PMID- 10567400
OWN - NLM
STAT- MEDLINE
DCOM- 19991229
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 48
DP  - 1999 Nov 26
TI  - Membrane type 4 matrix metalloproteinase (MT4-MMP, MMP-17) is a
      glycosylphosphatidylinositol-anchored proteinase.
PG  - 34260-6
AB  - Among the five membrane-type matrix metalloproteinases (MT-MMPs), MT1-, MT2-,
      MT3-, and MT5-MMPs have about a 20-amino acid cytoplasmic tail following the
      transmembrane domain. In contrast, a putative transmembrane domain of MT4-MMP
      locates at the very C-terminal end, and the expected cytoplasmic tail is very
      short or nonexistent. Such sequences often act as a glycosylphosphatidylinositol 
      (GPI) anchoring signal rather than as a transmembrane domain. We thus examined
      the possibility that MT4-MMP is a GPI-anchored proteinase. Our results showed
      that [(3)H]ethanolamine, which can be incorporated into the GPI unit,
      specifically labeled the MT4-MMP C-terminal end in a sequence-dependent manner.
      In addition, phosphatidylinositol-specific phospholipase C treatment released the
      MT4-MMP from the surface of transfected cells. These results indicate that
      MT4-MMP is the first GPI-anchored proteinase in the MMP family. During
      cultivation of the transfected cells, MT4-MMP appeared to be shed from the cell
      surface by the action of an endogenous metalloproteinase. GPI anchoring of
      MT4-MMP on the cell surface indicates a unique biological function and character 
      for this proteinase.
FAU - Itoh, Y
AU  - Itoh Y
AD  - Department of Cancer Cell Research, Institute of Medical Science, University of
      Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.
FAU - Kajita, M
AU  - Kajita M
FAU - Kinoh, H
AU  - Kinoh H
FAU - Mori, H
AU  - Mori H
FAU - Okada, A
AU  - Okada A
FAU - Seiki, M
AU  - Seiki M
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Glycosylphosphatidylinositols)
RN  - 0 (Protease Inhibitors)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Thiophenes)
RN  - 10028-17-8 (Tritium)
RN  - 47E5O17Y3R (Phenylalanine)
RN  - 5KV86114PT (Ethanolamine)
RN  - BK349F52C9 (batimastat)
RN  - EC 3.1.4.- (Type C Phospholipases)
RN  - EC 3.1.4.11 (Phosphoinositide Phospholipase C)
RN  - EC 3.4.- (Endopeptidases)
RN  - EC 3.4.24.- (MMP17 protein, human)
RN  - EC 3.4.24.- (Matrix Metalloproteinases)
RN  - EC 3.4.24.- (Matrix Metalloproteinases, Membrane-Associated)
RN  - EC 3.4.24.- (Metalloendopeptidases)
RN  - EC 3.4.24.- (Mmp17 protein, mouse)
RN  - EC 4.6.1.13 (Phosphatidylinositol Diacylglycerol-Lyase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites
MH  - CHO Cells
MH  - COS Cells
MH  - Cricetinae
MH  - Endopeptidases/drug effects/metabolism
MH  - Ethanolamine/metabolism
MH  - Fluorescent Antibody Technique, Indirect
MH  - Glycosylphosphatidylinositols/*metabolism
MH  - Humans
MH  - Matrix Metalloproteinases/chemistry/genetics/*metabolism
MH  - Matrix Metalloproteinases, Membrane-Associated
MH  - *Metalloendopeptidases
MH  - Mice
MH  - Microscopy, Confocal
MH  - Molecular Sequence Data
MH  - Phenylalanine/analogs & derivatives/pharmacology
MH  - Phosphatidylinositol Diacylglycerol-Lyase
MH  - Phosphoinositide Phospholipase C
MH  - Protease Inhibitors/pharmacology
MH  - Recombinant Fusion Proteins/analysis/genetics
MH  - Sequence Alignment
MH  - Thiophenes/pharmacology
MH  - Tritium
MH  - Type C Phospholipases/pharmacology
EDAT- 1999/11/24 00:00
MHDA- 1999/11/24 00:01
CRDT- 1999/11/24 00:00
PHST- 1999/11/24 00:00 [pubmed]
PHST- 1999/11/24 00:01 [medline]
PHST- 1999/11/24 00:00 [entrez]
AID - 10.1074/jbc.274.48.34260 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Nov 26;274(48):34260-6. doi: 10.1074/jbc.274.48.34260.