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Knockdown of N-Acetylglucosaminyltransferase-II Reduces Matrix Metalloproteinase 2 Activity and Suppresses Tumorigenicity in Neuroblastoma Cell Line

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Department of Biochemistry and Molecular Biology Brody School of Medicine, East Carolina University Greenville, Greenville, NC 27834, USA
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Department of Microbiology and Immunology, Brody School of Medicine, East Carolina University Greenville, Greenville, NC 27834, USA
*
Author to whom correspondence should be addressed.
Biology 2020, 9(4), 71; https://doi.org/10.3390/biology9040071
Received: 4 March 2020 / Revised: 30 March 2020 / Accepted: 30 March 2020 / Published: 4 April 2020
(This article belongs to the Section Cell Biology)
Neuroblastoma (NB) development and progression are accompanied by changes in N-glycans attached to proteins. Here, we investigated the role of N-acetylglucosaminyltransferase-II (GnTII, MGAT2) protein substrates in neuroblastoma (NB) cells. MGAT2 was silenced in human BE(2)-C NB (HuNB) cells to generate a novel cell line, HuNB(-MGAT2), lacking complex type N-glycans, as in rat B35 NB cells. Changes in N-glycan types were confirmed by lectin binding assays in both cell lines, and the rescued cell line, HuNB(-/+MGAT2). Western blotting of cells heterologously expressing a voltage-gated K+ channel (Kv3.1b) showed that some hybrid N-glycans of Kv3.1b could be processed to complex type in HuNB(-/+MGAT2) cells. In comparing HuNB and HuNB(-MGAT2) cells, decreased complex N-glycans reduced anchorage-independent cell growth, cell proliferation, and cell invasiveness, while they enhanced cell-cell interactions. Cell proliferation, invasiveness and adhesion of the HuNB(-/+MGAT2) cells were more like the HuNB than HuNB(-MGAT2). Western blotting revealed lower protein levels of MMP-2, EGFR and Gab2 in glycosylation mutant cells relative to parental cells. Gelatin zymography demonstrated that decreased MMP-2 protein activity was related to lowered MMP-2 protein levels. Thus, our results support that decreased complex type N-glycans suppress cell proliferation and cell invasiveness in both NB cell lines via remodeling ECM. View Full-Text
Keywords: glycans; neuroblastoma; cell invasiveness; cell proliferation; MMP-2; EGFR; Gab2; cell adhesion glycans; neuroblastoma; cell invasiveness; cell proliferation; MMP-2; EGFR; Gab2; cell adhesion
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Hall, M.K.; Whitman, A.A.; Weidner, D.A.; Schwalbe, R.A. Knockdown of N-Acetylglucosaminyltransferase-II Reduces Matrix Metalloproteinase 2 Activity and Suppresses Tumorigenicity in Neuroblastoma Cell Line. Biology 2020, 9, 71.

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