MMP15

MMP15, or matrix metalloproteinase 15, is a member of the matrix metalloproteinase family and a membrane-type metalloproteinase. It is anchored to the cell surface as a single-pass transmembrane protein and functions as a zinc-dependent endopeptidase. The protein contains a signal peptide, a propeptide with the cysteine-switch motif, a catalytic domain, a hinge region, and a hemopexin-like domain, followed by a transmembrane segment and a short cytoplasmic tail. Activation involves proteolytic removal of the propeptide, releasing the active enzyme at the cell surface.

Functionally, MMP15 participates in pericellular proteolysis of extracellular matrix components such as collagens and gelatin, facilitating cell migration, invasion, and tissue remodeling. It can remodel the extracellular environment and may participate in the activation of other matrix metalloproteinases, contributing to processes such as angiogenesis and wound healing. Expression levels and activity are regulated by developmental cues, cytokines, growth factors, and interactions with tissue inhibitors of metalloproteinases (TIMPs), as well as by subcellular localization to the cell membrane.

Clinical and biological relevance is noted in various contexts. Aberrant MMP15 expression or activity has been described in several cancers and inflammatory conditions, where it can be associated with enhanced invasive potential or altered tissue remodeling. However, its precise roles are context-dependent and continue to be an area of investigation. In summary, MMP15 is a membrane-anchored protease that contributes to pericellular matrix remodeling and may influence pathological processes involving tissue invasion and remodeling.