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J Biol Chem, Vol. 275, Issue 2, 1384-1390, January 14, 2000

Post-translational Proteolytic Processing of Procollagen C-terminal Proteinase Enhancer Releases a Metalloproteinase Inhibitor*

Joni D. MottDagger §, Christina L. Thomas, Morgan T. RosenbachDagger , Kazuhiko Takahara, Daniel S. Greenspan, and Michael J. BandaDagger par

From the Dagger  Department of Radiology, University of California, San Francisco, California 94143-0750 and  Departments of Pathology and Laboratory Medicine and Biomolecular Chemistry, University of Wisconsin, Madison, Wisconsin 53706

Activity of matrix metalloproteinases (MMP) is regulated by a family of proteins called tissue inhibitors of metalloproteinases (TIMP). Four TIMPs have been cloned, and their molecular weights range from 29,000 to 20,000. By reverse zymography, we have observed a metalloproteinase inhibitor with an apparent molecular weight of 16,500 from medium conditioned by human brain tumor cells. Antibodies directed against TIMPs failed to react with the 16,500 molecular weight inhibitor, indicating that it was not a truncated form of a known TIMP. The inhibitor was isolated from conditioned medium using affinity and ion exchange chromatography. N-terminal sequences of the inhibitor matched amino acid sequences within the C-terminal domain of a protein known as procollagen C-terminal proteinase enhancer (PCPE). Thus, the inhibitor was named CT-PCPE. Comparison of the N-terminal domain of TIMP with CT-PCPE revealed that both contained six cysteine residues. As in the case of TIMP, reduction and alkylation abolished the inhibitory activity of CT-PCPE. Purified CT-PCPE inhibited MMP-2 with an IC50 value much greater than that of TIMP-2. This implies that MMPs may not be the physiologic targets for CT-PCPE inhibition. However, these results suggest that CT-PCPE may constitute a new class of metalloproteinase inhibitor.

* This work was supported by funds from the University of California Academic Senate Cancer Research Coordinating Committee (to M. J. B.) and National Institutes of Health Grants T32-ES07106 (to J. D. M.) and AR43621 and GM46846 (to D. S. G.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence should be addressed. Present address: Mail Stop 74-157, Lawrence Berkeley National Laboratory, Berkeley, CA 94720. Tel.: 510-486-5641; Fax: 510-486-5043; E-mail: JDMott@lbl.gov.

par Present address: Life Sciences Div., Lawrence Berkeley National Laboratory, Berkeley, CA 94720.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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