N-Glycosylation on Asn50 of SND1 Is Required for Glioma U87 Cell Proliferation and Metastasis

Figure 2

Analysis of N-glycosylation in SND1. (a) Human glioma U87 cells were treated by tunicamycin (TM) and peptide -N-glycosidase F (PNGase F); the level of SND1 was determined by electrophoresis in 6% SDS-PAGE and then immunoblotted with anti-SND1 antibodies. (b) Three-dimensional structure for human SND1. Locations of four potential N-glycosylation sites (Asn50, Asn168, Asn283, and Asn416) were indicated in yellow. (c) The schematic illustrates structural domains of human SND1 and its potential N-glycosylation site mutagenesis (N50Q, N168Q, N283Q, and N416Q) SN: staphylococcal nuclease domains. Asn (N); Gln (Q). (d) Cell lysate from U87 cells expressing WT-SND1, or its single mutants were analyzed by 6% SDS-PAGE with an anti-GFP antibody. GAPDH was used as a loading control.

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