ADAMTS-1 cleaves a cartilage proteoglycan, aggrecan

Kouji Kuno; Yasunori Okada; Hiroto Kawashima; Hiroyuki Nakamura; Masayuki Miyasaka; Hiroshi Ohno; Kouji Matsushima

doi:10.1016/S0014-5793(00)01854-8

ADAMTS-1 cleaves a cartilage proteoglycan, aggrecan

Kouji Kuno, Yasunori Okada, Hiroto Kawashima, Hiroyuki Nakamura, Masayuki Miyasaka, Hiroshi Ohno, Kouji Matsushima

病理学

研究成果: Article › 査読

218 被引用数 (Scopus)

抄録

A disintegrin-like and metalloproteinase with thrombospondin type I motifs-1 (ADAMTS-1) is an extracellular matrix-anchored metalloproteinase. In this study we have demonstrated that ADAMTS-1 is able to cleave a major cartilage proteoglycan, aggrecan. N-terminal sequencing analysis of the cleavage product revealed that ADAMTS-1 cleaves the Glu¹⁸⁷¹-Leu¹⁸⁷² bond within the chondroitin sulfate attachment domain of aggrecan. In addition, deletional analysis demonstrated that the C-terminal spacer region of ADAMTS-1 is necessary to degrade aggrecan. These results suggest that ADAMTS-1 may be involved in the turnover of aggrecan in vivo. (C) 2000 Federation of European Biochemical Societies.

本文言語	English
ページ（範囲）	241-245
ページ数	5
ジャーナル	FEBS Letters
巻	478
号	3
DOI	https://doi.org/10.1016/S0014-5793(00)01854-8
出版ステータス	Published - 2000 8 4

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

文献へのアクセス

10.1016/S0014-5793(00)01854-8

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引用スタイル

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title = "ADAMTS-1 cleaves a cartilage proteoglycan, aggrecan",

abstract = "A disintegrin-like and metalloproteinase with thrombospondin type I motifs-1 (ADAMTS-1) is an extracellular matrix-anchored metalloproteinase. In this study we have demonstrated that ADAMTS-1 is able to cleave a major cartilage proteoglycan, aggrecan. N-terminal sequencing analysis of the cleavage product revealed that ADAMTS-1 cleaves the Glu1871-Leu1872 bond within the chondroitin sulfate attachment domain of aggrecan. In addition, deletional analysis demonstrated that the C-terminal spacer region of ADAMTS-1 is necessary to degrade aggrecan. These results suggest that ADAMTS-1 may be involved in the turnover of aggrecan in vivo. (C) 2000 Federation of European Biochemical Societies.",

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T1 - ADAMTS-1 cleaves a cartilage proteoglycan, aggrecan

AU - Kuno, Kouji

AU - Okada, Yasunori

AU - Kawashima, Hiroto

AU - Nakamura, Hiroyuki

AU - Miyasaka, Masayuki

AU - Ohno, Hiroshi

AU - Matsushima, Kouji

PY - 2000/8/4

Y1 - 2000/8/4

N2 - A disintegrin-like and metalloproteinase with thrombospondin type I motifs-1 (ADAMTS-1) is an extracellular matrix-anchored metalloproteinase. In this study we have demonstrated that ADAMTS-1 is able to cleave a major cartilage proteoglycan, aggrecan. N-terminal sequencing analysis of the cleavage product revealed that ADAMTS-1 cleaves the Glu1871-Leu1872 bond within the chondroitin sulfate attachment domain of aggrecan. In addition, deletional analysis demonstrated that the C-terminal spacer region of ADAMTS-1 is necessary to degrade aggrecan. These results suggest that ADAMTS-1 may be involved in the turnover of aggrecan in vivo. (C) 2000 Federation of European Biochemical Societies.

AB - A disintegrin-like and metalloproteinase with thrombospondin type I motifs-1 (ADAMTS-1) is an extracellular matrix-anchored metalloproteinase. In this study we have demonstrated that ADAMTS-1 is able to cleave a major cartilage proteoglycan, aggrecan. N-terminal sequencing analysis of the cleavage product revealed that ADAMTS-1 cleaves the Glu1871-Leu1872 bond within the chondroitin sulfate attachment domain of aggrecan. In addition, deletional analysis demonstrated that the C-terminal spacer region of ADAMTS-1 is necessary to degrade aggrecan. These results suggest that ADAMTS-1 may be involved in the turnover of aggrecan in vivo. (C) 2000 Federation of European Biochemical Societies.

KW - Aggrecan

KW - Cartilage degradation

KW - Disintegrin and metalloproteinase thrombospondin

KW - Extracellular matrix

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