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O-glycosylation pattern of CD24 from mouse brain

  • Christina Bleckmann , Hildegard Geyer , Annika Lieberoth , Frauke Splittstoesser , Yan Liu , Ten Feizi , Melitta Schachner , Ralf Kleene , Vernon Reinhold und Rudolf Geyer
Veröffentlicht/Copyright: 5. März 2009
Biological Chemistry
Aus der Zeitschrift Band 390 Heft 7

Abstract

The cell adhesion molecule CD24 is a highly glycosylated glycoprotein that plays important roles in the central nervous system, the immune system and in tumor biology. Since CD24 comprises only a short protein core of approximately 30 amino acids and low conservation among species, it has been proposed that the functions of CD24 are mediated by its glycosylation pattern. Our present study provides evidence that interaction of CD24 with the cell adhesion molecule L1 is mediated by O-linked glycans carrying α2,3-linked sialic acid. Furthermore, de-N-glycosylated CD24 was shown to promote or inhibit neurite outgrowth of cerebellar neurons or dorsal root ganglion neurons, respectively, to the same extent as untreated CD24. Therefore, this study is focused on the structural elucidation of the chemically released, permethylated CD24 O-glycans by electrospray ionization ion trap mass spectrometry. Our analyses revealed the occurrence of a diverse mixture of mucin-type and O-mannosyl glycans carrying, in part, functionally relevant epitopes, such as 3-linked sialic acid, disialyl motifs, LeX, sialyl-LeX or HNK-1 units. Hence, our data provide the basis for further studies on the contribution of carbohydrate determinants to CD24-mediated biological activities.


Corresponding author

Received: 2008-12-18
Accepted: 2009-2-5
Published Online: 2009-03-05
Published in Print: 2009-07-01

©2009 by Walter de Gruyter Berlin New York

Artikel in diesem Heft

  1. Guest Editorial
  2. Highlight: Perspectives in glycobiology
  3. Cell biology and glycosylation: protein targeting by O- and N-linked glycosylation
  4. Glycosylation- and phosphorylation-dependent intracellular transport of lysosomal hydrolases
  5. Glycosylation pattern of brush border-associated glycoproteins in enterocyte-like cells: involvement of complex-type N-glycans in apical trafficking
  6. Impact of glycosylation and detergent-resistant membranes on the function of intestinal sucrase-isomaltase
  7. MUC1 traverses apical recycling endosomes along the biosynthetic pathway in polarized MDCK cells
  8. Cell biology and glycosylation: carbohydrate-mediated recognition and signaling in cell proliferation and differentiation
  9. From structural to functional glycomics: core substitutions as molecular switches for shape and lectin affinity of N-glycans
  10. Brain development needs sugar: the role of polysialic acid in controlling NCAM functions
  11. Beyond glycosylation: sialic acid precursors act as signaling molecules and are involved in cellular control of differentiation of PC12 cells
  12. Glycosylation and disease
  13. Management of the human mucosal defensive barrier: evidence for glycan legislation
  14. Regulation and pathophysiological implications of UDP-GlcNAc 2-epimerase/ManNAc kinase (GNE) as the key enzyme of sialic acid biosynthesis
  15. GD3 synthase overexpression enhances proliferation and migration of MDA-MB-231 breast cancer cells
  16. Tumor-associated MUC1 glycopeptide epitopes are not subject to self-tolerance and improve responses to MUC1 peptide epitopes in MUC1 transgenic mice
  17. Protein-specific glycosylation and its control
  18. Protein-specific glycosylation: signal patches and cis-controlling peptidic elements
  19. O-glycosylation pattern of CD24 from mouse brain
  20. Advancements in analytical techniques
  21. Carbohydrate microarrays: key developments in glycobiology
  22. On-line nano-HPLC/ESI QTOF MS monitoring of α2–3 and α2–6 sialylation in granulocyte glycosphingolipidome
Heruntergeladen am 31.12.2025 von https://www.degruyterbrill.com/document/doi/10.1515/BC.2009.044/html
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