Endometase in Androgen-Repressed Human Prostate Cancer
Annual rept. 25 Feb 2002-25 Feb 2003
FLORIDA STATE UNIV TALLAHASSEE
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The spread of prostate cancer cells to other parts of the body is the leading cause of patient death. In 2000, we reported the discovery, cloning, and characterization of human matrix metalloproteinase-26 MMP-26, endometase. We have been testing three specific hypotheses 1 The expression levels of MMP-26 is correlated with the metastatic potentials and the degrees of malignancy of human prostate cells 2MMP-26 has unique structure and enzymatic function 3 MMP-26 enhances prostate cancer invasion by digesting extracellular matrix proteins and inactivating serine proteinase inhibitors, and specific inhibitors of MMP-26 block prostate cancer invasion. We have 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. MMP-26 promoted prostate cancer invasion via activation of pro-gelatinase BMMP-9. The endometase active site structure and function have been investigated using synthetic metalloproteinase inhibitors. These results suggest that endometases may be a novel marker for prostate cancer diagnosis and prognosis and a new target for prostate cancer therapy. More detailed results and summary are described in attached two J. Biol. Chem. papers published and in press from Dr. Sangs laboratory.
- Anatomy and Physiology
- Medicine and Medical Research