ADAMTSL-6 Is a Novel Extracellular Matrix Protein That Binds to Fibrillin-1 and Promotes Fibrillin-1 Fibril Formation

Tsutsui, Ko; Manabe, Ri-ichiroh; Yamada, Tomiko; Nakano, Itsuko; Oguri, Yasuko; Keene, Douglas R.; Sengle, Gerhard; Sakai, Lynn Y.; Sekiguchi, Kiyotoshi

doi:https://doi.org/10.1074/jbc.M109.076919

ADAMTSL-6 Is a Novel Extracellular Matrix Protein That Binds to Fibrillin-1 and Promotes Fibrillin-1 Fibril Formation

Tsutsui, Ko; Manabe, Ri-ichiroh; Yamada, Tomiko et al.

Journal of Biological Chemistry, 2010, 285(7), 4870-4882

アクセス数:960件（2025-07-13 04:58 集計）

固定URL: https://hdl.handle.net/11094/71423

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タイトル	ADAMTSL-6 Is a Novel Extracellular Matrix Protein That Binds to Fibrillin-1 and Promotes Fibrillin-1 Fibril Formation
著者	著者名 Tsutsui, Ko
	NRID 1000030280837 1000030280837 著者名 Manabe, Ri-ichiroh
	著者名 Yamada, Tomiko
	著者名 Nakano, Itsuko
	著者名 Oguri, Yasuko
	著者名 Keene, Douglas R.
	著者名 Sengle, Gerhard
	著者名 Sakai, Lynn Y.
	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. Ko Tsutsui, Ri-ichiroh Manabe, Tomiko Yamada, Itsuko Nakano, Yasuko Oguri, Douglas R. Keene, Gerhard Sengle, Lynn Y. Sakai and Kiyotoshi Sekiguchi. ADAMTSL-6 Is a Novel Extracellular Matrix Protein That Binds to Fibrillin-1 and Promotes Fibrillin-1 Fibril Formation. J. Biol. Chem. 2010; 285: 4870-4882 © the American Society for Biochemistry and Molecular Biology
抄録	ADAMTS (A disintegrin and metalloproteinase with thrombospondin motifs)-like (ADAMTSL) proteins, a subgroup of the ADAMTS superfamily, share several domains with ADAMTS proteinases, including thrombospondin type I repeats, a cysteine-rich domain, and an ADAMTS spacer, but lack a catalytic domain. We identified two new members of ADAMTSL proteins, ADAMTSL-6α and -6β, that differ in their N-terminal amino acid sequences but have common C-terminal regions. When transfected into MG63 osteosarcoma cells, both isoforms were secreted and deposited into pericellular matrices, although ADAMTSL-6α, in contrast to -6β, was barely detectable in the conditioned medium. Immunolabeling at the light and electron microscopic levels showed their close association with fibrillin-1-rich microfibrils in elastic connective tissues. Surface plasmon resonance analyses demonstrated that ADAMTSL-6β binds to the N-terminal half of fibrillin-1 with a dissociation constant of ∼80 nm. When MG63 cells were transfected or exogenously supplemented with ADAMTSL-6, fibrillin-1 matrix assembly was promoted in the early but not the late stage of the assembly process. Furthermore, ADAMTSL-6 transgenic mice exhibited excessive fibrillin-1 fibril formation in tissues where ADAMTSL-6 was overexpressed. All together, these results indicated that ADAMTSL-6 is a novel microfibril-associated protein that binds directly to fibrillin-1 and promotes fibrillin-1 matrix assembly.
出版者	American Society for Biochemistry and Molecular Biology
収録物名	Journal of Biological Chemistry
巻(号)	285(7)
ページ	4870-4882
刊行年月	2010-02
言語	英語
ハンドルURL	https://hdl.handle.net/11094/71423
eISSN	1083351X
NCID	AA1202441X
関連情報 (isIdenticalTo)	DOI (出版社版) https://doi.org/10.1074/jbc.M109.076919
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. 2010, 285(7), p. 4870-4882
DC.title	ADAMTSL-6 Is a Novel Extracellular Matrix Protein That Binds to Fibrillin-1 and Promotes Fibrillin-1 Fibril Formation
DC.creator	Tsutsui, Ko
	Manabe, Ri-ichiroh
	Yamada, Tomiko
	Nakano, Itsuko
	Oguri, Yasuko
	Keene, Douglas R.
	Sengle, Gerhard
	Sakai, Lynn Y.
	Sekiguchi, Kiyotoshi
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	2010-02
DC.identifier	https://doi.org/10.1074/jbc.M109.076919
DC.description	This research was originally published in the Journal of Biological Chemistry. Ko Tsutsui, Ri-ichiroh Manabe, Tomiko Yamada, Itsuko Nakano, Yasuko Oguri, Douglas R. Keene, Gerhard Sengle, Lynn Y. Sakai and Kiyotoshi Sekiguchi. ADAMTSL-6 Is a Novel Extracellular Matrix Protein That Binds to Fibrillin-1 and Promotes Fibrillin-1 Fibril Formation. J. Biol. Chem. 2010; 285: 4870-4882 © the American Society for Biochemistry and Molecular Biology
DCTERMS.abstract	ADAMTS (A disintegrin and metalloproteinase with thrombospondin motifs)-like (ADAMTSL) proteins, a subgroup of the ADAMTS superfamily, share several domains with ADAMTS proteinases, including thrombospondin type I repeats, a cysteine-rich domain, and an ADAMTS spacer, but lack a catalytic domain. We identified two new members of ADAMTSL proteins, ADAMTSL-6α and -6β, that differ in their N-terminal amino acid sequences but have common C-terminal regions. When transfected into MG63 osteosarcoma cells, both isoforms were secreted and deposited into pericellular matrices, although ADAMTSL-6α, in contrast to -6β, was barely detectable in the conditioned medium. Immunolabeling at the light and electron microscopic levels showed their close association with fibrillin-1-rich microfibrils in elastic connective tissues. Surface plasmon resonance analyses demonstrated that ADAMTSL-6β binds to the N-terminal half of fibrillin-1 with a dissociation constant of ∼80 nm. When MG63 cells were transfected or exogenously supplemented with ADAMTSL-6, fibrillin-1 matrix assembly was promoted in the early but not the late stage of the assembly process. Furthermore, ADAMTSL-6 transgenic mice exhibited excessive fibrillin-1 fibril formation in tissues where ADAMTSL-6 was overexpressed. All together, these results indicated that ADAMTSL-6 is a novel microfibril-associated protein that binds directly to fibrillin-1 and promotes fibrillin-1 matrix assembly.
DC.format	71423
citation_title	ADAMTSL-6 Is a Novel Extracellular Matrix Protein That Binds to Fibrillin-1 and Promotes Fibrillin-1 Fibril Formation
citation_author	Tsutsui, Ko
	Manabe, Ri-ichiroh
	Yamada, Tomiko
	Nakano, Itsuko
	Oguri, Yasuko
	Keene, Douglas R.
	Sengle, Gerhard
	Sakai, Lynn Y.
	Sekiguchi, Kiyotoshi
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	英語
citation_date	2010-02
citation_journal_title	Journal of Biological Chemistry
citation_volume	285
citation_issue	7
citation_firstpage	4870
citation_lastpage	4882
citation_doi	https://doi.org/10.1074/jbc.M109.076919
citation_public_url	https://hdl.handle.net/11094/71423

ADAMTSL-6 Is a Novel Extracellular Matrix Protein That Binds to Fibrillin-1 and Promotes Fibrillin-1 Fibril Formation

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