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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.

Original publication




Journal article


Febs lett

Publication Date





142 - 146


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