- Abstract:
-
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 lab...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1016/s0014-5793(00)01919-0
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- Journal:
- FEBS letters
- Volume:
- 480
- Issue:
- 2-3
- Pages:
- 142-146
- Publication date:
- 2000-09-05
- DOI:
- EISSN:
-
1873-3468
- ISSN:
-
0014-5793
- URN:
-
uuid:29159d7d-df89-45ea-837e-2fda78257c21
- Source identifiers:
-
224284
- Local pid:
- pubs:224284
- Language:
- English
- Keywords:
- Copyright date:
- 2000
Journal article
Membrane-type 6 matrix metalloproteinase (MT6-MMP, MMP-25) is the second glycosyl-phosphatidyl inositol (GPI)-anchored MMP.
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