Back to Search Start Over

Developmental regulation of oligosialylation in zebrafish

Authors :
Ken Kitajima
Chang-Jen Huang
Lan-Yi Chang
Yann Guérardel
Chihiro Sato
Kay-Hooi Khoo
Anne Harduin-Lepers
Institute of Biological Chemistry (IBC Sinica)
Academia Sinica
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF)
Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA)
Institute of Biochemical Sciences
National Taiwan University [Taiwan] (NTU)
Department of Bioengineering Sciences
Nagoya University
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF)
Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS)
Université de Lille-Centre National de la Recherche Scientifique (CNRS)
Source :
Glycoconjugate Journal, Glycoconjugate Journal, Springer Verlag, 2009, 26 (3), pp.247-61. ⟨10.1007/s10719-008-9161-5⟩, Glycoconjugate Journal, Springer Verlag, 2009, 26 (3), pp.247-261. ⟨10.1007/s10719-008-9161-5⟩, Glycoconjugate Journal, 2009, 26 (3), pp.247-261. ⟨10.1007/s10719-008-9161-5⟩
Publication Year :
2009
Publisher :
HAL CCSD, 2009.

Abstract

International audience; Zebrafish appears as a relevant model for the functional study of glycoconjugates along vertebrate's development. Indeed, as a prelude to such studies, we have previously identified a vast array of potentially stage-specific glycoconjugates, which structures are reminiscent of glycosylation pathways common to all vertebrates. In the present study, we have focused on the identification and regulation of major protein and lipids associated α2-8-linked oligosialic acids motifs in the early development of zebrafish. By a combination of partial hydrolysis, anion exchange HPLC-FD and mass spectrometry, we demonstrated that glycoproteins and glycolipids differed by the extent and the nature of their substituting oligosialylated sequences. Furthermore, relative quantifications showed that α2-8-linked sialylation was differentially regulated in both families of glycoconjugates along development. Accordingly, we established that α2,8-sialyltransferase mRNA levels was directly correlated with changes of α2,8-sialylation status of glycolipids, but independent of those observed on major glycoproteins that appear to originate from the mother.

Details

Language :
English
ISSN :
02820080 and 15734986
Database :
OpenAIRE
Journal :
Glycoconjugate Journal, Glycoconjugate Journal, Springer Verlag, 2009, 26 (3), pp.247-61. ⟨10.1007/s10719-008-9161-5⟩, Glycoconjugate Journal, Springer Verlag, 2009, 26 (3), pp.247-261. ⟨10.1007/s10719-008-9161-5⟩, Glycoconjugate Journal, 2009, 26 (3), pp.247-261. ⟨10.1007/s10719-008-9161-5⟩
Accession number :
edsair.doi.dedup.....7252eb29cfeb1a76cfbb5333f1c1f146