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. 2014 Mar 4;44(5):1433–1442. doi: 10.3892/ijo.2014.2319

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Copyright © 2014, Spandidos Publications

This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.

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Figure 2. — O-glycosylation inhibitor, benzyl-GalNAc (BZ) treatment resulted in the enhancement of PNA and VVA lectin reactivity suggesting the inhibition of elongation of O-glycosylation (PNA, ^*P<0.05; VVA, ^**P<0.005; NS, not significant) (A). ConA and L-PHA lectin binding activity which is related to N-glycans was not dramatically changed. Treatment of BZ did not show alteration of cell adhesive capacity to human recombinant galectin-1 (NS, not significant; et, ethanol control; BZ, benzyl-GalNAc) (B). Representative results from two independent experiments in triplicate are shown.

Figure 2. — O-glycosylation inhibitor, benzyl-GalNAc (BZ) treatment resulted in the enhancement of PNA and VVA lectin reactivity suggesting the inhibition of elongation of O-glycosylation (PNA, ^*P<0.05; VVA, ^**P<0.005; NS, not significant) (A). ConA and L-PHA lectin binding activity which is related to N-glycans was not dramatically changed. Treatment of BZ did not show alteration of cell adhesive capacity to human recombinant galectin-1 (NS, not significant; et, ethanol control; BZ, benzyl-GalNAc) (B). Representative results from two independent experiments in triplicate are shown.