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HandWiki. Matrix Metallopeptidase. Encyclopedia. Available online: https://encyclopedia.pub/entry/36087 (accessed on 26 September 2026).
HandWiki. Matrix Metallopeptidase. Encyclopedia. Available at: https://encyclopedia.pub/entry/36087. Accessed September 26, 2026.
HandWiki. "Matrix Metallopeptidase" Encyclopedia, https://encyclopedia.pub/entry/36087 (accessed September 26, 2026).
HandWiki. (2022, November 23). Matrix Metallopeptidase. In Encyclopedia. https://encyclopedia.pub/entry/36087
HandWiki. "Matrix Metallopeptidase." Encyclopedia. Web. 23 November, 2022.
Matrix Metallopeptidase
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The content is sourced from: https://handwiki.org/wiki/Biology:Matrix_metallopeptidase

Matrix metallopeptidases (MMPs), also known as matrix metalloproteinases or matrixins, are metalloproteinases that are calcium-dependent zinc-containing endopeptidases; other family members are adamalysins, serralysins, and astacins. The MMPs belong to a larger family of proteases known as the metzincin superfamily. 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. 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 (1962), 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. Recently matrix metalloproteinases have been proposed as markers of many pathological conditions for their ability to degrade extracellular matrix components and remodel tissues. Herein, MMPs have been reported as one of the main factors of cancer progression and metastasis formation. This led to the emerging research field in biosensors development for the detection of such enzymes.

metallopeptidases metalloproteinases extracellular matrix

References

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  2. "Human skin collagenase. Isolation and mechanism of attack on the collagen molecule". Biochim Biophys Acta 151 (3): 637–45. 1968. doi:10.1016/0005-2744(68)90010-7. PMID 4967132.  https://dx.doi.org/10.1016%2F0005-2744%2868%2990010-7
  3. "The zymogen of tadpole collagenase". Biochemistry 10 (16): 3035–41. 1971. doi:10.1021/bi00792a008. PMID 4331330.  https://dx.doi.org/10.1021%2Fbi00792a008
  4. "The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family". Proc Natl Acad Sci USA 87 (14): 5578–82. 1990. doi:10.1073/pnas.87.14.5578. PMID 2164689.  http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=54368
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  10. "Modeling of enzyme-substrate complexes for the metalloproteases MMP-3, ADAM-9 and ADAM-10". J. Comput.-Aided Mol. Des. 17 (9): 551–65. 2003. doi:10.1023/B:JCAM.0000005765.13637.38. PMID 14713188.  https://dx.doi.org/10.1023%2FB%3AJCAM.0000005765.13637.38
  11. "Epilysin, a novel human matrix metalloproteinase (MMP-28) expressed in testis and keratinocytes and in response to injury". J Biol Chem 276 (13): 10134–10144. 2001. doi:10.1074/jbc.M001599200. PMID 11121398.  https://dx.doi.org/10.1074%2Fjbc.M001599200
  12. Snoek-van Beurden PAM; Von den Hoff JW (2005). "Zymographic techniques for the analysis of matrix metalloproteinases and their inhibitors". BioTechniques 38 (1): 73–83. doi:10.2144/05381RV01. PMID 15679089.  https://dx.doi.org/10.2144%2F05381RV01
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