PMID- 10799478
OWN - NLM
STAT- MEDLINE
DCOM- 20000608
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 275
IP  - 19
DP  - 2000 May 12
TI  - Membrane type 4 matrix metalloproteinase (MMP17) has tumor necrosis factor-alpha 
      convertase activity but does not activate pro-MMP2.
PG  - 14046-55
AB  - Membrane type 4 matrix metalloproteinase (MT4-MMP) shows the least sequence 
      homology to the other MT-MMPs, suggesting a distinct function for this protein. 
      We have isolated a complete cDNA corresponding to the mouse homologue which 
      includes the signal peptide and a complete pro-domain, features that were lacking 
      from the human form originally isolated. Mouse MT4-MMP (mMT4-MMP) expressed in 
      COS-7 cells is located at the cell surface but does not show ability to activate 
      pro-MMP2. The pro-catalytic domain was expressed in Escherichia coli as insoluble 
      inclusions and active enzyme recovered after refolding. Activity of the isolated 
      catalytic domain against synthetic peptides commonly used for MMP enzyme assays 
      could be inhibited by TIMP1, -2, and -3. The recombinant mMT4-MMP catalytic 
      domain was also unable to activate pro-MMP2 and was very poor at hydrolyzing 
      components of the extracellular matrix with the exception of fibrinogen and 
      fibrin. mMT4-MMP was able to hydrolyze efficiently a peptide consisting of the 
      pro-tumor necrosis factor alpha (TNFalpha) cleavage site, a glutathione 
      S-transferase-pro-TNFalpha fusion protein, and was found to shed pro-TNFalpha 
      when co-transfected in COS-7 cells. MT4-MMP was detected by Western blot in 
      monocyte/macrophage cell lines which in combination with its fibrinolytic and 
      TNFalpha-converting activity suggests a role in inflammation.
FAU - English, W R
AU  - English WR
AD  - School of Biological Sciences, University of East Anglia, University Plain, 
      Norwich, Norfolk NR4 7TJ, United Kingdom.
FAU - Puente, X S
AU  - Puente XS
FAU - Freije, J M
AU  - Freije JM
FAU - Knauper, V
AU  - Knauper V
FAU - Amour, A
AU  - Amour A
FAU - Merryweather, A
AU  - Merryweather A
FAU - Lopez-Otin, C
AU  - Lopez-Otin C
FAU - Murphy, G
AU  - Murphy G
LA  - eng
SI  - GENBANK/AJ010731
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 (DNA, Complementary)
RN  - 0 (Enzyme Precursors)
RN  - 0 (Protease Inhibitors)
RN  - 0 (Tumor Necrosis Factor-alpha)
RN  - EC 3.4.24.- (ADAM Proteins)
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 3.4.24.86 (ADAM17 Protein)
SB  - IM
MH  - ADAM Proteins
MH  - ADAM17 Protein
MH  - Animals
MH  - Base Sequence
MH  - Catalysis
MH  - Cell Line
MH  - DNA, Complementary
MH  - Enzyme Activation
MH  - Enzyme Precursors/*metabolism
MH  - Humans
MH  - Leukocytes/enzymology
MH  - *Matrix Metalloproteinases
MH  - Matrix Metalloproteinases, Membrane-Associated
MH  - Metalloendopeptidases/genetics/*metabolism
MH  - Mice
MH  - Molecular Sequence Data
MH  - Protease Inhibitors/pharmacology
MH  - Protein Folding
MH  - Protein Processing, Post-Translational
MH  - Sequence Homology, Amino Acid
MH  - Tumor Necrosis Factor-alpha/*metabolism
EDAT- 2000/05/09 09:00
MHDA- 2000/06/10 09:00
CRDT- 2000/05/09 09:00
PHST- 2000/05/09 09:00 [pubmed]
PHST- 2000/06/10 09:00 [medline]
PHST- 2000/05/09 09:00 [entrez]
AID - S0021-9258(19)80567-7 [pii]
AID - 10.1074/jbc.275.19.14046 [doi]
PST - ppublish
SO  - J Biol Chem. 2000 May 12;275(19):14046-55. doi: 10.1074/jbc.275.19.14046.