of this study provide the groundwork for further investigation into the numerous glycan-lectin interactions that are exhibited by immortalised cell lines.
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    Journal Title
    Journal of Cellular Biochemistry
    Volume
    112
    Issue
    9
    DOI
    https://doi.org/10.1002/jcb.23139
    Subject
    Biochemistry and cell biology
    Cellular interactions (incl. adhesion, matrix, cell wall)
    Receptors and membrane biology
    Cancer cell biology
    Medical physiology
    Publication URI
    http://hdl.handle.net/10072/43447
    Collection
    • Journal articles

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