3.4.24.80: membrane-type matrix metalloproteinase-1
This is an abbreviated version!
For detailed information about membrane-type matrix metalloproteinase-1, go to the full flat file.
Word Map on EC 3.4.24.80
-
3.4.24.80
-
metalloproteinases
-
mmp-2
-
metastasis
-
endothelial
-
zymography
-
angiogenesis
-
gelatin
-
gelatinase
-
timps
-
prommp-2
-
mesenchymal
-
invasiveness
-
vessel
-
basement
-
integrins
-
angiogenic
-
fibrosarcoma
-
matrigel
-
transwell
-
furin
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fibronectin
-
zymogen
-
gelatinolytic
-
progelatinase
-
ectodomain
-
invadopodia
-
hemopexin
-
alphavbeta3
-
proproteins
-
mt-mmps
-
collagen-rich
-
anti-invasive
-
matrix-degrading
-
collagenolytic
-
pro-matrix
-
emmprin
-
hemopexin-like
-
membrane-tethered
-
proenzyme
-
convertase
-
invasion-promoting
-
analysis
-
diagnostics
-
cona-induced
-
medicine
-
drug development
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endoglin
-
reck
-
podosomes
-
mmp-dependent
-
cortactin
- 3.4.24.80
- metalloproteinases
- mmp-2
- metastasis
- endothelial
-
zymography
- angiogenesis
- gelatin
- gelatinase
- timps
- prommp-2
- mesenchymal
-
invasiveness
- vessel
-
basement
- integrins
-
angiogenic
- fibrosarcoma
- matrigel
-
transwell
- furin
- fibronectin
- zymogen
-
gelatinolytic
- progelatinase
- ectodomain
-
invadopodia
- hemopexin
- alphavbeta3
- proproteins
-
mt-mmps
-
collagen-rich
-
anti-invasive
-
matrix-degrading
-
collagenolytic
-
pro-matrix
-
emmprin
-
hemopexin-like
-
membrane-tethered
- proenzyme
-
convertase
-
invasion-promoting
- analysis
- diagnostics
-
cona-induced
- medicine
- drug development
- endoglin
- reck
- podosomes
-
mmp-dependent
- cortactin
Reaction
endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at Asn37-/-Leu. Other bonds hydrolysed include Gly35-/-Ile in the propeptide of collagenase 3, and Asn341-/-Phe, Asp441-/-Leu and Gln354-/-Thr in the aggrecan interglobular domain =
Synonyms
ectMMP-14, gelatinase A, interstitial MT1-MMP, matrix metalloprotease 14, matrix metalloproteinase 14, matrix metalloproteinase MT 1, matrix metalloproteinase MT-MMP-1, matrix metalloproteinase MT1-MMP, matrix metalloproteinase-14, membrane type 1 matrix, membrane type 1 matrix metalloproteinase, membrane type 1 MMP, membrane type 1-matrix metalloproteinase, membrane type 1-MMP, membrane type I MMP, membrane type matrix metalloproteinase, membrane type MMP-1, membrane type MT1-MMP, membrane type-1 matrix metalloprotease, membrane type-1 matrix metalloprotease 1, membrane type-1 matrix metalloproteinase, membrane type-1 MMP, membrane type-I matrix metalloproteinase, membrane type-I MMP, membrane-anchored matrix metalloproteinase 14, membrane-type 1 matrix metalloproteinase, membrane-type 1 matrix metalloproteinase 1, membrane-type 1 MMP, membrane-type 1-matrix metalloproteinase, membrane-type I matrix metalloproteinase, membrane-type matrix metalloproteinase MT1-MMP, membrane-type matrix metalloproteinase-1, membrane-type metalloproteinase MT1-MMP, membrane-type MMP, metalloproteinase, MMP-14, MMP-2, MMP-8, MMP14, mmp14a, mmp14b, More, MT-MMP-1, MT-MMP1, MT1-MMP, MT1-MMP/MMP-14, MT1-MPP, MTI-MMP, pericellular collagenase, proteinase, matrix metallo-, sMT1-MMP
ECTree
3.4.24.80 membrane-type matrix metalloproteinase-1Advanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.24.80 - membrane-type matrix metalloproteinase-1
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
((Gly-Pro-4-hydroxyproline)5-Gly-Pro-Lys(7-methoxycoumarin-4-yl) acetyl)-Gly-Pro-Gln-Gly-Cys(4-methoxybenzyl)-Arg-Gly-Gln-Lys(2,4-dinitrophenyl)-Gly-Val-Arg-(Gly-Pro-4-hydroxyproline)5-NH2 + H2O
?
triple-helical substrate fTHP-9
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-L-Lys-Pro-Leu-Gly-Leu-Lys(N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2 + H2O
?
-
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Ala-Cys(p-OmeBz)-Trp-Ala-Arg(Dpa)-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Leu-(3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2 + H2O
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly + Leu-(3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Tyr-Ala-Nva-Trp-Met-Lys-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-GTQGQEARGS-dinitrophenol NH2 + H2O
?
substrate covering the aggrecanase cleavage site of aggrecan
-
-
?
(7-methoxycoumarin-4-yl)acetyl-L-Pro-Leu-Gly-Leu-(3-[2,4-dinitrophenyl]-L-2,3-diaminopropionyl)-Ala-Arg-NH2 + H2O
?
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-LAQAVRSSK-dinitrophenol NH2 + H2O
?
quenched fluorescent substrate mimicking the cleavage site of pro tumor necrosis factor alpha
-
-
?
(7-methoxycoumarin-4-yl)acetyl-P-3-cyclohexylalanyl-norvalyl-HA-dinitrophenol NH2 + H2O
?
collagenase substrate
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-cyclohexylalanine-Gly-norvaline-His-Ala-(N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-NH2 + H2O
?
-
degradation of synthetic substrate is pH-independent
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Ala-Cys(p-OMeBz)-Trp-Ala-Arg(N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Ala-Gln-Ala-Val-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Arg-Ser-Ser-Arg-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Ala-Nva-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Lys-Pro-Leu-Ala-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
?
-
-
-
-
?
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly-Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2 + H2O
(Gly-Pro-Hyp)5-Gly-Pro-Lys(Mca)-Gly-Pro-Gln-Gly + Cys(Mob)-Arg-Gly-Gln-Lys(Dnp)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
triple-helical substrate fTHP-9
-
-
?
alpha subunit of low density lipoprotein receptor-related protein + H2O
?
-
-
-
-
?
brain-specific angiogenesis inhibitor 1 + H2O
vasculostatin-120 + vasculostatin-40
-
the N terminus of BAI1 is cleaved extracellularly to generate a truncated receptor (vasculostatin-120) and a 40000 Da fragment (vasculostatin-40)
-
-
?
CCN3 + H2O
CPPQCPGR + DGQIGCVPR + KVEVPGECCEK + KPVMVIGTCTCHTNCPK + ?
-
-
-
?
collagen I alpha-1 chain + H2O
?
-
overall enzymatic activity is higher on the alpha-2 chain for both MMP-1 and MMP-2. In MMP-2 a marked difference for substrate affinity (higher for the alpha-1 chain) is overwhelmed by an even more marked propensity to cleave the alpha-2 chain
-
-
?
collagen I alpha-2 chain + H2O
?
-
overall enzymatic activity is higher on the alpha-2 chain for both MMP-1 and MMP-2. In MMP-2 a marked difference for substrate affinity (higher for the alpha-1 chain) is overwhelmed by an even more marked propensity to cleave the alpha-2 chain
-
-
?
collagen type I alpha-1 chain + H2O
?
-
the MMP-14 ectodomain preferentially cleaves the alpha-1 chain of collagen type I
-
-
?
cross-linked fibrin II + H2O
?
des-fibrinopeptides A and B, prepared by clotting fibrinogen with thrombin in the presence of factor XIIIa
-
-
?
dabcyl-Gly-Gly-Pro-Gln-Gly-Ile-Trp-Gly-Gln-Lys(fluorescein)-Ahx-Cys + H2O
?
-
-
-
?
endoglin + H2O
soluble endoglin + ?
-
MMP-14 cleaves membrane-bound endoglin at a site in close proximity to the transmembrane domain between Gly586-Leu-587
-
-
?
epidermal growth factor receptor + H2O
?
-
the enzyme plays a role in transactivation
-
-
?
extracellular matrix metalloproteinase inducer + H2O
extracellular matrix metalloproteinase inducer fragment + ?
-
-
22000 Da in length
-
?
galectin-3
?
-
cleaved to the 22 kDa degradation product when exposed to cells expressing membrane-anhored wild type MT1-MMP or the recombinant 50 kDa enzyme form
-
-
?
heparin-binding epidermal growth factor + H2O
heparin-binding epidermal growth factor mN3-fragment + ?
-
-
-
-
?
inactive pro-matrix metalloproteinase-2 + H2O
active matrix metalloproteinase-2 + ?
-
-
-
-
?
kidney injury molecule-1 + H2O
?
the enzyme cleaves and sheds the substrate's ectodomain
-
-
?
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2 + H2O
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly + Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
-
-
-
?
N-hexanoyl((GP-4-hydroxy-L-proline)5GPK(7-methoxycoumarin-4-yl)acetyl)GPQGLRGQK(2,4-dinitrophenyl)GVR(GP-4-hydroxy-L-proline)5-NH2 + H2O
N-hexanoyl((GP-4-hydroxy-L-proline)5GPK(7-methoxycoumarin-4-yl)acetyl)GPQGL + RGQK(2,4-dinitrophenyl)GVR(GP-4-hydroxy-L-proline)5-NH2
-
-
-
-
?
neuronal glial antigen 2 + H2O
?
three (210, 160, and 51-52 kDa) major cleavage products are formed
-
-
?
PA83
?
-
efficiently cleaved by MT1-MMP at the substrate-enzyme ratio as low as 1: 50
-
-
?
pro-MMP-2
?
-
MT1-MMP accomplishes full pro-MMP-2 activation, cleavage within the prodomain at the Asn37-Leu38 peptide bond
-
-
?
progelatinase A + H2O
gelatinase A + ?
-
activation, gelatinase A is matrix metalloproteinase-2
-
-
?
progelatinase A E375A + H2O
?
syn: pro-matrix metalloproteinase 2, cleaves at N37-L38 only
-
-
?
rat-tail tendon type I collagen + H2O
?
-
degraded by deltaTM-MT1-MMP at 37°C
-
-
?
receptor of complement component 1q + H2O
?
cleaves at Gly79-Gln80, cleavage with CAT/PEX domain leads to fragments with the following MW: 17 kDa, 12 kDa and 11 kDa
-
-
?
syndecan-1 G245L glutathione transferase protein + H2O
?
cleaves at G82-L83 peptide bond
-
-
?
type I collagen + H2O
denatured type I collagen
-
bound by recombinant linker/hemopexin C domain of MT1-MMP
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
?
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
?
fluorescent peptide
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
?
-
fluorescent peptide
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
?
-
cdMT1-MMP is catalytically more efficient towards small peptide substrates than deltaTM-MT1-MMP and the haemopexin domain of MT1-MMP facilitates the hydrolysis of triple-helical substrates
-
-
?
aggrecan + H2O
?
recombinant fusion protein with G332A mutation, substrate is cleaved at the aggrecanase site in its interglobular domain sequence segment, products are fragments with the following MW: 72 kDa, 66 kDA and 42 kDa
-
-
?
apolipoprotein E + H2O
?
-
the 34 kDa apoE protein is initially processed by MMP-14 into fragments with molecular masses of 28, 23, 21, and 11 kDa. The primary MMP-14 cleavage sites are Ala176-Ile177, Pro183-Leu184, Pro202-Leu203, and Gln249-Ile250. The MMP-14-mediated cleavage of apoE is consistent regardless of whether apoE exists in its lipid-bound or lipid-free form. Upon digestion with MMP-14, apoE loses its ability to suppress the platelet-derived growth factor-induced migration of rat vascular smooth muscle cells
-
-
?
E-cadherin + H2O
?
-
MT1-MMP sheds E-cadherin at cell-cell adherens junctions
-
-
?
Fibronectin + H2O
?
-
cell surface active pMMP-2 cDNAs bound to MT1-MMP enhances substrate digestion, cytoplasmic tail of MT1-MMP not required for digestion
-
-
?
Gelatin + H2O
?
-
rat-tail tendon type I collagen boiled for 5 min and denatured to gelatin, when degraded by deltaTM-MT1-MMP and cdMT1-MMP
-
-
?
heparin-binding epidermal growth factor + H2O
?
-
the enzyme removes the NH2-terminal 20 amino acids by cleaving between A-83LC
-
-
?
heparin-binding epidermal growth factor + H2O
?
-
the enzyme removes the NH2-terminal 20 amino acids by cleaving between A-83LC
-
-
?
hepatocyte growth factor activator inhibitor-1 + H2O
?
the 66 kDa protein is cleaved to 58, 42, and 16 kDa fragments
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
MMP14 is essential for proMMP-2 activation: pro-MMP-2 activation by MMP14/TIMP complex is realized in an environment of low TIMP concentration
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
the TIMP-2-dependent pathway of MMP-2 activation involves tissue inhibitor of MMP-2 as a bridging molecule between MT1-MMP and pro-MMP-2. Thus, net activity of MT1-MMP and MMP-2 is regulated in a complex manner depending on TIMP-2 concentration. For the TIMP-2-independent pathway, claudin recruits MT-MMP and MMP-2 at a tight junction to achieve elevated focal concentrations, and consequently enhances activation of pro-MMP-2. Pro-MMP-2 associates with TIMP-2-deficient cells through the hemopexin domain, and is processed by MT2-MMP
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
pro-MMP-2 is cleaved by an adjacent TIMP-2-free MT1-MMP between Asn37 and Leu38, generating an activated intermediate form that is further processed to the fully activated form by an intermolecular auto-cleavage when an intermediate form is present at a sufficiently high concentration at the cell surface, mechanism, overview. MT1-MMP cannot cleave other direct substrates at the TIMP-2 level that induces efficient pro-MMP-2 processing
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
the TIMP-2-dependent pathway of MMP-2 activation involves tissue inhibitor of MMP (TIMP)-2 as a bridging molecule between MT1-MMP and pro-MMP-2. Thus, net activity of MT1-MMP and MMP-2 is regulated in a complex manner depending on TIMP-2 concentration. For the TIMP-2-independent pathway, claudin recruits MT-MMP and MMP-2 at a tight junction to achieve elevated focal concentrations, and consequently enhances activation of pro-MMP-2. Pro-MMP-2 associates with TIMP-2-deficient cells through the hemopexin domain, and is processed by MT2-MMP
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
-
pro-MMP-2 is cleaved by an adjacent TIMP-2-free MT1-MMP between Asn37 and Leu38, generating an activated intermediate form that is further processed to the fully activated form by an intermolecular auto-cleavage when an intermediate form is present at a sufficiently high concentration at the cell surface, mechanism, overview. MT1-MMP cannot cleave other direct substrates at the TIMP-2 level that induces efficient pro-MMP-2 processing
-
-
?
progelatinase A + H2O
?
syn: pro-matrix metalloproteinase 2, leads to activation of progelatinase A
-
-
?
progelatinase A + H2O
?
-
syn: pro-matrix metalloproteinase 2, leads to activation of progelatinase A
-
-
?
progelatinase A + H2O
?
syn: pro-matrix metalloproteinase 2, leads to activation of progelatinase A
-
-
?
progelatinase A + H2O
?
-
syn: pro-matrix metalloproteinase 2, leads to activation of progelatinase A
-
-
?
progelatinase A + H2O
?
syn: pro-matrix metalloproteinase 2, leads to activation of progelatinase A
-
-
?
syndecan-1 core protein + H2O
?
cleaves preferably at G245-L246 peptide bond
-
-
?
transglutaminase + H2O
?
tissue transglutaminase that binds fibronectin
-
-
?
Type I collagen + H2O
?
-
-
-
-
?
Type I collagen + H2O
?
-
cleavage of collagen by MT1-MMP regulates cell growth and invasion in a collagen-rich environment
-
-
?
Type I collagen + H2O
?
-
type I collagen binds MT1-MMP via a hemopexin-like domain and is cleaved
-
-
?
additional information
?
-
-
membrane type 1 matrix metalloproteinase activates progelatinase A, a type IV collagenase, on the cell surface of tumors. Membrane type 1-matrix metalloproteinase may play an important role in the invasive growth and spread of breast cancer cells by specifically activating pro-MMP-2 to cleave the connective-tissue barrier
-
-
?
additional information
?
-
role in extracellular matrix remodelling under physiological and pathological conditions
-
-
?
additional information
?
-
degrades components of tissue barriers, regulates cell-extracellular matrix interaction by processing cell adhesion molecules such as CD44 and integrin alpha v chain
-
-
?
additional information
?
-
-
degrades components of tissue barriers, regulates cell-extracellular matrix interaction by processing cell adhesion molecules such as CD44 and integrin alpha v chain
-
-
?
additional information
?
-
-
the enzyme regulates extracellular matrix remodeling and is capable of cleaving a wide variety of transmembrane proteins. The enzymatic activity of MT1-MMP is regulated by endogenous inhibitors, TIMP, the tissue inhibitor of metalloproteinases
-
-
?
additional information
?
-
-
hydrolysis of triple helical substrates that, via addition of N-terminal alkyl chains, differ in their thermal stabilities, substitution of Cys(4-methoxybenzyl) for Leu in the P1' subsite is greatly favored by MMP-14, increase in substrate triple-helical thermal stability leads to the decreased ability of the enzyme to cleave such substrates
-
-
?
additional information
?
-
-
rat-tail tendon type I collagen not degraded by cdMT1-MMP at 37°C
-
-
?
additional information
?
-
-
MT1-MMP plays an important role in early cancer dissemination by converting epithelial cells to migratory mesenchymal-like cells
-
-
?
additional information
?
-
-
pro-alpha2 integrin subunit is not a substrate
-
-
?
additional information
?
-
-
enzyme regulation, transcription factor EGR1 is involved, overview
-
-
?
additional information
?
-
-
membrane-type MMPs are membrane spanning binding sites that play an important role in the cell surface activation of MMPs such as MMP-2
-
-
?
additional information
?
-
-
MT1-MMP on cell surface rapidly turns over by auto-degradation or clathrin-dependent internalization. MT1-MMP inactivated by TIMP-2 avoids auto-degradation, and accumulates on the cell surface, overview. Tetraspanins are attracting attention as binding proteins of MT1-MMP, which regulate subcellular localization and compartmentalization of MT1-MMP and consequent MT1-MMP activities
-
-
?
additional information
?
-
-
overview of MT1-MMP-associating proteins by localization and MT1-MMP-associating membrane proteins by function. Some proteins, such as MT1-SP, EGFR, 5T4, DCP, and CD36L1, preferentially precipitate pro-MT1-MMP, other proteins, e.g. GA733-1, HAI-1, HAI-2, TF, THBD, and CD9, precipitate preferentially the active form of MT1-MMP indicating that these proteins may form a complex on the cell surface
-
-
?
additional information
?
-
-
membrane proteins were cleaved by MT1-MMP in a MMI270-sensitive manner
-
-
?
additional information
?
-
the enzyme does not degrade fibroblast growth factor-2 or fibroblast growth factor receptor-2
-
-
?
additional information
?
-
interaction analysis of MMP14 with proteins in HeLa cells identified by inactive catalytic domain capture yeast 2-hybrid analysis, overview. Detection of CCN5 as a MMP14 substrate by yeast 2-hybrid screening
-
-
?
additional information
?
-
CCN = cysteine rich protein 61/connective tissue growth factor/nephroblastoma overexpressed
-
-
?
additional information
?
-
modeling of enzyme-substrate interaction
-
-
?
additional information
?
-
-
in vivo growth of FaDu cells co-injected with murine fibroblasts is increased, while their progression is reduced in MT1-MMP-deficient fibroblasts, overview
-
-
?
additional information
?
-
-
MT1-MMP on cell surface rapidly turns over by auto-degradation or clathrin-dependent internalization. MT1-MMP inactivated by TIMP-2 avoids auto-degradation, and accumulates on the cell surface, overview. Tetraspanins are attracting attention as binding proteins of MT1-MMP, which regulate subcellular localization and compartmentalization of MT1-MMP and consequent MT1-MMP activities
-
-
?
additional information
?
-
-
MT1-MMP is increased in myocardial ischemia and reperfusion, and contributes to myocardial dysfunction, upstream induction mechanism by release of endothelin and protein kinase C activation, microdialysis analysis, overview
-
-
?
