The analysis of N-glycans of cell membrane proteins from human hematopoietic cell lines reveals distinctions in their pattern
-
Stefan O. Reinke
,
Marion Bayer
Abstract
Human cell lines are often different in their features and present variations in the glycosylation patterns of cell membrane proteins. Protein glycosylation is the most common posttranslational modification and plays a particular role in functionality and bioactivity. The key approach of this study is the comparative analysis of five hematopoietic cell lines for their N-glycosylation pattern. The N-glycans of membrane proteins were elucidated by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF-MS) and MALDI-TOF/TOF-MS analyses. Furthermore, the expression of a set of glycosyltransferases was determined via RT-PCR. The B-lymphoma BJA-B and promyelocytic HL-60 cell lines distinguish in levels and linkages of glycan-bound sialic acids. Furthermore, subclones of BJA-B and HL-60 cells, which completely lack UDP-N-acetylglucosamine 2-ēpimerase/N-acetylmannosamine kinase (GNE), the key enzyme of sialic acid biosynthesis, contained almost no sialylated N-glycans. Compared to wild-type cells, the GNE-deficient cells pres\xadented a similar cell surface N-glycosylation pattern in terms of antennarity and fucosylation. The Jurkat T-cell line revealed only partially sialylated N-glycans. Additionally, the different hematopoietic cell lines vary in their level of bisecting GlcNAcylation and antennary fucosylation with the quantities of bisecting N-acetylglucosamine (GlcNAc) and core fucose coinciding with the expression of GnT-III and FucT-VIII. Of note is the occurrence of N-acetyllactosamine (LacNAc) extensions on tetraantennary structures in GNE-deficient cell lines.
©2012 by Walter de Gruyter Berlin Boston
Artikel in diesem Heft
- Masthead
- Masthead
- Guest Editorial
- Highlight: Dolce vita – a sample from European glycobiology
- Highlight: Dolce Vita – A Sample From European Glycobiology
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- Fungal α-arabinofuranosidases of glycosyl hydrolase families 51 and 54 show a dual arabinofuranosyl- and galactofuranosyl-hydrolyzing activity
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- Research Articles/Short Communications
- Membranes, Lipids, Glycobiology
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Artikel in diesem Heft
- Masthead
- Masthead
- Guest Editorial
- Highlight: Dolce vita – a sample from European glycobiology
- Highlight: Dolce Vita – A Sample From European Glycobiology
- Complicated N-linked glycans in simple organisms
- Methylation – an uncommon modification of glycans
- Protein O-glycosylation analysis
- A sensitive gel-based global O-glycomics approach reveals high levels of mannosyl glycans in the high mass region of the mouse brain proteome
- Glycan profiles of the 27 N-glycosylation sites of the HIV envelope protein CN54gp140
- The analysis of N-glycans of cell membrane proteins from human hematopoietic cell lines reveals distinctions in their pattern
- The structure of the extracellular teichoic acids from the allergy-protective bacterium Lactococcus lactis G121
- Aminoquinolines as fluorescent labels for hydrophilic interaction liquid chromatography of oligosaccharides
- Fungal α-arabinofuranosidases of glycosyl hydrolase families 51 and 54 show a dual arabinofuranosyl- and galactofuranosyl-hydrolyzing activity
- Glycoengineering the N-acyl side chain of sialic acid of human erythropoietin affects its resistance to sialidase
- Shiga toxin glycosphingolipid receptor expression and toxin susceptibility of human pancreatic ductal adenocarcinomas of differing origin and differentiation
- Review
- Structural determinants of the eosinophil cationic protein antimicrobial activity
- Research Articles/Short Communications
- Membranes, Lipids, Glycobiology
- Anticancer peptide NK-2 targets cell surface sulphated glycans rather than sialic acids
- Proteolysis
- Extracellular aspartic protease SAP2 of Candida albicans yeast cleaves human kininogens and releases proinflammatory peptides, Met-Lys-bradykinin and des-Arg9-Met-Lys-bradykinin
