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

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/43036

Title: Structural and functional changes of sulfated glycosaminoglycans in Xenopus laevis during embryogenesis
Authors: Yamada, Shuhei Browse this author →KAKEN DB
Onishi, Masako Browse this author
Fujinawa, Reiko Browse this author
Tadokoro, Yuko Browse this author
Okabayashi, Koji Browse this author
Asashima, Makoto Browse this author
Sugahara, Kazuyuki Browse this author →KAKEN DB
Keywords: Xenopus laevis
chondroitin sulfate
heparan sulfate
glycosaminoglycan
embryogenesis
Issue Date: May-2009
Publisher: Oxford University Press
Journal Title: Glycobiology
Volume: 19
Issue: 5
Start Page: 488
End Page: 498
Publisher DOI: 10.1093/glycob/cwp005
PMID: 19190026
Abstract: 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.
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
Type: article (author version)
URI: http://hdl.handle.net/2115/43036
Appears in Collections:生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 山田 修平

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