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 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.
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