MMP17 peptide

We try to monitor gene expression of matrix MMPs in rat's liver tissue after ischemia and reperfusion (I/R) by gene chip. MMPs activities change in the serum before and after I/R were also monitored. I/R was induced by clamping the common hepatic artery and portal vein for 40 min. and reperfused for 90 min. Blood samples collected prior to I and after R were analyzed for AST, ALT, hydroxyl radical and tumor necrosis factor (TNFalpha). This protocol resulted in the highly expressed of MMP 13, MMP15 and MMP17 in gene chips. MMPs activities in serum were also significantly increased after I/R. Biochemical data of AST, ALT, Hydroxyl radical and TNFalpha were concomitantly increased. Ilomastat, an MMP inhibitor, attenuated I/R-induced liver injury. After administration of oxygen radical scavenger, N-acetylcysteine, MMP activities were suppressed. These results indicate that reperfusion of the rat's liver could induce increase of MMPs gene expressions and MMP activities in which oxygen radicals production release may be involved.

The process of cancer progression involves the action of multiple proteolytic systems, among which the family of matrix metalloproteinases (MMPs) play a pivotal role. The MMPs evolved to accomplish their proteolytic tasks in multiple cellular and tissue microenvironments including lipid rafts by incorporation and deletions of specific structural domains. The membrane type-MMPs (MT-MMPs) incorporated membrane anchoring domains that display these proteases at the cell surface, and thus they are optimal pericellular proteolytic machines. Two members of the MT-MMP subfamily, MMP-17 (MT4-MMP) and MMP-25 (MT6-MMP), are anchored to the plasma membrane via a glycosyl-phosphatidyl inositol (GPI) anchor, which confers these enzymes a unique set of regulatory and functional mechanisms that separates them from the rest of the MMP family. Discovered almost a decade ago, the body of work on GPI-MT-MMPs today is still surprisingly limited when compared to other MT-MMPs. However, new evidence shows that the GPI-MT-MMPs are highly expressed in human cancer, where they are associated with progression. Accumulating biochemical and functional evidence also highlights their distinct properties. In this review, we summarize the structural, biochemical, and biological properties of GPI-MT-MMPs and present an overview of their expression and role in cancer. We further discuss the potential implications of GPI-anchoring for enzyme function. Finally, we comment on the new scientific challenges that lie ahead to better understand the function and role in cancer of these intriguing but yet unique MMPs.