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Originally published In Press as doi:10.1074/jbc.M210975200 on February 13, 2003

J. Biol. Chem., Vol. 278, Issue 17, 15056-15064, April 25, 2003
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Activation of Pro-gelatinase B by Endometase/Matrilysin-2 Promotes Invasion of Human Prostate Cancer Cells*

Yun-Ge ZhaoDagger , Ai-Zhen XiaoDagger , Robert G. NewcomerDagger , Hyun I. ParkDagger , Tiebang KangDagger , Leland W. K. Chung§, Mark G. Swanson, Haiyen E. Zhau§, John Kurhanewicz, and Qing-Xiang Amy SangDagger ||

From the Dagger  Department of Chemistry and Biochemistry and Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida 32306-4390, the § Molecular Urology and Therapeutics Program, Emory University Winship Cancer Institute, Atlanta, Georgia 30322, and the  Magnetic Resonance Science Center, University of California, San Francisco, California 94143-1290

This work has explored a putative biochemical mechanism by which endometase/matrilysin-2/matrix metalloproteinase-26 (MMP-26) may promote human prostate cancer cell invasion. Here, we showed that the levels of MMP-26 protein in human prostate carcinomas from multiple patients were significantly higher than those in prostatitis, benign prostate hyperplasia, and normal prostate glandular tissues. The role of MMP-26 in prostate cancer progression is unknown. MMP-26 was capable of activating pro-MMP-9 by cleavage at the Ala93-Met94 site of the prepro-enzyme. This activation proceeded in a time- and dose-dependent manner, facilitating the efficient cleavage of fibronectin by MMP-9. The activated MMP-9 products generated by MMP-26 appeared more stable than those cleaved by MMP-7 under the conditions tested. To investigate the contribution of MMP-26 to cancer cell invasion via the activation of MMP-9, highly invasive and metastatic human prostate carcinoma cells, androgen-repressed prostate cancer (ARCaP) cells were selected as a working model. ARCaP cells express both MMP-26 and MMP-9. Specific anti-MMP-26 and anti-MMP-9 functional blocking antibodies both reduced the invasiveness of ARCaP cells across fibronectin or type IV collagen. Furthermore, the introduction of MMP-26 antisense cDNA into ARCaP cells significantly reduced the MMP-26 protein level in these cells and strongly suppressed the invasiveness of ARCaP cells. Double immunofluorescence staining and confocal laser scanning microscopic images revealed that MMP-26 and MMP-9 were co-localized in parental and MMP-26 sense-transfected ARCaP cells. Moreover, MMP-26 and MMP-9 proteins were both expressed in the same human prostate carcinoma tissue samples examined. These results indicate that MMP-26 may be a physiological and pathological activator of pro-MMP-9.

* This work was supported in part by Department of Defense/United States Army Prostate Cancer Research Program Grant DAMD17-02-1-0238, National Institutes of Health Grant CA78646, American Cancer Society, Florida Division, Grant F01FSU-1, the Florida State University Research Foundation (to Q.-X. A. S.), and National Institutes of Health Grants CA82739 and CA76620 (to H. E. Z. and L. W. K. C., respectively).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: Dept. of Chemistry and Biochemistry, Florida State University, 203 DLC, Chemistry Research Bldg., Rm. 203, Tallahassee, FL 32306-4390. Tel.: 850-644-8683; Fax: 850-644-8281; E-mail: sang@chem.fsu.edu.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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