O-glycosylation pattern of CD24 from mouse brain

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  • Christina Bleckmann
    Institute of Biochemistry, Faculty of Medicine, University of Giessen, Friedrichstrasse 24, D-35392 Giessen, Germany
  • Hildegard Geyer
    Institute of Biochemistry, Faculty of Medicine, University of Giessen, Friedrichstrasse 24, D-35392 Giessen, Germany
  • Annika Lieberoth
    Zentrum für Molekulare Neurobiologie Hamburg, University of Hamburg, Martinistrasse 52, D-20246 Hamburg, Germany
  • Frauke Splittstoesser
    Zentrum für Molekulare Neurobiologie Hamburg, University of Hamburg, Martinistrasse 52, D-20246 Hamburg, Germany
  • Yan Liu
    Imperial College, The Glycosciences Laboratory, Northwick Park Institute for Medical Research, Watford Road, Harrow, Middlesex, HAI 3UJ, UK
  • Ten Feizi
    Imperial College, The Glycosciences Laboratory, Northwick Park Institute for Medical Research, Watford Road, Harrow, Middlesex, HAI 3UJ, UK
  • Melitta Schachner
    Zentrum für Molekulare Neurobiologie Hamburg, University of Hamburg, Martinistrasse 52, D-20246 Hamburg, Germany
  • Ralf Kleene
    Zentrum für Molekulare Neurobiologie Hamburg, University of Hamburg, Martinistrasse 52, D-20246 Hamburg, Germany
  • Vernon Reinhold
    Division of Molecular, Cellular and Biomedical Sciences, University of New Hampshire, Gregg Hall, 32 Colovos Road, Durham, NH 03824, USA
  • Rudolf Geyer
    Institute of Biochemistry, Faculty of Medicine, University of Giessen, Friedrichstrasse 24, D-35392 Giessen, Germany

Description

<jats:title>Abstract</jats:title> <jats:p>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, Le<jats:sup>X</jats:sup>, sialyl-Le<jats:sup>X</jats:sup> or HNK-1 units. Hence, our data provide the basis for further studies on the contribution of carbohydrate determinants to CD24-mediated biological activities.</jats:p>

Journal

  • bchm

    bchm 390 (7), 627-645, 2009-03-05

    Walter de Gruyter GmbH

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