Document Detail

O-glycosylation pattern of CD24 from mouse brain.
MedLine Citation:
PMID:  19284289     Owner:  NLM     Status:  MEDLINE    
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 alpha2,3-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(X), sialyl-Le(X) or HNK-1 units. Hence, our data provide the basis for further studies on the contribution of carbohydrate determinants to CD24-mediated biological activities.
Christina Bleckmann; Hildegard Geyer; Annika Lieberoth; Frauke Splittstoesser; Yan Liu; Ten Feizi; Melitta Schachner; Ralf Kleene; Vernon Reinhold; Rudolf Geyer
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biological chemistry     Volume:  390     ISSN:  1431-6730     ISO Abbreviation:  Biol. Chem.     Publication Date:  2009 Jul 
Date Detail:
Created Date:  2009-06-30     Completed Date:  2009-08-18     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9700112     Medline TA:  Biol Chem     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  627-45     Citation Subset:  IM    
Institute of Biochemistry, Faculty of Medicine, University of Giessen, D-35392 Giessen, Germany.
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MeSH Terms
Antigens, CD24 / immunology,  metabolism*
Antigens, CD57 / immunology
Carbohydrate Sequence
Epitopes / immunology
Mannose / chemistry
Mass Spectrometry
Molecular Sequence Data
Neural Cell Adhesion Molecule L1 / metabolism
Neurites / metabolism
Oxygen / metabolism*
Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase / metabolism
Polysaccharides / analysis,  chemistry,  metabolism
Sugar Alcohols / metabolism
Reg. No./Substance:
0/Antigens, CD24; 0/Antigens, CD57; 0/Epitopes; 0/Neural Cell Adhesion Molecule L1; 0/Polysaccharides; 0/Sugar Alcohols; 31103-86-3/Mannose; 7782-44-7/Oxygen; EC Asparagine Amidase

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