Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

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.

Type

Journal article

Journal

FEBS Lett

Publication Date

01/09/2000

Volume

480

Pages

142 - 146

Keywords

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