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Membrane type (MT) matrix metalloproteinases (MMPs) are recently recognized members of the family of Zn(2+)- and Ca(2+)-dependent MMPs. MMP-17 is, therefore, a competent Zn(2+)-dependent MMP with unique specificity among synthetic substrates and the capability to both degrade gelatin and activate progelatinase A (1). (MMP-17) is expressed mainly in the brain, leukocytes, the colon, the ovary, and the testis. The expression of MMP-17 in leukocytes together with its putative membrane localization suggest that this enzyme could be involved in the activation of membrane-bound precursors of growth factors or inflammatory mediators such as tumor necrosis factor-alpha (2). glycosylphospha-tidylinositol (GPI) anchoring of MT4-MMP on the cell surface indicates a unique biological function and character for this proteinase (3).