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

Number of Access:1,013（2025-08-18 14:07 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/71423

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Title	ADAMTSL-6 Is a Novel Extracellular Matrix Protein That Binds to Fibrillin-1 and Promotes Fibrillin-1 Fibril Formation
Creator	CreatorName Tsutsui, Ko
	NRID 1000030280837 1000030280837 CreatorName Manabe, Ri-ichiroh
	CreatorName Yamada, Tomiko
	CreatorName Nakano, Itsuko
	CreatorName Oguri, Yasuko
	CreatorName Keene, Douglas R.
	CreatorName Sengle, Gerhard
	CreatorName Sakai, Lynn Y.
	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. 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
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.
Publisher	American Society for Biochemistry and Molecular Biology
Source Title	Journal of Biological Chemistry
Volume (Issue)	285(7)
Page	4870-4882
Date of Issued	2010-02
Language	English
Handle URL	https://hdl.handle.net/11094/71423
eISSN	1083351X
NCID	AA1202441X
Relation.isIdenticalTo	DOI (Publisher Version) https://doi.org/10.1074/jbc.M109.076919
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. 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	English
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	English
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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