Role of type III homology repeats in cell adhesive function within the cell-binding domain of fibronectin

Kimizuka, Fusao; Ohdate, Yoichi; Kawase, Yasutoshi; Shimojo, Tomoko; Taguchi, Yuki; Hashino, Kimikazu; Goto, Shoichi; Hashi, Hidetaka; Kato, Ikunoshin; Sekiguchi, Kiyotoshi; Titani, Koiti

doi:https://doi.org/10.1016/S0021-9258(18)49952-8

アクセス数:179件（2025-01-15 16:55 集計）

固定URL: https://hdl.handle.net/11094/71441

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タイトル	Role of type III homology repeats in cell adhesive function within the cell-binding domain of fibronectin
著者	著者名 Kimizuka, Fusao
	著者名 Ohdate, Yoichi
	著者名 Kawase, Yasutoshi
	著者名 Shimojo, Tomoko
	著者名 Taguchi, Yuki
	著者名 Hashino, Kimikazu
	著者名 Goto, Shoichi
	著者名 Hashi, Hidetaka
	著者名 Kato, Ikunoshin
	NRID 1000050187845 1000050187845 researchmap permalink read0054833 read0054833 Scopus Author ID 7201662709 7201662709 ORCID 0000-0002-6433-1410 0000-0002-6433-1410 著者名 Sekiguchi, Kiyotoshi
	NRID 1000060179942 1000060179942 著者名 Titani, Koiti
内容	This research was originally published in the Journal of Biological Chemistry. F Kimizuka, Y Ohdate, Y Kawase, T Shimojo, Y Taguchi, K Hashino, S Goto, H Hashi, I Kato, K Sekiguchi and K Titani. Role of type III homology repeats in cell adhesive function within the cell-binding domain of fibronectin. J. Biol. Chem. 1991; 266: 3045-3051 © the American Society for Biochemistry and Molecular Biology
抄録	Recombinant fibronectin (FN) fragments and their mutant proteins were produced to elucidate the role of type III homology repeats in cell adhesive activity within the cell-binding domain of FN. Cell adhesive activity of the 11.5-kDa fragment, the cell attachment site of the cell-binding domain, was less than 0.1% that of native FN despite the presence of the Arg-Gly-Asp-Ser sequence. The activity increased as type III homology repeats were added to the N terminus of the 11.5-kDa fragment, and a 52-kDa fragment with four additional type III repeats had almost the same activity of native FN. Deletion of Arg-Gly-Asp from the fully active fragments completely abolished the cell adhesive activity. Deletion of one or two repeats from the 52-kDa fragment affected the extent of the cell adhesive activity, the degree of the effect being inversely correlated with the distance of the deletion from the type III repeat containing Arg-Gly-Asp-Ser. Rearrangement of type III repeats caused much loss of activity. These results suggest that the number and kinds of type III repeats and their correct alignment rather than the putative synergistic site decide the extent of the specific cell adhesive activity.
出版者	American Society for Biochemistry and Molecular Biology
収録物名	Journal of Biological Chemistry
巻(号)	266(5)
ページ	3045-3051
刊行年月	1991-02
言語	英語
ハンドルURL	https://hdl.handle.net/11094/71441
eISSN	1083351X
NCID	AA1202441X
関連情報 (isIdenticalTo)	DOI (出版社版) https://doi.org/10.1016/S0021-9258(18)49952-8
アクセス権	open access
出版タイプ	Version of Record
カテゴリ	学術雑誌論文 Journal Article

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. 1991, 266(5), p. 3045-3051
DC.title	Role of type III homology repeats in cell adhesive function within the cell-binding domain of fibronectin
DC.creator	Kimizuka, Fusao
	Ohdate, Yoichi
	Kawase, Yasutoshi
	Shimojo, Tomoko
	Taguchi, Yuki
	Hashino, Kimikazu
	Goto, Shoichi
	Hashi, Hidetaka
	Kato, Ikunoshin
	Sekiguchi, Kiyotoshi
	Titani, Koiti
DC.publisher	American Society for Biochemistry and Molecular Biology
DC.language' scheme='DCTERMS.RFC1766	英語
DC.type' scheme='DCTERMS.DCMIType	text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	1991-02
DC.identifier	https://doi.org/10.1016/S0021-9258(18)49952-8
DC.description	This research was originally published in the Journal of Biological Chemistry. F Kimizuka, Y Ohdate, Y Kawase, T Shimojo, Y Taguchi, K Hashino, S Goto, H Hashi, I Kato, K Sekiguchi and K Titani. Role of type III homology repeats in cell adhesive function within the cell-binding domain of fibronectin. J. Biol. Chem. 1991; 266: 3045-3051 © the American Society for Biochemistry and Molecular Biology
DCTERMS.abstract	Recombinant fibronectin (FN) fragments and their mutant proteins were produced to elucidate the role of type III homology repeats in cell adhesive activity within the cell-binding domain of FN. Cell adhesive activity of the 11.5-kDa fragment, the cell attachment site of the cell-binding domain, was less than 0.1% that of native FN despite the presence of the Arg-Gly-Asp-Ser sequence. The activity increased as type III homology repeats were added to the N terminus of the 11.5-kDa fragment, and a 52-kDa fragment with four additional type III repeats had almost the same activity of native FN. Deletion of Arg-Gly-Asp from the fully active fragments completely abolished the cell adhesive activity. Deletion of one or two repeats from the 52-kDa fragment affected the extent of the cell adhesive activity, the degree of the effect being inversely correlated with the distance of the deletion from the type III repeat containing Arg-Gly-Asp-Ser. Rearrangement of type III repeats caused much loss of activity. These results suggest that the number and kinds of type III repeats and their correct alignment rather than the putative synergistic site decide the extent of the specific cell adhesive activity.
DC.format	71441
citation_title	Role of type III homology repeats in cell adhesive function within the cell-binding domain of fibronectin
citation_author	Kimizuka, Fusao
	Ohdate, Yoichi
	Kawase, Yasutoshi
	Shimojo, Tomoko
	Taguchi, Yuki
	Hashino, Kimikazu
	Goto, Shoichi
	Hashi, Hidetaka
	Kato, Ikunoshin
	Sekiguchi, Kiyotoshi
	Titani, Koiti
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	英語
citation_date	1991-02
citation_journal_title	Journal of Biological Chemistry
citation_volume	266
citation_issue	5
citation_firstpage	3045
citation_lastpage	3051
citation_doi	https://doi.org/10.1016/S0021-9258(18)49952-8
citation_public_url	https://hdl.handle.net/11094/71441

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