Cloning of MMP-26. A novel matrilysin-like proteinase

Eur J Biochem. 2000 Jun;267(11):3323-9. doi: 10.1046/j.1432-1327.2000.01363.x.


A cDNA encoding a novel human matrix metalloproteinase (MMP), named MMP-26, was cloned from fetal cDNA. The deduced 261-amino-acid sequence is homologous to macrophage metalloelastase (51.8% identity). It includes only the minimal characteristic features of the MMP family: a signal peptide, a prodomain and a catalytic domain. As with MMP-7, this new MMP does not comprise the hemopexin domain, which is believed to be involved in substrate recognition. A study of MMP-26 mRNA steady states levels reveals, among the tissue examined, a specific expression in placenta. MMP-26 mRNA could also be detected in several human cell lines such as HEK 293 kidney cells and HFB1 lymphoma cells. Recombinant MMP-26 was produced in mammalian cells and used to demonstrate a proteolytic activity of the enzyme on gelatin and beta-casein.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • COS Cells
  • Catalytic Domain
  • Cell Line
  • Chlorocebus aethiops
  • DNA, Complementary / genetics
  • Expressed Sequence Tags
  • Gene Expression Profiling
  • Humans
  • Matrix Metalloproteinases / genetics*
  • Matrix Metalloproteinases / metabolism
  • Matrix Metalloproteinases, Secreted
  • Molecular Sequence Data
  • Organ Specificity
  • Placenta / enzymology*
  • Pregnancy Proteins / genetics*
  • Protein Sorting Signals / genetics
  • Protein Structure, Tertiary
  • RNA, Messenger / metabolism
  • Recombinant Fusion Proteins / metabolism
  • Sequence Homology, Amino Acid
  • Substrate Specificity
  • Transfection


  • DNA, Complementary
  • Pregnancy Proteins
  • Protein Sorting Signals
  • RNA, Messenger
  • Recombinant Fusion Proteins
  • MMP26 protein, human
  • Matrix Metalloproteinases
  • Matrix Metalloproteinases, Secreted

Associated data

  • GENBANK/AF230354