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The analysis of N-glycans of cell membrane proteins from human hematopoietic cell lines reveals distinctions in their pattern.
- Source :
- Biological Chemistry; Aug2012, Vol. 393 Issue 8, p731-747, 17p, 1 Black and White Photograph, 4 Charts, 7 Graphs
- Publication Year :
- 2012
-
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-acetyllucosamie 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. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 14316730
- Volume :
- 393
- Issue :
- 8
- Database :
- Complementary Index
- Journal :
- Biological Chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 83468659
- Full Text :
- https://doi.org/10.1515/hsz-2012-0195