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Chondroitin / dermatan sulfate modification enzymes in zebrafish development.

Habicher J, Haitina T, Eriksson I, Holmborn K, Dierker T, Ahlberg PE, Ledin J - PLoS ONE (2015)

Bottom Line: 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.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.We also compared CS/DS composition with that of heparan sulfate (HS).

View Article: PubMed Central - PubMed

Affiliation: Department of Organismal Biology, Science for Life Laboratory, Uppsala University, Uppsala, Sweden.

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.

No MeSH data available.


Related in: MedlinePlus

Whole mount in situ hybridization of the CS/DS 6-O-sulfotransferases chst3a (A), chst3b (B) and chst7 (C).All images show lateral views, if not otherwise stated in the figure. hb: hindbrain, n: notochord, ov: otic vesicle, pc: pharyngeal cartilage, pf: pectoral fin, tb: tailbud, s: somites
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pone.0121957.g004: Whole mount in situ hybridization of the CS/DS 6-O-sulfotransferases chst3a (A), chst3b (B) and chst7 (C).All images show lateral views, if not otherwise stated in the figure. hb: hindbrain, n: notochord, ov: otic vesicle, pc: pharyngeal cartilage, pf: pectoral fin, tb: tailbud, s: somites

Mentions: chst3a, chst3b and chst7 lack staining at the 2-cell stage (¾ hpf) indicating no maternally deposited mRNA (Fig. 4). The chst3a probe shows weak overall staining at the 5- and 15-somite stages (11–16 hpf), as well as strong somite staining (Fig. 4A). At 24 and 48 hpf staining is limited to the head and the pectoral fins (at 48 hpf). At 72 hpf, staining is restricted to the pharyngeal cartilages and the pectoral fins (Fig. 4A). chst3b displays only very weak staining from the 5 somite stage (11 hpf) to 48 hpf (Fig. 4B). At 72 hpf, the pectoral fins show increased staining (Fig. 4B). At the 5- and 15-somite stage (11–16 hpf), the chst7 probe strongly stains the notochord and tail bud (Fig. 4C). At 24 hpf, staining is still detected at the tail bud but starts shifting to the head region where it gets prominent from 36 hpf (Fig. 4C). At 48 and 72 hpf the hindbrain stains strongly as well as the pharyngeal cartilages. (Fig. 4C).


Chondroitin / dermatan sulfate modification enzymes in zebrafish development.

Habicher J, Haitina T, Eriksson I, Holmborn K, Dierker T, Ahlberg PE, Ledin J - PLoS ONE (2015)

Whole mount in situ hybridization of the CS/DS 6-O-sulfotransferases chst3a (A), chst3b (B) and chst7 (C).All images show lateral views, if not otherwise stated in the figure. hb: hindbrain, n: notochord, ov: otic vesicle, pc: pharyngeal cartilage, pf: pectoral fin, tb: tailbud, s: somites
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4368567&req=5

pone.0121957.g004: Whole mount in situ hybridization of the CS/DS 6-O-sulfotransferases chst3a (A), chst3b (B) and chst7 (C).All images show lateral views, if not otherwise stated in the figure. hb: hindbrain, n: notochord, ov: otic vesicle, pc: pharyngeal cartilage, pf: pectoral fin, tb: tailbud, s: somites
Mentions: chst3a, chst3b and chst7 lack staining at the 2-cell stage (¾ hpf) indicating no maternally deposited mRNA (Fig. 4). The chst3a probe shows weak overall staining at the 5- and 15-somite stages (11–16 hpf), as well as strong somite staining (Fig. 4A). At 24 and 48 hpf staining is limited to the head and the pectoral fins (at 48 hpf). At 72 hpf, staining is restricted to the pharyngeal cartilages and the pectoral fins (Fig. 4A). chst3b displays only very weak staining from the 5 somite stage (11 hpf) to 48 hpf (Fig. 4B). At 72 hpf, the pectoral fins show increased staining (Fig. 4B). At the 5- and 15-somite stage (11–16 hpf), the chst7 probe strongly stains the notochord and tail bud (Fig. 4C). At 24 hpf, staining is still detected at the tail bud but starts shifting to the head region where it gets prominent from 36 hpf (Fig. 4C). At 48 and 72 hpf the hindbrain stains strongly as well as the pharyngeal cartilages. (Fig. 4C).

Bottom Line: 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.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.We also compared CS/DS composition with that of heparan sulfate (HS).

View Article: PubMed Central - PubMed

Affiliation: Department of Organismal Biology, Science for Life Laboratory, Uppsala University, Uppsala, Sweden.

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.

No MeSH data available.


Related in: MedlinePlus