Biology:MMP14

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Matrix metalloproteinase-14 is an enzyme that in humans is encoded by the MMP14 gene.[1]

Function

Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Deficits in MMP14 leads to premature aging, short lifespan, and cell senescence in mice,[2] suggesting an important role of MMP14 in extracellular matrix remodeling during aging. Most MMP's are secreted as inactive pro-proteins which are activated when cleaved by extracellular proteinases.

However, the protein encoded by this gene is a member of the membrane-type MMP (MT-MMP) subfamily; each member of this subfamily contains a potential transmembrane domain suggesting that these proteins are tethered to the cell surface rather than secreted.

"This protein activates MMP2 protein, and this activity may be involved in tumor invasion."[3]


Interactions

MMP14 has been shown to interact with TIMP2.[4]

See also

References

  1. "A matrix metalloproteinase expressed on the surface of invasive tumour cells". Nature 370 (6484): 61–5. Jul 1994. doi:10.1038/370061a0. PMID 8015608. Bibcode1994Natur.370...61S. 
  2. Gutiérrez‐Fernández, Ana; Soria‐Valles, Clara; Osorio, Fernando G.; Gutiérrez‐Abril, Jesús; Garabaya, Cecilia; Aguirre, Alina; Fueyo, Antonio; Fernández‐García, María Soledad et al. (2015-07-14). "Loss of MT1‐MMP causes cell senescence and nuclear defects which can be reversed by retinoic acid" (in en). The EMBO Journal 34 (14): 1875–1888. doi:10.15252/embj.201490594. ISSN 0261-4189. PMID 25991604. 
  3. "Entrez Gene: MMP14 matrix metallopeptidase 14 (membrane-inserted)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4323. 
  4. "Tissue inhibitor of metalloproteinase-2 (TIMP-2) binds to the catalytic domain of the cell surface receptor, membrane type 1-matrix metalloproteinase 1 (MT1-MMP)". J. Biol. Chem. 273 (2): 1216–22. Jan 1998. doi:10.1074/jbc.273.2.1216. PMID 9422789. 

Further reading

External links

  • The MEROPS online database for peptidases and their inhibitors: M10.014