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Synthesis of the glycosaminoglycan-protein linkage tetraosyl peptide moieties of betaglycan, which serve as a hexosamine acceptor for enzymatic glycosyl transfer
Title: | Synthesis of the glycosaminoglycan-protein linkage tetraosyl peptide moieties of betaglycan, which serve as a hexosamine acceptor for enzymatic glycosyl transfer |
Authors: | Tamura, Jun-ichi Browse this author | Nakamura-Yamamoto, Tomomi Browse this author | Nishimura, Yuko Browse this author | Mizumoto, Shuji Browse this author | Takahashi, Jun Browse this author | Sugahara, Kazuyuki Browse this author |
Keywords: | Chondroitin sulfate | Heparan sulfate | Glycoconjugate synthesis | Glycosyl transfer | N-Acetylgalactosaminyltransferase-I | α1,4-N-Acetylglucosaminyltransferase-I |
Issue Date: | 13-Oct-2010 |
Publisher: | Elsevier |
Journal Title: | Carbohydrate Research |
Volume: | 345 |
Issue: | 15 |
Start Page: | 2115 |
End Page: | 2123 |
Publisher DOI: | 10.1016/j.carres.2010.06.019 |
Abstract: | Betaglycan, also known as TGF-β type III receptor, is a membrane-anchored proteoglycan, which has two glycosaminoglycan (GAG) attachment sites (López-Casillas et.al. J. Cell Biol. 1994, 124, 557-568). Chondroitin sulfate (CS) or heparan sulfate (HS) can attach to the first site, Ser535, whereas only CS attaches to the second, Ser546. Although the mechanism behind the assembly of CS and HS is not fully understood, it has been reported that the assembly of HS requires not only a cluster of acidic residues but also hydrophobic residues located near the Ser-Gly attachment sites (Esko, J. D. Zhang, L Curr. Opin. Struct. Biol. 1996, 6, 663-670). To further understand the effects of amino acids close to the Ser residues of the GAG-attachment sites on the glycosyltransferases, two tetraosyl peptides derived from the CS attachment sites of betaglycan, GLcA-Gal-Gal-Xyl-SerGlyAspAsnGly (1) and GLcA-Gal-Gal-Xyl-SerGlyAspAsnGlyPheProGly (2), were synthesized, and used as donor substrates for β1,4-N-acetylgalactosaminyltransferase-I (β4GaINAcT-I) and α1,4-N-acetylglucosaminyltransferase-I (α4GlcNAcT-I). Both the chemically synthesized linkage region tetrasaccharides were far better acceptors for β4GalNAcT-I than for α4GlcNAcT-1 in vitro, although they also showed appreciable acceptor activity for α4GlcNAcT-I. |
Type: | article (author version) |
URI: | http://hdl.handle.net/2115/44158 |
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)
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Submitter: 菅原 一幸
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