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, Rudolf Geyer

Research output: Contribution to journalArticlepeer-review

71 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)627-645
Number of pages19
JournalBiological Chemistry
Issue number7
StatePublished - Jul 1 2009
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Clinical Biochemistry


  • CD24
  • ESI-MS
  • HNK-1
  • Mass spectrometry
  • Mucin type O-glycans
  • O-mannosyl glycans


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