Matrix metalloproteinases (MMPs), also known as matrix metallopeptidases or matrixins, are metalloproteinases that are calcium-dependent zinc-containing endopeptidases;[1] other family members are adamalysins, serralysins, and astacins. The MMPs belong to a larger family of proteases known as the metzincin superfamily.[2]
Collectively, these enzymes are capable of degrading all kinds of extracellular matrix proteins, but also can process a number of bioactive molecules. They are known to be involved in the cleavage of cell surface receptors, the release of apoptotic ligands (such as the FAS ligand), and chemokine/cytokine inactivation.[3] MMPs are also thought to play a major role in cell behaviors such as cell proliferation, migration (adhesion/dispersion), differentiation, angiogenesis, apoptosis, and host defense.
They were first described in vertebrates in 1962,[4] including humans, but have since been found in invertebrates and plants. They are distinguished from other endopeptidases by their dependence on metal ions as cofactors, their ability to degrade extracellular matrix, and their specific evolutionary DNA sequence.
^Verma RP, Hansch C (March 2007). "Matrix metalloproteinases (MMPs): chemical-biological functions and (Q)SARs" (PDF). Bioorg. Med. Chem.15 (6): 2223–68. doi:10.1016/j.bmc.2007.01.011. PMID 17275314. Archived from the original (PDF) on 13 May 2015. Retrieved 21 October 2015.
^Matrix Metalloproteinases: Its implications in cardiovascular disorders
^Van Lint P, Libert C (December 2007). "Chemokine and cytokine processing by matrix metalloproteinases and its effect on leukocyte migration and inflammation". J. Leukoc. Biol.82 (6): 1375–81. doi:10.1189/jlb.0607338. PMID 17709402.
^Gross, J.; Lapiere, C. M. (June 1962). "Collagenolytic activity in amphibian tissues: a tissue culture assay". Proceedings of the National Academy of Sciences. 48 (6): 1014–22. Bibcode:1962PNAS...48.1014G. doi:10.1073/pnas.48.6.1014. PMC 220898. PMID 13902219.
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