MMP11

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
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View/Edit Human

Stromelysin-3 (SL-3) also known as matrix metalloproteinase-11 (MMP-11) is an enzyme that in humans is encoded by the MMP11 gene.[1][2][3][4]

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. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the enzyme encoded by this gene is activated intracellularly by furin within the constitutive secretory pathway. Also in contrast to other MMP's, this enzyme cleaves alpha 1-proteinase inhibitor but weakly degrades structural proteins of the extracellular matrix.[4]

References

  1. Levy A, Zucman J, Delattre O, Mattei MG, Rio MC, Basset P (Aug 1992). "Assignment of the human stromelysin 3 (STMY3) gene to the q11.2 region of chromosome 22". Genomics. 13 (3): 881–3. doi:10.1016/0888-7543(92)90175-R. PMID 1639418.
  2. Anglard P, Melot T, Guerin E, Thomas G, Basset P (Oct 1995). "Structure and promoter characterization of the human stromelysin-3 gene". J Biol Chem. 270 (35): 20337–44. doi:10.1074/jbc.270.35.20337. PMID 7657606.
  3. Luo D, Mari B, Stoll I, Anglard P (Jul 2002). "Alternative splicing and promoter usage generates an intracellular stromelysin 3 isoform directly translated as an active matrix metalloproteinase". J Biol Chem. 277 (28): 25527–36. doi:10.1074/jbc.M202494200. PMID 12006591.
  4. 4.0 4.1 "Entrez Gene: MMP11 matrix metallopeptidase 11 (stromelysin 3)".

Further reading