Cloning of MMP-26 - A novel matrilysin-like proteinase

A cDNA encoding a novel human matrix metalloproteinase (MMP), named MMP-26, was cloned from fetal cDNA. The deduced 261-amino-acid sequence is homolog ous to macrophage metalloelastase (51.8% identity). It includes only the mi nimal characteristic features of the MMP family: a signal peptide, a prodom ain and a catalytic domain. As with MMP-7, this new MMP does not comprise t he hemopexin domain, which is believed to be involved in substrate recognit ion. A study of MMP-26 mRNA steady states levels reveals, among the tissue examined, a specific expression in placenta. MMP-26 mRNA could also be dete cted in several human cell lines such as HEK 293 kidney cells and HFB1 lymp homa cells. Recombinant MMP-26 was produced in mammalian cells and used to demonstrate a proteolytic activity of the enzyme on gelatin and beta-casein .