Membrane-type 6 matrix metalloproteinase (MT6-MMP, MMP-25) is the second glycosyl-phosphatidyl inositol (GPI)-anchored MMP

FEBS Lett. 2000 Sep 1;480(2-3):142-6. doi: 10.1016/s0014-5793(00)01919-0.


A recently identified membrane-type 6 matrix metalloproteinase (MT6-MMP) has a hydrophobic stretch of 24 amino acids at the C-terminus. This hydrophobicity pattern is similar to glycosyl-phosphatidyl inositol (GPI)-anchored MMP, MT4-MMP, and other GPI-anchored proteins. Thus, we tested the possibility that MT6-MMP was also a GPI-anchored proteinase. Our results showed that MT6-MMP as well as MT4-MMP were labeled with [3H]ethanolamine indicating the presence of a GPI unit with incorporated label. In addition, phosphatidyl inositol-specific phospholipase C treatment released MT6-MMP from the surface of transfected cells. These results strongly indicate that MT6-MMP is a GPI-anchored protein. Since two members of MT-MMPs are now assigned as GPI-anchored proteinase, MT-MMPs can be subgrouped into GPI type and transmembrane type.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • CHO Cells
  • COS Cells
  • Cricetinae
  • Enzyme Activation
  • Enzyme Precursors / metabolism
  • GPI-Linked Proteins
  • Glycosylphosphatidylinositols / metabolism*
  • Humans
  • Matrix Metalloproteinase 2 / metabolism
  • Matrix Metalloproteinases / metabolism*
  • Matrix Metalloproteinases, Membrane-Associated
  • Mice
  • Molecular Sequence Data


  • Enzyme Precursors
  • GPI-Linked Proteins
  • Glycosylphosphatidylinositols
  • Matrix Metalloproteinases
  • Matrix Metalloproteinases, Membrane-Associated
  • matrix metalloproteinase 25
  • Matrix Metalloproteinase 2