PUBLICATION
Developmental regulation of oligosialylation in zebrafish
- Authors
- Chang, L.Y., Harduin-Lepers, A., Kitajima, K., Sato, C., Huang, C.J., Khoo, K.H., and Guérardel, Y.
- ID
- ZDB-PUB-080826-22
- Date
- 2009
- Source
- Glycoconjugate journal 26(3): 247-261 (Journal)
- Registered Authors
- Huang, Chang-Jen
- Keywords
- α2,8-sialylation, α2,8-sialyltransferases, Neu5Ac/Neu5Gc, Zebrafish, Early development, Glycolipids, Glycoproteins
- MeSH Terms
-
- Animals
- Embryo, Nonmammalian/enzymology
- Embryonic Development*
- Gene Expression Regulation, Developmental
- Gene Expression Regulation, Enzymologic
- Glycolipids/chemistry
- Glycolipids/metabolism
- Glycoproteins/metabolism
- N-Acetylneuraminic Acid/chemistry
- N-Acetylneuraminic Acid/metabolism*
- Neuraminidase/metabolism
- Polysaccharides/chemistry
- Polysaccharides/metabolism
- RNA, Messenger/genetics
- RNA, Messenger/metabolism
- Sialyltransferases/genetics
- Sialyltransferases/metabolism
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
- Zebrafish/embryology*
- Zebrafish/metabolism*
- PubMed
- 18704683 Full text @ Glycoconj. J.
Citation
Chang, L.Y., Harduin-Lepers, A., Kitajima, K., Sato, C., Huang, C.J., Khoo, K.H., and Guérardel, Y. (2009) Developmental regulation of oligosialylation in zebrafish. Glycoconjugate journal. 26(3):247-261.
Abstract
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 alpha2-8-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 alpha2-8-linked sialylation was differentially regulated in both families of glycoconjugates along development. Accordingly, we established that alpha2,8-sialyltransferase mRNA levels was directly correlated with changes of alpha2,8-sialylation status of glycolipids, but independent of those observed on major glycoproteins that appear to originate from the mother.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping