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Title
  • Structural and functional changes of sulfated glycosaminoglycans in Xenopus laevis during embryogenesis
Creator

Yamada, Shuhei

Onishi, Masako

Fujinawa, Reiko

Tadokoro, Yuko

Okabayashi, Koji

Asashima, Makoto

Sugahara, Kazuyuki

Rights
    • This is a pre-copy-editing, author-produced PDF of an article accepted for publication in Glycobiology following peer review. The definitive publisher-authenticated version 19(5):488-498, May 2009 is available online at: http://dx.doi.org/10.1093/glycob/cwp005
Subject
  • Other Xenopus laevis
  • Other chondroitin sulfate
  • Other heparan sulfate
  • Other glycosaminoglycan
  • Other embryogenesis
  • NDC 491
Description
Other
  • Xenopus laevis is an excellent animal for analyzing early vertebrate development. Various effects of glycosaminoglycans (GAGs) on growth factor-related cellular events during embryogenesis have been demonstrated in Xenopus. To elucidate the relationship between alterations in fine structure and changes in the specificity of growth factor-binding during Xenopus development, heparan sulfate (HS) and chondroitin/dermatan sulfate (CS/DS) chains were isolated at four different embryonic stages and their structure and growth factor-binding capacities were compared. The total amounts of both HS and CS/DS chains decreased from the pre-midblastula transition to the gastrula stage, but increased exponentially during the following developmental stages. The length of HS chains was not significantly affected by development, whereas that of CS/DS chains increased with development. The disaccharide composition of GAGs in embryos also changed during development. The degree of sulfation of the HS chains gradually decreased with development. The predominant sulfation position in the CS/DS chains shifted from C4 to C6 of GalNAc during embryogenesis. Growth factor-binding experiments using a BIAcore system demonstrated that GAGs bound growth factors including fibroblast growth factors-1, and -2, midkine, and pleiotrophin, with comparable affinities. These affinities significantly varied during development, although the correlation between the structural alterations of GAGs and the change in the ability to bind growth factors remains to be clarified. Expression of saccharide sequences, which specifically interact with a growth factor, might be regulated during development.
PublisherOxford University Press
Date Issued 2009-05
Languageeng
NIItypejournal article
VersiontypeAM
Identifier URI http://hdl.handle.net/2115/43036
Relation
  • isIdenticalTo PMID 19190026
  • isIdenticalTo DOI https://doi.org/10.1093/glycob/cwp005
Journal
    • ISSN 0959-6658
    • ISSN 1460-2423
    • Glycobiology
    19(5), 488-498
File
Oaidate2019-03-15T05:20:33Z