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.
Original language | English |
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Pages (from-to) | 241-245 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 478 |
Issue number | 3 |
DOIs | |
Publication status | Published - 2000 Aug 4 |
Keywords
- Aggrecan
- Cartilage degradation
- Disintegrin and metalloproteinase thrombospondin
- Extracellular matrix
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology