Reduction of N-Acetylglucosaminyltransferase-I Activity Promotes Neuroblastoma Invasiveness and EGF-Stimulated Proliferation In Vitro.

Aberrant N-glycosylation has been associated with progression of the pediatric cancer neuroblastoma (NB) but remains understudied. Here we investigated oligomannose N-glycans in NB by genetic editing of in a human NB cell line, BE(2)-C, called BE(2)-C(MGAT1). Lectin binding studies confirmed that BE(2)-C(MGAT1) had decreased complex and increased oligomannose N-glycans.

Limited N-Glycan Processing Impacts Chaperone Expression Patterns, Cell Growth and Cell Invasiveness in Neuroblastoma.

Enhanced N-glycan branching is associated with cancer, but recent investigations supported the involvement of less processed N-glycans. Herein, we investigated how changes in N-glycosylation influence cellular properties in neuroblastoma (NB) using rat N-glycan mutant cell lines, NB_1(-), NB_1(-) and NB_1(-), as well as the parental cell line NB_1. The two earlier mutant cells have compromised N-acetylglucosaminyltransferase-I (GnT-I) and GnT-II activities.

Kv3-Expressing Cells Present More Elaborate N-Glycans with Changes in Cytoskeletal Proteins, Neurite Structure and Cell Migration.

The cues contained by N-glycans relay the quality, cellular destination, and interactions of proteins, thereby, impacting cellular physiology. Voltage-gated K (Kv3) channels have two conserved N-glycosylation sites which are vital for Kv3 channel activity, and primary motor neuron development. Our previous studies showed that the parental (NB_1) and N-glycan mutant (NB_1(-Mgat1), NB_1(-Mgat2), and NB_1(-Mgat3)) Neuroblastoma (NB) cell lines have compromised N-acetylglucosaminyltransferase activities: GnT-I, GnT-II, or GnT-III.

Functional analysis of N-acetylglucosaminyltransferase-I knockdown in 2D and 3D neuroblastoma cell cultures.

Tumor development can be promoted/suppressed by certain N-glycans attached to proteins at the cell surface. Here we examined aberrant neuronal properties in 2D and 3D rat neuroblastoma (NB) cell cultures with different N-glycan populations. Lectin binding studies revealed that the engineered N-glycosylation mutant cell line, NB_1(-Mgat1), expressed solely oligomannose N-glycans, and verified that the parental cell line, NB_1, and a previous engineered N-glycosylation mutant, NB_1(-Mgat2), expressed significant levels of higher order N-glycans, complex and hybrid N-glycans, respectively.