A novel cell adhesive protein engineered by insertion of the Arg-Gly-Asp-Ser tetrapeptide

Maeda, Toshinaga; Oyama, Rieko; Ichihara, Keiko; Kimizuka, Fusao; Kato, Ikunoshin; Titani, Koiti; Sekiguchi, Kiyotoshi

doi:https://doi.org/10.1016/S0021-9258(19)84803-2

A novel cell adhesive protein engineered by insertion of the Arg-Gly-Asp-Ser tetrapeptide

Maeda, Toshinaga; Oyama, Rieko; Ichihara, Keiko et al.

Journal of Biological Chemistry, 1989, 264(26), 15165-15168

アクセス数:566件（2025-07-19 07:40 集計）

固定URL: https://hdl.handle.net/11094/71443

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タイトル	A novel cell adhesive protein engineered by insertion of the Arg-Gly-Asp-Ser tetrapeptide
著者	NRID 1000020250342 1000020250342 著者名 Maeda, Toshinaga
	著者名 Oyama, Rieko
	著者名 Ichihara, Keiko 著者の別表記 Tanaka, Keiko
	著者名 Kimizuka, Fusao
	著者名 Kato, Ikunoshin
	NRID 1000060179942 1000060179942 著者名 Titani, Koiti
	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
内容	This research was originally published in the Journal of Biological Chemistry. T Maeda, R Oyama, K Ichihara-Tanaka, F Kimizuka, I Kato, K Titani and K Sekiguchi. A novel cell adhesive protein engineered by insertion of the Arg-Gly-Asp-Ser tetrapeptide. J. Biol. Chem. 1989; 264: 15165-15168 © the American Society for Biochemistry and Molecular Biology
抄録	A tetrapeptide Arg-Gly-Asp-Ser (RGDS) has been shown to be a versatile cell recognition signal of extracellular matrix components for the interaction with cells. We introduced the RGDS tetrapeptide into a truncated form of protein A, a staphylococcal immunoglobulin-binding protein, by inserting an oligonucleotide cassette encoding the tetrapeptide into the coding region of the protein A expression vector pRIT2T. The mutagenized protein was capable of not only binding to immunoglobulin G but also mediating cell attachment and spreading onto an inert substrate. Cell adhesion mediated by the mutagenized protein was inhibitable by a synthetic peptide Gly-Arg-Gly-Asp-Ser but not by a related peptide Gly-Arg-Gly-Glu-Ser, confirming that the inserted RGDS tetrapeptide served as a recognition signal for cell adhesion. Furthermore, the RGDS-containing protein was capable of adhering cells onto an immunoglobulin-coated surface which could not by itself support cell adhesion. Thus, the cell adhesive and immunoglobulin binding activities of the mutagenized protein appear to function coordinately. The protocol described here is essentially applicable to any protein and, therefore, provides a general principle in tailoring novel multifunctional proteins having cell adhesive activity.
出版者	American Society for Biochemistry and Molecular Biology
収録物名	Journal of Biological Chemistry
巻(号)	264(26)
ページ	15165-15168
刊行年月	1989-09
言語	英語
ハンドルURL	https://hdl.handle.net/11094/71443
eISSN	1083351X
NCID	AA1202441X
関連情報 (isIdenticalTo)	DOI (出版社版) https://doi.org/10.1016/S0021-9258(19)84803-2
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. 1989, 264(26), p. 15165-15168
DC.title	A novel cell adhesive protein engineered by insertion of the Arg-Gly-Asp-Ser tetrapeptide
DC.creator	Maeda, Toshinaga
	Oyama, Rieko
	Ichihara, Keiko
	Kimizuka, Fusao
	Kato, Ikunoshin
	Titani, Koiti
	Sekiguchi, Kiyotoshi
DC.creator	Tanaka, Keiko
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	1989-09
DC.identifier	https://doi.org/10.1016/S0021-9258(19)84803-2
DC.description	This research was originally published in the Journal of Biological Chemistry. T Maeda, R Oyama, K Ichihara-Tanaka, F Kimizuka, I Kato, K Titani and K Sekiguchi. A novel cell adhesive protein engineered by insertion of the Arg-Gly-Asp-Ser tetrapeptide. J. Biol. Chem. 1989; 264: 15165-15168 © the American Society for Biochemistry and Molecular Biology
DCTERMS.abstract	A tetrapeptide Arg-Gly-Asp-Ser (RGDS) has been shown to be a versatile cell recognition signal of extracellular matrix components for the interaction with cells. We introduced the RGDS tetrapeptide into a truncated form of protein A, a staphylococcal immunoglobulin-binding protein, by inserting an oligonucleotide cassette encoding the tetrapeptide into the coding region of the protein A expression vector pRIT2T. The mutagenized protein was capable of not only binding to immunoglobulin G but also mediating cell attachment and spreading onto an inert substrate. Cell adhesion mediated by the mutagenized protein was inhibitable by a synthetic peptide Gly-Arg-Gly-Asp-Ser but not by a related peptide Gly-Arg-Gly-Glu-Ser, confirming that the inserted RGDS tetrapeptide served as a recognition signal for cell adhesion. Furthermore, the RGDS-containing protein was capable of adhering cells onto an immunoglobulin-coated surface which could not by itself support cell adhesion. Thus, the cell adhesive and immunoglobulin binding activities of the mutagenized protein appear to function coordinately. The protocol described here is essentially applicable to any protein and, therefore, provides a general principle in tailoring novel multifunctional proteins having cell adhesive activity.
DC.format	71443
citation_title	A novel cell adhesive protein engineered by insertion of the Arg-Gly-Asp-Ser tetrapeptide
citation_author	Maeda, Toshinaga
	Oyama, Rieko
	Ichihara, Keiko
	Kimizuka, Fusao
	Kato, Ikunoshin
	Titani, Koiti
	Sekiguchi, Kiyotoshi
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	英語
citation_date	1989-09
citation_journal_title	Journal of Biological Chemistry
citation_volume	264
citation_issue	26
citation_firstpage	15165
citation_lastpage	15168
citation_doi	https://doi.org/10.1016/S0021-9258(19)84803-2
citation_public_url	https://hdl.handle.net/11094/71443

A novel cell adhesive protein engineered by insertion of the Arg-Gly-Asp-Ser tetrapeptide

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