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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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ADAM Proteins
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ADAMTS1 Protein
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Aggrecans
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Amino Acid Motifs
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Amino Acid Sequence
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Animals
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Cartilage / chemistry*
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Cattle
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Chondroitin Sulfates / metabolism
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Disintegrins / genetics
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Disintegrins / metabolism*
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Extracellular Matrix Proteins*
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Lectins, C-Type
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Metalloendopeptidases / genetics
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Metalloendopeptidases / metabolism*
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Mice
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Molecular Sequence Data
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Molecular Weight
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Mutation / genetics
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Peptide Fragments / chemistry
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Peptide Fragments / genetics
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Peptide Fragments / metabolism
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Proteoglycans / chemistry
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Proteoglycans / genetics
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Proteoglycans / metabolism*
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Sequence Analysis, Protein
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Substrate Specificity
Substances
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Acan protein, mouse
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Aggrecans
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Disintegrins
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Extracellular Matrix Proteins
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Lectins, C-Type
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Peptide Fragments
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Proteoglycans
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Recombinant Fusion Proteins
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Chondroitin Sulfates
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ADAM Proteins
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ADAMTS1 Protein
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Adamts1 protein, mouse
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Metalloendopeptidases