Diverse expression of N-acetylglucosaminyltransferase V and complex-type β1,6-branched N-glycans in uveal and cutaneous melanoma cells
| Autor: | Magdalena Rydlewska, Małgorzata Przybyło, Anna Lityńska, Ewa Pocheć |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
Uveal Neoplasms
Glycan Glycosylation Skin Neoplasms N-Acetylglucosaminyltransferases General Biochemistry Genetics and Molecular Biology Malignant transformation Extracellular matrix chemistry.chemical_compound Cell Movement Polysaccharides Cell Line Tumor medicine Humans Gene Melanoma biology medicine.disease Molecular biology carbohydrates (lipids) Fibronectin Gene Expression Regulation Neoplastic chemistry Biochemistry Cutaneous melanoma biology.protein |
| Zdroj: | Acta biochimica Polonica. 62(2) |
| ISSN: | 1734-154X |
| Popis: | Although both uveal (UM) and cutaneous (CM) melanoma cells derive from the transformed melanocytes, their biology varies significantly in several aspects. Malignant transformation is frequently associated with alternations in cell glycosylation, in particular those concerning branched complex-type N-glycans. These changes occur principally in β1,4-N-acetylglucosaminyltransferase III (GnT-III) that catalyzes the synthesis of glycans with bisected N-acetylglucosamine (GlcNAc) and β1,6-N-acetylglucosaminyltransferase V (GnT-V) that is involved in forming β1,6-branched antenna in complex-type glycans. We searched for the reasons of a different behavior of CM and UM cells in the expression of GnT-III and GnT-V and their oligosaccharide products. Our study showed that UM cells have more β1,6-branched glycans than CM cells, what results from a higher expression of MGAT5 gene encoding GnT-V. The higher β1,6-branching of glycans in UM may contribute to their higher potential to migrate on fibronectin and weaker binding to main extracellular matrix proteins, observed in our previous studies. |
| Databáze: | OpenAIRE |
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