Change search
ReferencesLink to record
Permanent link

Direct link
Nematodes join the family of chondroitin sulfate-synthesizing organisms: Identification of an active chondroitin sulfotransferase in Caenorhabditis elegans
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology. Uppsala University, Science for Life Laboratory, SciLifeLab.
Boston Univ, Dept Biochem, Ctr Biomed Mass Spectrometry, Med Campus, Boston, MA 02215 USA..
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Evolution and Developmental Biology. Uppsala University, Science for Life Laboratory, SciLifeLab.
Boston Univ, Dept Biochem, Ctr Biomed Mass Spectrometry, Med Campus, Boston, MA 02215 USA..
Show others and affiliations
2016 (English)In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 6, 34662Article in journal (Refereed) Published
Abstract [en]

Proteoglycans are proteins that carry sulfated glycosaminoglycans (GAGs). They help form and maintain morphogen gradients, guiding cell migration and differentiation during animal development. While no sulfated GAGs have been found in marine sponges, chondroitin sulfate (CS) and heparan sulfate (HS) have been identified in Cnidarians, Lophotrocozoans and Ecdysozoans. The general view that nematodes such as Caenorhabditis elegans, which belong to Ecdysozoa, produce HS but only chondroitin without sulfation has therefore been puzzling. We have analyzed GAGs in C. elegans using reversed-phase ion-pairing HPLC, mass spectrometry and immunohistochemistry. Our analyses included wild type C. elegans but also a mutant lacking two HS sulfotransferases (hst-6 hst-2), as we suspected that the altered HS structure could boost CS sulfation. We could indeed detect sulfated CS in both wild type and mutant nematodes. While 4-O-sulfation of galactosamine dominated, we also detected 6-O-sulfated galactosamine residues. Finally, we identified the product of the gene C41C4.1 as a C. elegans CS-sulfotransferase and renamed it chst-1 (CarboHydrate SulfoTransferase) based on loss of CS-4-O-sulfation in a C41C4.1 mutant and in vitro sulfotransferase activity of recombinant C41C4.1 protein. We conclude that C. elegans indeed manufactures CS, making this widely used nematode an interesting model for developmental studies involving CS.

Place, publisher, year, edition, pages
2016. Vol. 6, 34662
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:uu:diva-306734DOI: 10.1038/srep34662ISI: 000384654100001PubMedID: 27703236OAI: oai:DiVA.org:uu-306734DiVA: diva2:1045558
Funder
Swedish Research Council
Available from: 2016-11-10 Created: 2016-11-03 Last updated: 2016-11-10Bibliographically approved

Open Access in DiVA

fulltext(1717 kB)32 downloads
File information
File name FULLTEXT01.pdfFile size 1717 kBChecksum SHA-512
b53cf3324ebd29e499f4e0317cda5fadde4bcab9f70a9bf5031fc37789ff2507bebe9270c5fffb4e230a5552e5b786646fe228f5e565f1335a8eda3c73832095
Type fulltextMimetype application/pdf

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Dierker, TabeaHaitina, TatjanaHinas, AndreaKjellén, Lena
By organisation
Department of Medical Biochemistry and MicrobiologyScience for Life Laboratory, SciLifeLabEvolution and Developmental BiologyMicrobiology
In the same journal
Scientific Reports
Biological Sciences

Search outside of DiVA

GoogleGoogle Scholar
Total: 32 downloads
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 50 hits
ReferencesLink to record
Permanent link

Direct link