Matrix metallopeptidase 24 (MMP24)

Matrix metallopeptidase 24 (MMP24), also known as membrane-type 5 matrix metalloproteinase (MT5-MMP), is a type I transmembrane zinc-dependent endopeptidase that belongs to the matrix metalloproteinase (MMP) family. Distinct from many secreted MMPs, MMP24 is anchored to the cell membrane and is involved in the proteolytic breakdown of extracellular matrix components during normal physiological processes such as embryogenesis, tissue remodeling, and neuro-immune interactions, as well as in pathological states including cancer, inflammation, and neurovascular diseases. MMP24 specifically regulates cleavage of substrates such as N-cadherin (CDH2) and can activate pro-MMP2, suggesting roles in neural cell function, peripheral nociception, and maintenance of neural stem cell quiescence. It features the characteristic MMP catalytic, hemopexin-like, and transmembrane domains, and its dysregulation or overexpression is implicated in tissue-destructive pathologies. No selective inhibitors of MMP24 are currently in clinical use, and development of such drugs must address the risk of off-target effects common to general MMP inhibition.

Other names

Matrix metalloproteinase-24MT5-MMPMatrix metallopeptidase 24 (membrane-inserted)Matrix metalloproteinase 24 (membrane-inserted)Membrane-type 5 matrix metalloproteinaseMembrane-type matrix metalloproteinase 5MT-MMP 5MT-MMP5MT5MMPMTMMP5MMP25

Inhibition of zinc-dependent protease activity (for MMP inhibitors in general); Blockade of substrate cleavage and downstream extracellular matrix remodeling (as expected for MMP-targeted drugs)