Encyclopedia of Cancer

Living Edition
| Editors: Manfred Schwab

Matrix Metalloproteinases

  • M. Sharon Stack
Living reference work entry
DOI: https://doi.org/10.1007/978-3-642-27841-9_3561-2

Synonyms

Definition

The matrix metalloproteinases (MMPs), or matrixins, are a family of zinc-dependent metalloendopeptidases that are widely expressed. They cleave a variety of extracellular substrates including, but not limited to, protein and proteoglycan components of the extracellular matrix (ECM). MMPs belong to the metzincin family of endopeptidases, characterized by the presence of three zinc-binding histidine residues within the active site (HexxHxxGxxH). MMPs are believed to catalyze localized hydrolysis of extracellular matrix proteins including collagens, fibronectin, laminins, and proteoglycans, thereby modifying the integrity of the connective tissue.

Characteristics

Domain Structure

MMPs are synthesized as prepro-enzymes and, following removal of the signal peptide, are generally secreted in proenzyme or zymogen form. The latency of the zymogen is maintained by the presence of an unpaired cysteine residue in the propeptide domain (Fig. 1), contained...

Keywords

Zymogen Activation Pericellular Proteolysis Tumor Cell Conditioned Medium Pace Family Essential Zinc 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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References

  1. Benbow U, Brinckerhoff CE (1997) The AP-1 site and MMP gene regulation: what is all the fuss about? Matrix Biol 15:519–526CrossRefPubMedGoogle Scholar
  2. Birkedal-Hansen H (1995) Proteolytic remodeling of extracellular matrix. Curr Opin Cell Biol 7:728–735CrossRefPubMedGoogle Scholar
  3. Ellerbroek SM, Stack MS (1999) Membrane associated matrix metalloproteinases in metastasis. Bioessays 21:940–949CrossRefPubMedGoogle Scholar
  4. Holmbeck K, Bianco P, Caterina J et al (1999) MT1-MMP-deficient mice develop dwarfism, osteopenia, arthritis, and connective tissue disease due to inadequate collagen turnover. Cell 99:81–92CrossRefPubMedGoogle Scholar
  5. Nagase H, Woessner JF (1999) Matrix metalloproteinases. J Biol Chem 274:21491–21494CrossRefPubMedGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2015

Authors and Affiliations

  1. 1.Northwestern University Medical SchoolChicagoUSA