O-glycosylation pattern of CD24 from mouse brain.
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O-glycosylation pattern of CD24 from mouse brain. / Bleckmann, Christina; Geyer, Hildegard; Lieberoth, Annika; Splittstoesser, Frauke; Liu, Yan; Feizi, Ten; Schachner, Melitta; Kleene, Ralf; Reinhold, Vernon; Geyer, Rudolf.
in: BIOL CHEM, Jahrgang 390, Nr. 7, 7, 2009, S. 627-645.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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T1 - O-glycosylation pattern of CD24 from mouse brain.
AU - Bleckmann, Christina
AU - Geyer, Hildegard
AU - Lieberoth, Annika
AU - Splittstoesser, Frauke
AU - Liu, Yan
AU - Feizi, Ten
AU - Schachner, Melitta
AU - Kleene, Ralf
AU - Reinhold, Vernon
AU - Geyer, Rudolf
PY - 2009
Y1 - 2009
N2 - 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.
AB - 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.
M3 - SCORING: Zeitschriftenaufsatz
VL - 390
SP - 627
EP - 645
JO - BIOL CHEM
JF - BIOL CHEM
SN - 1431-6730
IS - 7
M1 - 7
ER -
