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Biochem Biophys Res Commun. 2000 Nov 30;278(3):511-5.

ADAM 12-S cleaves IGFBP-3 and IGFBP-5 and is inhibited by TIMP-3.

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  • 1Institute of Molecular Pathology, University of Copenhagen, Frederik V's Vej 11, Copenhagen, DK-2100, Denmark.

Erratum in

  • Biochem Biophys Res Commun 2001 Jan 12;280(1):421.

Abstract

ADAMs are a family of multidomain proteins having proteolytic and cell adhesion activities. We have previously shown that ADAM 12-S, the secreted soluble form of human ADAM 12, is a catalytically active protease. We now describe the purification of full-length recombinant ADAM 12-S and demonstrate that it cleaves insulin-like growth factor binding protein-3 (IGFBP-3). This result supports a role for ADAM 12-S in the degradation of IGFBP-3 in the blood of pregnant women. Furthermore, we tested for proteolysis of other members of the IGF binding protein family and found that ADAM 12-S cleaves IGFBP-5 in addition to IGFBP-3, but does not cleave IGFBP-1, -2, -4, or -6. ADAM 12-S may therefore be the IGFBP-5 protease that is secreted by osteoblasts and other cells. Cleavage of both IGFBP-3 and -5 by ADAM 12-S was inhibited by TIMP-3, raising the possibility that TIMP-3 is a physiological inhibitor of ADAM 12-S.

Copyright 2000 Academic Press.

PMID:
11095942
[PubMed - indexed for MEDLINE]
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