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ADAMTS-1 is an active metalloproteinase associated with the extracellular matrix.

Cellular disintegrin and metalloproteinases (ADAMs) are a family of genes with a sequence similar to the snake venom metalloproteinases and disintegrins. ADAMTS-1 is a unique ADAM family protein with respect to the presence of thrombospondin type I motifs and the capacity to bind to the extracellular matrix. Because ADAMTS-1 has a potential zinc-binding motif in the metalloproteinase domain, we examined in this study whether ADAMTS-1 is an active metalloproteinase by means of the proteinase trapping mechanism of alpha2-macroglobulin. We found that the soluble type of ADAMTS-1 protein is able to form a covalent-binding complex with alpha2-macroglobulin. Furthermore, the point mutation within the zinc-binding motif of ADAMTS-1 protein eliminates its capacity to bind to alpha2-macroglobulin. These data demonstrate that the metalloproteinase domain of ADAMTS-1 is catalytically active. In addition, we showed that the removal of the pro-domain from the ADAMTS-1 precursor is impaired in the furin-deficient cell line, LoVo, and that the processing ability of the cells is restored by the co-expression of the furin cDNA. These data provide evidence that the ADAMTS-1 precursor is processed in vivo by furin endopeptidase in the secretory pathway. Consequently, ADAMTS-1 is an active metalloprotease that is associated with the extracellular matrix. This study strongly suggests that ADAMTS-1 may play a role in the inflammatory process through its protease activity.

Pubmed ID: 10373500


  • Kuno K
  • Terashima Y
  • Matsushima K


The Journal of biological chemistry

Publication Data

June 25, 1999

Associated Grants


Mesh Terms

  • ADAM Proteins
  • Amino Acid Sequence
  • Animals
  • COS Cells
  • Disintegrins
  • Extracellular Matrix
  • Glycosylation
  • Metalloendopeptidases
  • Molecular Sequence Data
  • Molecular Weight
  • Protein Binding
  • Solubility
  • Zinc
  • alpha-Macroglobulins