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Fig. 8 | Breast Cancer Research

Fig. 8

From: Quantitative glycoproteomics analysis identifies novel FUT8 targets and signaling networks critical for breast cancer cell invasiveness

Fig. 8

FUT8 modulates core fucosylation and adhesive capability of αvβ5 integrins. a Integrins αv and β5 were core fucosylated by FUT8 in HEK-293 T cells. Recombinant integrin αv (upper panel) and integrin β5 (lower panel) in the control or two FUT8-KO 293 T cell lines were probed with biotinylated LCA, then detected with streptavidin-conjugated horseradish peroxidase. Protein domain organization of these selected proteins are depicted according to Uniprot data. Amino acid number and potential N-linked glycosites are marked on the upper and lower side, respectively. Core-fucosylated sites verified by LC–MS/MS analysis are in red. TM, transmembrane domain. b Core fucosylation of integrin αv. LC–MS/MS summed extracted ion chromatogram (XIC) of identified core-fucosylated glycopeptides for integrin αv. The number on asparagine (N) indicates the position in the protein sequence. c and d Functional blocking antibodies abolished cell adhesion to vitronectin and laminin-5 in MDA-MB-231 cells. Plates were pre-coated with 5 μg/ml vitronectin (c) or laminin-5 (d). MDA-MB-231 cells were pre-incubated with anti-integrin antibodies (10 μg/ml) before cells were placed on coated plates for 10 min at 37 °C. Adherent cells were quantified after fixation and stained with crystal violet. Data are mean ± SD. **p < 0.01 compare with control IgG. e and f FUT8 KO reduced cell adhesion to vitronectin and laminin-5 in MDA-MB-231 cells. Parental or FUT8-KO MDA-MB-231 cells were allowed to attach to vitronectn-coated (e) or laminin-5-coated (f) plates. Adherent cells were quantified after fixation and stained with crystal violet. Data are mean ± SD. **p < 0.01, FUT8-KO versus parental cells

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