PMID- 10085137
OWN - NLM
STAT- MEDLINE
DCOM- 19990429
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 13
DP  - 1999 Mar 26
TI  - Identification and characterization of the fifth membrane-type matrix
      metalloproteinase MT5-MMP.
PG  - 8925-32
AB  - A new member of the membrane-type matrix metalloproteinase (MT-MMP) subfamily
      tentatively named MT5-MMP was isolated from mouse brain cDNA library. It is
      predicted to contain (i) a candidate signal sequence, (ii) a propeptide region
      with the highly conserved PRCGVPD sequence, (iii) a potential furin recognition
      motif RRRRNKR, (iv) a zinc-binding catalytic domain, (v) a hemopexin-like domain,
      (vi) a 24-residue hydrophobic domain as a potential transmembrane domain, and
      (vii) a short cytosolic domain. Reverse transcriptase-polymerase chain reaction
      analysis of its transcripts indicates that MT5-MMP is expressed in a
      brain-specific manner consistent with the origin of its EST clone from
      cerebellum. It is also highly expressed during embryonic development at stages
      day 11 and 15. Like other MT-MMPs, MT5-MMP specifically activates progelatinase A
      when co-expressed in Madin-Darby canine kidney cells. Its ability to activate
      progelatinase A is dependent on its proteolytic activity since a mutation
      converting Glu to Ala in the zinc binding motif HE255LGH renders MT5-MMP inactive
      against progelatinase A. In contrast to other MT-MMPs, MT5-MMP tends to shed from
      cell surface as soluble proteinases, thus offering flexibility as both a cell
      bound and soluble proteinase for extracellular matrix remodeling processes. Taken
      together, these properties serve to distinguish MT5-MMP as a versatile MT-MMP
      playing an important role in extracellular matrix remodeling events in the brain 
      and during embryonic development.
FAU - Pei, D
AU  - Pei D
AD  - Department of Pharmacology, University of Minnesota, Minneapolis, Minnesota
      55455, USA. peixx003@tc.umn.edu
LA  - eng
SI  - GENBANK/AJ010262
GR  - CA76308/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Enzyme Precursors)
RN  - 0 (RNA, Messenger)
RN  - EC 3.4.24.- (Gelatinases)
RN  - EC 3.4.24.- (Matrix Metalloproteinases, Membrane-Associated)
RN  - EC 3.4.24.- (Metalloendopeptidases)
RN  - EC 3.4.24.- (Mmp24 protein, mouse)
RN  - EC 3.4.24.- (progelatinase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Brain/embryology/*enzymology
MH  - Cell Line
MH  - Cloning, Molecular
MH  - Embryonic and Fetal Development
MH  - Enzyme Activation/genetics
MH  - Enzyme Precursors/metabolism
MH  - Gelatinases/metabolism
MH  - Gene Expression Regulation, Developmental/genetics
MH  - Gene Expression Regulation, Enzymologic/genetics
MH  - Matrix Metalloproteinases, Membrane-Associated
MH  - Metalloendopeptidases/chemistry/*genetics/metabolism
MH  - Mice
MH  - Molecular Sequence Data
MH  - Mutation
MH  - RNA, Messenger/metabolism
MH  - Sequence Analysis, DNA
MH  - Sequence Homology, Amino Acid
EDAT- 1999/03/20 00:00
MHDA- 1999/03/20 00:01
CRDT- 1999/03/20 00:00
PHST- 1999/03/20 00:00 [pubmed]
PHST- 1999/03/20 00:01 [medline]
PHST- 1999/03/20 00:00 [entrez]
AID - 10.1074/jbc.274.13.8925 [doi]
AID - S0021-9258(19)87414-8 [pii]
PST - ppublish
SO  - J Biol Chem. 1999 Mar 26;274(13):8925-32. doi: 10.1074/jbc.274.13.8925.