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ADAMTS‐1 cleaves a cartilage proteoglycan, aggrecan
Author(s) -
Kuno Kouji,
Okada Yasunori,
Kawashima Hiroto,
Nakamura Hiroyuki,
Miyasaka Masayuki,
Ohno Hiroshi,
Matsushima Kouji
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01854-8
Subject(s) - aggrecan , adamts , proteoglycan , cartilage , chemistry , microbiology and biotechnology , articular cartilage , anatomy , biochemistry , metalloproteinase , biology , matrix metalloproteinase , medicine , osteoarthritis , pathology , thrombospondin , alternative medicine
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 Glu 1871 –Leu 1872 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.