PUBLICATION

Chondroitin / dermatan sulfate modification enzymes in zebrafish development

Authors
Habicher, J., Haitina, T., Eriksson, I., Holmborn, K., Dierker, T., Ahlberg, P.E., Ledin, J.
ID
ZDB-PUB-150325-19
Date
2015
Source
PLoS One   10: e0121957 (Journal)
Registered Authors
Keywords
none
MeSH Terms
  • Animals
  • Chondroitin Sulfates/metabolism*
  • Chromatography, High Pressure Liquid
  • Chromatography, Reverse-Phase
  • Dermatan Sulfate/analogs & derivatives*
  • Dermatan Sulfate/metabolism
  • Embryonic Development*
  • Heparitin Sulfate/metabolism
  • In Situ Hybridization
  • Phylogeny
  • Sulfotransferases/metabolism*
  • Time Factors
  • Zebrafish/embryology*
  • Zebrafish/metabolism*
  • Zebrafish Proteins/metabolism*
PubMed
25793894 Full text @ PLoS One
Abstract
Chondroitin/dermatan sulfate (CS/DS) proteoglycans consist of unbranched sulfated polysaccharide chains of repeating GalNAc-GlcA/IdoA disaccharide units, attached to serine residues on specific proteins. The CS/DS proteoglycans are abundant in the extracellular matrix where they have essential functions in tissue development and homeostasis. In this report a phylogenetic analysis of vertebrate genes coding for the enzymes that modify CS/DS is presented. We identify single orthologous genes in the zebrafish genome for the sulfotransferases chst7, chst11, chst13, chst14, chst15 and ust and the epimerase dse. In contrast, two copies were found for mammalian sulfotransferases CHST3 and CHST12 and the epimerase DSEL, named chst3a and chst3b, chst12a and chst12b, dsela and dselb, respectively. Expression of CS/DS modification enzymes is spatially and temporally regulated with a large variation between different genes. We found that CS/DS 4-O-sulfotransferases and 6-O-sulfotransferases as well as CS/DS epimerases show a strong and partly overlapping expression, whereas the expression is restricted for enzymes with ability to synthesize di-sulfated disaccharides. A structural analysis further showed that CS/DS sulfation increases during embryonic development mainly due to synthesis of 4-O-sulfated GalNAc while the proportion of 6-O-sulfated GalNAc increases in later developmental stages. Di-sulfated GalNAc synthesized by Chst15 and 2-O-sulfated GlcA/IdoA synthesized by Ust are rare, in accordance with the restricted expression of these enzymes. We also compared CS/DS composition with that of heparan sulfate (HS). Notably, CS/DS biosynthesis in early zebrafish development is more dynamic than HS biosynthesis. Furthermore, HS contains disaccharides with more than one sulfate group, which are virtually absent in CS/DS.
Genes / Markers
Figures
Show all Figures
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping