Binding of fibronectin and its proteolytic fragments to glycosaminoglycans : Exposure of cryptic glycosaminoglycan-binding domains upon limited proteolysis

Sekiguchi, Kiyotoshi; Hakomori, Sen-itiroh; Funahashi, Miyuki; Matsumoto, Isamu; Seno, Nobuko

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タイトル	Binding of fibronectin and its proteolytic fragments to glycosaminoglycans : Exposure of cryptic glycosaminoglycan-binding domains upon limited proteolysis
著者	Sekiguchi, Kiyotoshi Sekiguchi, Kiyotoshi
	Hakomori, Sen-itiroh Hakomori, Sen-itiroh
	Funahashi, Miyuki Funahashi, Miyuki
	Matsumoto, Isamu Matsumoto, Isamu
	Seno, Nobuko Seno, Nobuko
内容	This research was originally published in the Journal of Biological Chemistry. K Sekiguchi, S Hakomori, M Funahashi, I Matsumoto and N Seno. Binding of fibronectin and its proteolytic fragments to glycosaminoglycans : Exposure of cryptic glycosaminoglycan-binding domains upon limited proteolysis. J. Biol. Chem. 1983; 258: 14359-14365 © the American Society for Biochemistry and Molecular Biology
抄録	Binding of intact plasma fibronectin and its proteolytic fragments to glycosaminoglycans immobilized on agarose beads was systematically compared at different ionic strengths. In low ionic strength buffer, intact fibronectin bound to heparin and high sulfated heparan sulfate, but not to low sulfated heparan sulfate, dermatan sulfate, chondroitin sulfates A and C, or hyaluronic acid. Fractionation of the thermolysin digest of fibronectin on the glycosaminoglycan-Sepharoses at low ionic strength revealed that three groups of fragments, i.e. Mr = 150,000-140,000, 24,000, and 16,000 (150K-140K, 24K, and 16K) fragments, were capable of binding to glycosaminoglycans with different specificities and affinities. The 150K-140K fragments exhibited the same specificities as intact fibronectin, binding only to heparin and high sulfated heparan sulfate. However, the 24K fragment bound not only to these two glycosaminoglycans but also to low sulfated heparan sulfate and other glycosaminoglycans as well. The 16K fragments were also capable of binding to most glycosaminoglycans with lower affinity than the 24K fragment. These results suggest that the binding sites in the 24K and 16K fragments are cryptic in the intact protein, but are exposed after limited proteolysis. The binding of fibronectin and its fragments to glycosaminoglycans is dependent on the ionic strength. At physiologic ionic strength, only heparin-Sepharose could bind intact fibronectin. Similarly, only heparin-Sepharose could bind the 150K-140K and 24K fragments, but not the 16K fragments, at the same ionic condition. Other glycosaminoglycan-Sepharoses did not retain significant amounts of any of the fibronectin fragments, suggesting that the affinity of plasma fibronectin and its fragments to heparan sulfate and other glycosaminoglycans, except heparin, is not strong enough to achieve stable mono- (or di-) valent binding under physiologic conditions.
公開者	American Society for Biochemistry and Molecular Biology
掲載誌名	Journal of Biological Chemistry
巻	258
号	23
開始ページ	14359
終了ページ	14365
刊行年月	1983-12
ISSN	1083351X
NCID	AA1202441X
URL	http://hdl.handle.net/11094/71446
関連情報 (references)	http://www.jbc.org/content/258/23/14359
言語	英語
カテゴリ	学術雑誌論文 Journal Article

著者版フラグ	publisher
NII資源タイプ	学術雑誌論文
ローカル資源タイプ	学術雑誌論文
dcmi資源タイプ	text
DCTERMS.bibliographicCitation	Journal of Biological Chemistry.258(23) P.14359-P.14365
DC.title	Binding of fibronectin and its proteolytic fragments to glycosaminoglycans : Exposure of cryptic glycosaminoglycan-binding domains upon limited proteolysis
DC.creator	Sekiguchi, Kiyotoshi
	Hakomori, Sen-itiroh
	Funahashi, Miyuki
	Matsumoto, Isamu
	Seno, Nobuko
DC.publisher	American Society for Biochemistry and Molecular Biology
DC.language" scheme="DCTERMS.RFC1766	英語
DCTERMS.issued" scheme="DCTERMS.W3CDTF	1983-12
DC.identifier" scheme="DCTERMS.URI	http://hdl.handle.net/11094/71446
DC.description	This research was originally published in the Journal of Biological Chemistry. K Sekiguchi, S Hakomori, M Funahashi, I Matsumoto and N Seno. Binding of fibronectin and its proteolytic fragments to glycosaminoglycans : Exposure of cryptic glycosaminoglycan-binding domains upon limited proteolysis. J. Biol. Chem. 1983; 258: 14359-14365 © the American Society for Biochemistry and Molecular Biology
DCTERMS.abstract	Binding of intact plasma fibronectin and its proteolytic fragments to glycosaminoglycans immobilized on agarose beads was systematically compared at different ionic strengths. In low ionic strength buffer, intact fibronectin bound to heparin and high sulfated heparan sulfate, but not to low sulfated heparan sulfate, dermatan sulfate, chondroitin sulfates A and C, or hyaluronic acid. Fractionation of the thermolysin digest of fibronectin on the glycosaminoglycan-Sepharoses at low ionic strength revealed that three groups of fragments, i.e. Mr = 150,000-140,000, 24,000, and 16,000 (150K-140K, 24K, and 16K) fragments, were capable of binding to glycosaminoglycans with different specificities and affinities. The 150K-140K fragments exhibited the same specificities as intact fibronectin, binding only to heparin and high sulfated heparan sulfate. However, the 24K fragment bound not only to these two glycosaminoglycans but also to low sulfated heparan sulfate and other glycosaminoglycans as well. The 16K fragments were also capable of binding to most glycosaminoglycans with lower affinity than the 24K fragment. These results suggest that the binding sites in the 24K and 16K fragments are cryptic in the intact protein, but are exposed after limited proteolysis. The binding of fibronectin and its fragments to glycosaminoglycans is dependent on the ionic strength. At physiologic ionic strength, only heparin-Sepharose could bind intact fibronectin. Similarly, only heparin-Sepharose could bind the 150K-140K and 24K fragments, but not the 16K fragments, at the same ionic condition. Other glycosaminoglycan-Sepharoses did not retain significant amounts of any of the fibronectin fragments, suggesting that the affinity of plasma fibronectin and its fragments to heparan sulfate and other glycosaminoglycans, except heparin, is not strong enough to achieve stable mono- (or di-) valent binding under physiologic conditions.
citation_title	Binding of fibronectin and its proteolytic fragments to glycosaminoglycans : Exposure of cryptic glycosaminoglycan-binding domains upon limited proteolysis
citation_author	Sekiguchi, Kiyotoshi
	Hakomori, Sen-itiroh
	Funahashi, Miyuki
	Matsumoto, Isamu
	Seno, Nobuko
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	英語
citation_date	1983-12
citation_journal_title	Journal of Biological Chemistry
citation_volume	258
citation_issue	23
citation_firstpage	14359
citation_lastpage	14365
citation_issn	1083351X
citation_public_url	http://hdl.handle.net/11094/71446

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