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

Number of Access:594（2025-08-18 14:07 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/71443

Link to primary information

File	Format	Terms of use	Size	Views	Date.Available	Description	information
JBC_1989_15165_8	pdf	None	3.26 MB	164	2019.03.20

Item Information

Output File Export EndNote Basic Export Mendeley

Title	A novel cell adhesive protein engineered by insertion of the Arg-Gly-Asp-Ser tetrapeptide
Creator	NRID 1000020250342 1000020250342 CreatorName Maeda, Toshinaga
	CreatorName Oyama, Rieko
	CreatorName Ichihara, Keiko Creator.Alternative Tanaka, Keiko
	CreatorName Kimizuka, Fusao
	CreatorName Kato, Ikunoshin
	NRID 1000060179942 1000060179942 CreatorName Titani, Koiti
	NRID 1000050187845 1000050187845 researchmap permalink read0054833 read0054833 Scopus Author ID 7201662709 7201662709 ORCID 0000-0002-6433-1410 0000-0002-6433-1410 CreatorName Sekiguchi, Kiyotoshi
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
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.
Publisher	American Society for Biochemistry and Molecular Biology
Source Title	Journal of Biological Chemistry
Volume (Issue)	264(26)
Page	15165-15168
Date of Issued	1989-09
Language	English
Handle URL	https://hdl.handle.net/11094/71443
eISSN	1083351X
NCID	AA1202441X
Relation.isIdenticalTo	DOI (Publisher Version) https://doi.org/10.1016/S0021-9258(19)84803-2
Access Rights	open access
oaire:version	Version of Record
Category	学術雑誌論文 Journal Article

Resource Type	journal article
Local Type	Journal Article
DCMI Type	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	English
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	English
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

Link to primary information

Item Information

Show details