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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

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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)

Submitter: 菅原 一幸

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