Development of a mouse monoclonal antibody against the chondroitin sulfate-protein linkage region derived from shark cartilage

Akatsu, Chizuru; Fongmoon, Duriya; Mizumoto, Shuji; Jacquinet, Jean-Claude; Kongtawelert, Prachya; Yamada, Shuhei; Sugahara, Kazuyuki

Development of a mouse monoclonal antibody against the chondroitin sulfate-protein linkage region derived from shark cartilage

Akatsu, Chizuru; Fongmoon, Duriya; Mizumoto, Shuji et al.

Glycoconjugate Journal, 2010, 27(4), 387-399

Permalink : https://hdl.handle.net/2115/49189

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アクセス権	open access
URI	https://hdl.handle.net/2115/49189
タイトル	Development of a mouse monoclonal antibody against the chondroitin sulfate-protein linkage region derived from shark cartilage
著者	Akatsu, Chizuru ; Fongmoon, Duriya ; Mizumoto, Shuji ; Jacquinet, Jean-Claude ; Kongtawelert, Prachya ; Yamada, Shuhei ; Sugahara, Kazuyuki
著者名 Akatsu, Chizuru
著者名 Fongmoon, Duriya
e-Rad_Researcher 40443973 著者名 Mizumoto, Shuji
著者名 Jacquinet, Jean-Claude
著者名 Kongtawelert, Prachya
e-Rad_Researcher 70240017 著者名 Yamada, Shuhei
e-Rad_Researcher 60154449 著者名 Sugahara, Kazuyuki
言語	英語
キーワード	Proteoglycans
	Glycosaminoglycans
	Chondroitin sulfate
	Heparan sulfate
	Dermatan sulfate
	Monoclonal antibody
発行日	2010-05
出版者	Springer Netherlands
収録物名	Glycoconjugate Journal
巻(号)	27(4)
ページ	387-399
抄録	Glycosaminoglycans (GAGs) like chondroitin sulfate (CS) and heparan sulfate (HS) are synthesized on the tetrasaccharide linkage region, GlcAβ1-3Galβ1-3Galβ1-4Xylβ1-O-Ser, of proteoglycans. The Xyl can be modified by 2-O-phosphate in both CS and HS, whereas the Gal residues can be sulfated at C-4 and/or C-6 in CS but not in HS. To study the roles of these modifications, monoclonal antibodies were developed against linkage glycopeptides of shark cartilage CS proteoglycans, and one was characterized in detail. This antibody bound hexa- and pentasaccharide-peptides more strongly than tetrasaccharide-peptides, suggesting the importance of GalNAc. It did not react to the CS linkage region modified by 4-O-sulfation. Its reactivity was not affected by treatment with chondro-4-sulfatase or alkaline phosphatase. The results of an ELISA using various proteoglycans and glycopeptides with different modifications suggested the recognition of 6-O-sulfate on the GalNAc and/or Gal residues. Treatments with exopeptidases did not affect the reactivity of the hexasaccharide-peptide fraction, whereas weak alkali to cleave the Xyl-Ser linkage completely abolished the binding activity, suggesting the importance of the Xy-Ser linkage for the binding. Furthermore, the antibody stained wild-type CHO cells, but not mutant cells deficient in xylosyltransferase required for the synthesis of the linkage region. These results suggest that the antibody recognizes the structure GalNAc-GlcA-Gal-Gal-Xyl-Ser that is modified by 6-O-sulfation on GalNAc and/or Gal. The antibody will be a useful tool for investigating the significance of the linkage region in the biosynthesis and/or intracellular transport of different GAG chains.
資源タイプ	学術雑誌論文
出版タイプ	Accepted Manuscript
権利情報	The final publication is available at www.springerlink.com
PISSN	0282-0080
EISSN	1573-4986
関連情報	PMID 20336366
関連情報 (isVersionOf)	出版社版DOI https://doi.org/10.1007/s10719-010-9286-1