Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(7-methoxycoumarin-4-yl)-acetyl-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(dinitrophenyl)-NH2 + H2O
(7-methoxycoumarin-4-yl)-acetyl-Arg-Pro-Lys-Pro-Val-Glu + Nva-Trp-Arg-Lys(dinitrophenyl)-NH2
-
-
-
-
?
(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-Pro-cyclohexylalanine-Gly-Nve-His-Ala-(N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-NH2 + H2O
?
-
degradation of synthetic substrate is pH-independent
-
-
?
(GP4Hyp)4-GPQGIAGQRGVVGL4Hyp(GP4Hyp)4-NH2 + H2O
(GP4Hyp)4-GPQG + IAGQRGVVGL4Hyp(GP4Hyp)4-NH2
alpha1(I)772-786 THP
-
-
?
(GP4Hyp)4GPQ-Sar-IAGQRGVVG-Nle-GL4Hyp(GP4Hyp)4-NH2 + H2O
(GP4Hyp)4GPQ-Sar + IAGQRGVVG-Nle-GL4Hyp(GP4Hyp)4-NH2
-
-
-
?
(GP4Hyp)4GPQ-Sar-IAGQRGVVGL4Hyp(GP4Hyp)4-NH2 + H2O
(GP4Hyp)4GPQ-Sar + IAGQRGVVGL4Hyp(GP4Hyp)4-NH2
-
-
-
?
(GP4Hyp)4GPQGIAGQRGVVG-Nle-4Hyp(GP4Hyp)4-NH2 + H2O
(GP4Hyp)4GPQG + IAGQRGVVG-Nle-4Hyp(GP4Hyp)4-NH2
the substrate is hydrolyzed at the Gly775-Ile776 bond by the enzyme
-
-
?
2,4-dinitrophenyl-Pro-beta-cyclohexyl-Ala-Gly-Cys(Me)-His-Ala-Lys(N-methyl-2-aminobenzoyl)-NH2 + H2O
?
-
-
-
?
2,4-dinitrophenyl-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg-NH2 + H2O
?
Frog
-
-
-
-
?
2,4-dinitrophenyl-Pro-Leu-Ala-Leu-Trp-Ala-Arg-OH + H2O
?
-
-
-
?
Ac-Pro-Leu-Gly-SCH2(iBu)CO-Leu-Leu-GlyOEt + H2O
?
-
-
-
-
?
acetyl-Pro-Ala-Gly-Ile-Ala-Gly-Gln-Arg-ethyl ester + H2O
acetyl-Pro-Ala-Gly + Ile-Ala-Gly-Gln-Arg-ethyl ester
Frog
-
-
-
?
acetyl-Pro-Gln-Gly-Ile-Ala-Gly-ethyl ester + H2O
acetyl-Pro-Gln-Gly + Ile-Ala-Gly-ethyl ester
Frog
-
-
-
?
acetyl-Pro-Gln-Gly-Ile-Ala-Gly-Gln-Arg-ethyl ester + H2O
acetyl-Pro-Gln-Gly + Ile-Ala-Gly-Gln-Arg-ethyl ester + H2O
Frog
-
-
-
?
acetyl-Pro-Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln-Arg-ethyl ester + H2O
acetyl-Pro-Gly-Pro-Gln-Gly + Ile-Ala-Gly-Gln-Arg-ethyl ester
Frog
-
-
-
?
acetyl-Pro-Leu-Gly-Ala-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ala + Leu-Gly-ethyl ester
acetyl-Pro-Leu-Gly-Ile-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ile + Leu-Gly-ethyl ester
acetyl-Pro-Leu-Gly-Ile-Leu-Gly-OC2H5 + H2O
?
-
-
-
-
?
acetyl-Pro-Leu-Gly-Leu-Ala-Gly-OC2H5 + H2O
?
-
-
-
-
?
acetyl-Pro-Leu-Gly-Leu-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Leu + Leu-Gly-ethyl ester
acetyl-Pro-Leu-Gly-Leu-Leu-Gly-OC2H5 + H2O
?
-
-
-
-
?
acetyl-Pro-Leu-Gly-Phe-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Phe + Leu-Gly-ethyl ester
acetyl-Pro-Leu-Gly-S-Leu-Leu-Gly ethyl ester + H2O
?
-
-
-
-
?
acetyl-Pro-Leu-Gly-SCH[CH2CH(CH3)2CO]-Leu-Leu-OC2H5 + H2O
?
-
-
-
-
?
acetyl-Pro-Leu-Gly-SCH[CH2CH(CH3)2]CO-Leu-Leu-OC2H5 + H2O
acetyl-Pro-Leu-Gly + HSCH[CH2CH(CH3)2]CO-Leu-Leu-OC2H5
-
-
-
-
?
acetyl-Pro-Leu-Gly-Val-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Val + Leu-Gly-ethyl ester
alpha1(I)772-786 triple-helical peptide + H2O
?
-
-
-
-
?
bovine type I collagen + H2O
?
-
-
-
-
?
butyloxycarbonyl-Pro-Ala-Gly-Ile-Ala-Gly-ethyl ester + H2O
butyloxycarbonyl-Pro-Ala-Gly + Ile-Ala-Gly-ethyl ester
Frog
-
-
-
?
butyloxycarbonyl-Pro-Gln-Gly-Ile-Ala-Gly-ethyl ester + H2O
butyloxycarbonyl-Pro-Gln-Gly + Ile-Ala-Gly-ethyl ester
Frog
-
-
-
?
collagen I alpha-1 chain + H2O
?
collagen I alpha-2 chain + H2O
?
collagen III + H2O
?
-
degradation
-
-
?
Collagen type I + H2O
?
-
-
-
?
Collagen type III + H2O
?
collagen type IV alpha2 + H2O
?
GAQGIAGQ + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
GLQGIAGQ + H2O
?
-
-
-
-
?
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln-Gln + H2O
Gly-Pro-Gln-Gly + Ile-Ala-Gly-Gln-Gln
-
-
-
-
?
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln-Gln-Arg-Gly-Val-Val-Gly-Leu-Hyp-NH2 + H2O
Gly-Pro-Gln-Gly + Ile-Ala-Gly-Gln-Gln-Arg-Gly-Val-Val-Gly-Leu-Hyp-NH2
-
-
-
-
?
GNQGIAGQ + H2O
?
-
-
-
-
?
GNVGLAGA + H2O
?
-
-
-
-
?
GP-Hyp-GIAGA + H2O
?
-
-
-
-
?
GP-Hyp-IAGQ + H2O
?
-
-
-
-
?
GPDGIAGQ + H2O
?
-
-
-
-
?
GPLGIAGP + H2O
?
-
-
-
-
?
GPLGIAGQ + H2O
?
-
-
-
-
?
GPQGIAGA + H2O
?
-
-
-
-
?
GPQGIAGH + H2O
?
-
-
-
-
?
GPQGIAGP + H2O
?
-
-
-
-
?
GPQGIAGQ + H2O
?
-
-
-
-
?
GPQGIAGT + H2O
?
-
-
-
-
?
GPQGLAGQ + H2O
?
-
-
-
-
?
GPRGIAGQ + H2O
?
-
-
-
-
?
GPVGIAGQ + H2O
?
-
-
-
-
?
Human alpha2-macroglobulin + H2O
?
-
cleavage site: Gly679-Leu680
-
-
?
human pregnancy zone protein + H2O
?
-
cleavage sites: Gly685-Leu686, Gly687-Val688, Gly757-Ile758, Ala684-Leu684, and Ala685-Met686
-
-
?
human type I collagen + H2O
?
human type II collagen + H2O
?
human type III collagen + H2O
?
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
?
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
Mca-Pro-Leu-Gly + Leu-Dpa-Ala-Arg-NH2
-
-
-
?
Pro-Gln-Gly-Ile-Ala-Gly-Gln-Arg-ethyl ester + H2O
Pro-Gln-Gly + Ile-Ala-Gly-Gln-Arg-ethyl ester
Frog
-
-
-
?
PSYFLNAG + H2O
?
-
-
-
-
?
rat alpha1 macroglobulin + H2O
?
-
cleavage site: His681-Leu682, Phe691-Leu692
-
-
?
rat alpha1-inhibitor 3 (27J) + H2O
?
-
cleavage sites: Ala666-Val667
-
-
?
rat alpha1-inhibitor 3 (2J) + H2O
?
-
cleavage sites: Pro683-Val684
-
-
?
rhodamine 6G-labeled KDP-6-aminohexanoic acid-GPLGIAGIG-6-aminohexanoic acid-PKGY + H2O
rhodamine 6G-labeled KDP-6-aminohexanoic acid-GPLG + IAGIG-6-aminohexanoic acid-PKGY
-
fluorescent biosensor, substrate for matrix metalloproteinases MMP-2, MMP-9, MMP-14
-
-
?
type I procollagen + H2O
type I collagen + ?
-
-
-
-
?
type II collagen + H2O
?
-
interstitial collagen
-
-
?
type III collagen + H2O
?
[alpha1(I)]2alpha2(I)772-784 triple-helical peptide + H2O
?
-
-
-
-
?
[alpha1(II)769-783] fluorogenic triple-helical peptide-3 + H2O
?
-
-
-
-
?
[alpha1(II)769-783] fluorogenic triple-helical peptide-4 + H2O
?
-
-
-
-
?
[alpha1(II)769-783] single-stranded peptide-3 + H2O
?
-
-
-
-
?
fTHP-3 + H2O
additional information
-
acetyl-Pro-Leu-Gly-Ala-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ala + Leu-Gly-ethyl ester
Frog
-
-
-
?
acetyl-Pro-Leu-Gly-Ala-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ala + Leu-Gly-ethyl ester
-
very low activity
-
?
acetyl-Pro-Leu-Gly-Ala-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ala + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Ala-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ala + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Ala-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ala + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Ile-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ile + Leu-Gly-ethyl ester
Frog
-
-
-
?
acetyl-Pro-Leu-Gly-Ile-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ile + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Ile-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ile + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Ile-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ile + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Ile-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ile + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Leu-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Leu + Leu-Gly-ethyl ester
Frog
-
-
-
?
acetyl-Pro-Leu-Gly-Leu-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Leu + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Leu-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Leu + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Leu-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Leu + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Leu-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Leu + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Phe-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Phe + Leu-Gly-ethyl ester
Frog
-
-
-
?
acetyl-Pro-Leu-Gly-Phe-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Phe + Leu-Gly-ethyl ester
-
very low activity
-
?
acetyl-Pro-Leu-Gly-Phe-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Phe + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Phe-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Phe + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Phe-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Phe + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Val-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Val + Leu-Gly-ethyl ester
Frog
-
-
-
?
acetyl-Pro-Leu-Gly-Val-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Val + Leu-Gly-ethyl ester
-
very low activity
-
?
acetyl-Pro-Leu-Gly-Val-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Val + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Val-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Val + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Val-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Val + Leu-Gly-ethyl ester
-
-
-
?
casein + H2O
?
-
casein zymography assay method
-
-
?
Collagen + H2O
?
Frog
-
-
-
-
?
Collagen + H2O
?
Frog
-
native reconstituted guinea pig skin collagen fibrils
-
-
?
Collagen + H2O
?
-
-
-
-
?
Collagen + H2O
?
-
-
two collagen fragments representing 77% and 23% respectively of the length of the collagen molecule
?
Collagen + H2O
?
-
native reconstituted guinea pig skin collagen fibrils
-
-
?
Collagen + H2O
?
-
rat tendon type I collagen
-
-
?
Collagen + H2O
?
-
cleavage sites: of calf skin alpha1(I) chain collagen Gly775-Ile776, of calf skin collagen alpha2(I) chain Gly775-Leu776, of human liver collagen alpha1(III)chain Gly775-Ile776
-
-
?
Collagen + H2O
?
-
type X collagen, two cleavage sites, three products with 32000 Da, 18000 Da and 9000 Da chains
-
-
?
Collagen + H2O
?
-
183RWTNNFREY191, together with the C-terminal hemopexin domain, is essential for collagenolytic activity but additional structural elements in the catalytic domain are also required. These elements probably act in a concerted manner to cleave the collagen triple helix
-
-
?
Collagen + H2O
?
-
type I collagen
-
-
?
Collagen + H2O
?
natural collagen fascicles (termed extracellular matrix/ECM) from tendons of 6-months-old rats, degradation patterns of natural collagen-rich extracellular matrix by MMP-1 compared to MMP-13
-
-
?
Collagen + H2O
?
-
native calf skin collagen
-
-
?
Collagen + H2O
?
-
below 30°C the enzyme catalyzes a small number of cleavages in the native collagen molecule with no loss in tertiary structure. Fragments of 75, 67, and 62% of the molecular length from the A end are formed. At 37°C and neutral pH, the enzyme degrades native collagen fibrils or molecules to peptides most of which are dialyzable
-
-
?
Collagen + H2O
?
natural collagen fascicles (termed extracellular matrix/ECM) from tendons of 6-months-old rats, degradation patterns of natural collagen-rich extracellular matrix by MMP-1 compared to MMP-13. Cleavage sites identified in Col I-rich ECM under proteolytic degradation by MMP-1, overview
-
-
?
collagen I + H2O
?
-
degradation
-
-
?
collagen I + H2O
?
-
degradation, calf skin substrate
-
-
?
collagen I + H2O
?
-
degradation
-
-
?
collagen I alpha-1 chain + H2O
?
-
MMP-14 ectodomain preferentially cleaves the alpha-1 chain
-
-
?
collagen I alpha-1 chain + H2O
?
-
the overall enzymatic activity is higher on the alpha-2 chain for MMP-1 and MMP-2
-
-
?
collagen I alpha-2 chain + H2O
?
-
MMP-14 ectodomain preferentially cleaves the alpha-1 chain
-
-
?
collagen I alpha-2 chain + H2O
?
-
the overall enzymatic activity is higher on the alpha-2 chain for MMP-1 and MMP-2
-
-
?
Collagen type III + H2O
?
-
-
-
?
Collagen type III + H2O
?
ability of MMP-1 to unwind triple-helical collagen
-
-
?
Collagen type III + H2O
?
ability of MMP-1 to unwind triple-helical collagen. After binding the triple helix, the CAT domain can reorient to properly face the cleavage site. The dual Arg electrostatic ruler motif is modeled to be exposed in the type III collagen fibril. The two Arg residues found in type III collagen are conserved in the P5' and P17' subsites of types I and II collagen
-
-
?
collagen type IV alpha2 + H2O
?
cleavage at sites L715 and T917
-
-
?
collagen type IV alpha2 + H2O
?
cleavage at sites L715 and T917
-
-
?
decorin + H2O
?
cleavage at site T310
-
-
?
decorin + H2O
?
cleavage at site T310
-
-
?
human type I collagen + H2O
?
-
-
-
-
?
human type I collagen + H2O
?
-
-
-
-
?
human type I collagen + H2O
?
-
-
-
-
?
human type II collagen + H2O
?
-
-
-
-
?
human type II collagen + H2O
?
-
-
-
-
?
human type II collagen + H2O
?
-
-
-
-
?
human type III collagen + H2O
?
-
-
-
-
?
human type III collagen + H2O
?
-
-
-
-
?
human type III collagen + H2O
?
-
-
-
-
?
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
?
-
fluorogenic substrate
-
-
?
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
?
-
fluorogenic substrate
-
-
?
Type I collagen + H2O
?
-
-
-
-
?
Type I collagen + H2O
?
-
-
-
-
?
Type I collagen + H2O
?
-
a plasmin/MMP-10/MMP-1 proteolytic axis effectively enhances collagen type 1 degradation
-
-
?
Type I collagen + H2O
?
-
interstitial collagen
-
-
?
Type I collagen + H2O
?
-
production of type I collagen by periodontal ligament cells
-
-
?
Type I collagen + H2O
?
-
-
-
-
?
type III collagen + H2O
?
-
-
-
-
?
type III collagen + H2O
?
-
interstitial collagen
-
-
?
type III collagen + H2O
?
-
mechanism of interaction and cleavage of human type III collagen by fibroblast MMP-1 using a panel of recombinant human type III collagens containing engineered sequences in the vicinity of the cleavage site around residue I785, e.g. mutant FG-5015 I785P. Structural features of cleavage site determination in collagen type III, overview
-
-
?
fTHP-3 + H2O
additional information
-
-
the fluorogenic triple-helical substrate mimics the behavior of the native collagen substrate and may be useful for the investigation of collagenase triple-helical activity
the Gly-Leu bond is cleaved, the triple helix denatures and the two products generated are the single-stranded N-terminal peptide C6-(Gly-Pro-Hyp)5-Gly-Pro-Lys[(7-methoxycoumarin-4-yl)acetyl]-Gly-Pro-Gln-Gly and the single-stranded C-terminal peptide Leu-Arg-Gly-Gln-Lys-(2,4-dinitrophenyl)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
-
?
additional information
?
-
-
relative rates of hydrolysis in decreasing order: GPQGIAGQ, PSYFLNAG, GNVGLAGA
-
-
?
additional information
?
-
-
the enzyme prefers very lipophilic sequences
-
-
?
additional information
?
-
-
ligation of keratinocyte alpha2beta1 integrin by type 1 collagen induces expression of matrix metalloproteinase-1. The MMP-1 activity is required for the alpha2beta1 integrin-dependent migration of primary keratinocytes across collagenous matrices. MMP-1 binds to the I domain of the alpha2 intergrin subunit
-
-
?
additional information
?
-
-
matrix metalloproteinase 1 interacts with neuronal integrins and stimulates dephosphorylation of Akt and neuronal death through a non-proteolytic mechanism. MMP-1 might contribute to the neuronal damage which occurs in association with degenerative and inflammatpry conditions characterized by elevated levels of this proteinase
-
-
?
additional information
?
-
-
MMP-1 is involved in intestinal re-epithelization in vivo and is upregulated by cytokines relevant in wound repair
-
-
?
additional information
?
-
-
enzyme regulation on expression and protein levels, overview
-
-
?
additional information
?
-
-
MMP-1 is a single effector of the Raf/MEK/ERK signaling cascade, that prevents progression of melanoma from a primary to metastatic tumor
-
-
?
additional information
?
-
-
MMP1 expression is increased in Xeroderma pigmentosum, a rare, recessively inherited genetic disease characterized by skin cancer proneness and premature aging in photoexposed area
-
-
?
additional information
?
-
-
substance P up-regulates matrix metalloproteinase-1 and down-regulates collagen in human lung fibroblast, overview
-
-
?
additional information
?
-
-
active MMP-10, EC 3.4.24.22, does not cleave collagen type 1 directly, it does activate the collagenase MMP-1
-
-
?
additional information
?
-
-
matrix metalloproteinases are endopeptidases capable of cleaving various components of extracellular matrix
-
-
?
additional information
?
-
-
MMP-1 cleaves a specific glycine-isoleucine or glycine-leucine bond in fibrillar collagens, despite the presence of this sequence in other parts of the protein
-
-
?
additional information
?
-
MMP-1 preferentially binds the alpha2(I) chain
-
-
?
additional information
?
-
several different peptoid residues are incorporated into triple helical substrates at subsites P3, P1, P1', and P10' individually or in combination, and the effects of the peptoid residues are evaluated on the activities of full-length MMP-1 and other MMPs, collagenolytic matrix metalloproteinase activities toward peptomeric triple-helical substrates, overview. Most peptomers show little discrimination between MMPs. A peptomer containing N-methyl Gly (sarcosine) in the P1' subsite and N-isobutyl Gly (Nle) in the P10' subsite is not hydrolysed by MMP-1. Also no activity with (GP4Hyp)4-GPQG-Sar-AGQRGVVGL4Hyp(GP4Hyp)4-NH2, (GP4Hyp)4GPQG-Sar-AGQRGVVG-Nle-4Hyp(GP4Hyp)4-NH2, (GP4Hyp)4G-Sar-QGIAGQRGVVGL4Hyp(GP4Hyp)4-NH2, (GP4Hyp)4GPQGWAGQRGVVG-Nle-4Hyp(GP4Hyp)4-NH2, (GP4Hyp)4-GPQG-NIle-AGQRGVVGL4Hyp(GP4Hyp)4-NH2, (GP4Hyp)4GPQG-Sar-AGQRGVVG-Nle-4Hyp(GP4Hyp)4-NH2, (GP4Hyp)4GP-Lys(Mca)-G-Sar-AGQRGV-Lys(Dnp)-GNle-4Hyp(GP4Hyp)4-NH2 and Ac-(GP4Hyp)4-GP-Lys(Mca)-G-Sar-AGQRGV-Lys(Dnp)G-Nle-4Hyp(GP4Hyp)4-NH2, 4Hyp is hydroxyproline. The P10' subsite is important for collagenous substrate interaction with MMP-1, and this interaction occurs via the HPX domain. Molecular dynamics (MD) simulations, model of MMP-1 with the alpha1(I)772-786 THP, overview
-
-
?
additional information
?
-
-
myocardial matrix degradation by MMP-1 induced by thyroid hormone through enzyme activation, enzyme regulation involving suppression of tissue inhibitors of matrix metalloproteinases TIMPs and distribution, overview
-
-
?
additional information
?
-
proteomic analysis of MMP-1 activity using LC-MS/MS analysis
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(3-[(2-hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-phenyl)-carbamic acid tert-butyl ester
-
-
2-[benzyl([[(2-methylphenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
-
-
2-[benzyl([[(4-chlorophenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
-
-
2-[benzyl([[(4-fluorophenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
-
-
2-[benzyl([[(4-methylphenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
-
-
3-[((1R,4S)-7,7-Dimethyl-2-oxo-bicyclo[2.2.1]hept-1-ylmethanesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[(2,4-Dinitro-phenylsulfanyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[(2,5-Dichloro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[(2-Hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-benzoic acid
-
-
3-[(3-Chloro-4-ethylamino-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[(3-Chloro-4-nitro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[(4-Bromo-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[(4-Chloro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[(4-Fluoro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[(5-Dimethylamino-naphthalene-1-sulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[(Heptadecachlorooctane-1-sulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[3-(2,4-Dichloro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
3-[3-(3,4-Dichloro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
3-[3-(3-Chloro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
3-[3-(4-Chloro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
3-[3-(4-Chloro-phenylsulfonyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
3-[3-(4-Fluoro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
3-[3-(4-Fluoro-phenylsulfonyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
3-[3-Benzoyl-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
3-[Benzenesulfonyl-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[[3-[3-(4-chloro-phenylsulfonyl)-ureido]-benzenesulfonyl]-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[[3-[3-(4-fluoro-phenylsulfonyl)-ureido]-benzenesulfonyl]-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[[4-[3-(4-chloro-phenylsulfonyl)-ureido]-benzenesulfonyl]-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
3-[[4-[3-(4-fluoro-phenylsulfonyl)-ureido]-benzenesulfonyl]-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
4-[(2-Hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-benzoic acid
-
-
Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
-
pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
alpha2-Macroglobulin
-
-
-
astragaloside IV
AST, inhibits matrix metalloproteinase-1 in photoaging skin. Astragaloside IV is one of the major active compoxadnents extracted from Astragalus membranaceus. Effects of AST against collagen reducxadtion in UV-induced skin aging in human skin fibroblasts, and mechanism of multiple anti-photoaging effects, overview
benzo[a]pyrene
increases the mRNA levels of matrix metalloproteinases MMP-1, MMP-2, MMP-3, and MMP-9 in vascular smooth muscle cells and promotes the migration and invasion of cells
C3H7-POOH-Ile-Trp-NHMe
-
phosphonamidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
ClCH2CO-(N-OH)Leu-Ala-Gly-NH2
-
2-5 mM, 25°C, pH 7.4, Tris buffer, strong irreversible inhibition, inhibition increases with higher temperatures and inhibitor concentration
ClCH2CO-(N-OH)Phe-Ala-Ala-NH2
-
-
dexamethasone
-
significantly decreases active MMP-1 level and inhibits active MMP-1
disodium isostearyl 2-O-L-ascorbyl phosphate
-
i.e. disodium 2-(1,3,3-trimethyl-n-butyl)-5,7,7-trimethyl-n-octyl-L-ascorbyl phosphate or VCP-IS-2Na, an amphiphilic vitamin C derivative, increases proliferation of normal human skin fibroblasts, NHDFs and NB1RGBs, by 123% and 135% and inhibits MMP-1 production by a maximum of 19% and 11% in NHDF and NB1RGB cells at 0.05 mM, respectively
epigallocatechin gallate
competitive. the galloyl group is important for inhibitory activity
epigallocatechin-3-gallate
-
-
EtO-POOH-CH2-Leu-Trp-NHMe
-
pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
EtO-POOH-Ile-Ala-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
EtO-POOH-Ile-Ala-Gly-Gln-Arg-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt, weak inhibition
EtO-POOH-Ile-Ala-Gly-Glu-Arg(NO2)-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt, weak inhibition
EtO-POOH-Ile-Ala-Gly-Glu-Arg-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt, weak inhibition
EtO-POOH-Ile-Leu-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
EtO-POOH-Ile-Trp-NHMe
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
EtO-POOH-Ile-Tyr(OBzl)-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
EtO-POOH-Ile-Tyr-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
exopolysaccharide
-
obtained from mycelial culture of Grifola frondosa HB0071 may contribute to inhibitory action in photoaging skin by reducing the MMP-1-related matrix degradation system
-
fisetin
mixed-type inhibition
GM6001
-
a broad-spectrum MMP inhibitor
hexyl-POOH-CH2-Leu-Trp-NHMe
-
pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
hexyl-POOH-Leu-Trp-NHMe
-
pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
hexyl-POOH-O-Leu-Trp-NHMe
-
pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
HSCH(CH2C6H5)CO-Ala-Gly-Gln-D-Arg-NH2
Frog
-
-
HSCH(CH2CH(CH3)2)CO -Ala-Gly-Gln-D-Arg-NH2
Frog
-
-
HSCH2CH(NH2)CO-Ala-Gly-Gln-D-Arg-NH2
Frog
-
-
marimastat
-
i.e. BB-2516
mercaptophenylalanyl derivatives
Frog
-
-
-
N-2-methylphenylsulfonylureido-N-(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
-
N-2-methylphenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
-
N-2-methylphenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
-
N-2-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
-
N-2-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
-
N-4-chlorophenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
-
N-4-chlorophenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
-
N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine
-
-
N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
-
N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine
-
-
N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
-
N-4-fluorophenylsulfonylureido-N-(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
-
N-4-fluorophenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
-
N-4-fluorophenylsulfonylureido-N-[(10,11,dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine
-
-
N-4-fluorophenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
-
N-4-fluorophenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
-
N-4-fluorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
-
N-4-fluorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine
-
-
N-4-fluorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
-
N-4-methylphenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
-
N-4-methylphenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
-
N-4-methylphenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
-
N-4-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
-
N-4-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
-
N-Hydroxy-3-[(2-nitro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(3-nitro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-iodo-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-methoxy-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-(2,4,6-trimethyl-benzenesulfonyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-(2-nitro-phenylsulfanyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-(3-trifluoromethyl-benzenesulfonyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-(4-nitro-phenylsulfanyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-(nonachlorobutane-1-sulfonyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-(quinoline-8-sulfonyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-(toluene-4-sulfonyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-pentafluorobenzenesulfonyl-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-phenylmethanesulfonyl-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-trichloromethanesulfonyl-amino]-propionamide
-
-
N-Hydroxy-3-[(4-nitro-benzyl)-trifluoromethanesulfonyl-amino]-propionamide
-
-
N-hydroxy-3-[(4-nitro-benzyl)-[3-(3-o-tolylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
N-hydroxy-3-[(4-nitro-benzyl)-[3-(3-p-tolylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
N-hydroxy-3-[(4-nitro-benzyl)-[3-(3-phenylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
N-hydroxy-3-[(4-nitro-benzyl)-[4-(3-o-tolylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
N-hydroxy-3-[(4-nitro-benzyl)-[4-(3-p-tolylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
N-hydroxy-3-[(4-nitro-benzyl)-[4-(3-phenylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
N-Hydroxy-3-[(naphthalene-1-sulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
N-Hydroxy-3-[(naphthalene-2-sulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
N-Hydroxy-3-[1-(4-nitro-benzyl)-3-o-tolylsulfonyl-ureido]-propionamide
-
-
N-Hydroxy-3-[1-(4-nitro-benzyl)-3-p-tolylsulfonyl-ureido]-propionamide
-
-
N-Hydroxy-3-[1-(4-nitro-benzyl)-3-phenylsulfonyl-ureido]-propionamide
-
-
N-Hydroxy-3-[dimethylsulfamoyl-(4-nitro-benzyl)-amino]-propionamide
-
-
N-Hydroxy-3-[methanesulfonyl-(4-nitro-benzyl)-amino]-propionamide
-
-
N-phenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
-
N-phenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
-
N-phenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
-
naphthoyl-Gly-PSI[POOHCH2]-Leu-Trp-NHBzl
-
pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
PAI-1
-
functions as an upstream regulator of a MMP-1-initiated collagenolytic phenotype, it blocks conversion of MMP-1 to its active form. Neutralization of endogenous PAI-1 with function blocking antibodies accelerates both collagenolysis and activation of MMP-1
-
pedunculagin
potent inhibitory effect on MMP-1 and the increased type-I procollagen synthesis in ultraviolet B-induced human fibroblast
phthaloyl-Gly(P)-Ile-Trp-(R)NHCH-(Me)Ph
-
phosphonamidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
phthaloyl-Gly(P)-Ile-Trp-NHBzl
-
50 µM, 25°C, pH 7.4, Tris buffer, reversible inhibition, protects the enzyme partially from inactivation by ClCH2CO-(N-OH)Leu-Ala-Gly-NH2
phthaloyl-Gly-PSI[POOHNH]-Ile-Trp-(S)NHCH-(Me)Ph
-
phosphonamidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
TIMP-3
-
is induced by enamel matrix derivative
-
tissue inhibitor of matrix metalloproteinase-1
-
tissue inhibitor of matrix metalloproteinase-2
-
0.1 microM, inhibits both protease activity and migration in a 3-dimensional cross-linked collagen matrix
-
Tissue inhibitor of metalloproteinase-1
-
TIMP-1
-
tissue inhibitors of metalloproteinase-1
-
i.e. TIMP-1
-
trocade
-
i.e. RO-22-3555
[3-[(2-hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-phenyl]-carbamic acid tert-butyl ester
-
-
[4-[(2-hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-phenyl]-carbamic acid tert-butyl ester
-
-
[5-[(2-hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-2-methoxy-phenyl]-carbamic acid tert-butyl ester
-
-
1,10-phenanthroline
-
chelates the required Zn2+
Cys
-
-
EDTA
-
-
EDTA
complete inhibition at 20 mM
EDTA
complete inhibition at 20 mM
TIMP-1
-
-
-
TIMP-1
-
specific MMP-1 inhibitor. Inhibition of p38 signaling by SB203580 increases TIMP-1 secretion, as well as infection with Mycobacterium tuberculosis, overview
-
TIMP-1
-
determination in cell culture medium
-
TIMP-1
-
no apparent regulation of the expression of TIMP-1 by either tumor necrosis factor or enamel matrix derivative
-
TIMP-1
-
TIMP-1 from brain is upregulated in in the infarcted tissue compared to healthy control areas, overview
-
TIMP-1
-
expression profile of MMPs/TIMP-1 after myocardial infarction, angiotensin II receptor blockade improves MMPs/TIMP-1 balance, overview
-
TIMP-2
-
-
-
TIMP-2
-
expression of TIMP-2 in addition to bisphosphonate treatment markedly reduces the number of osteolytic lesions in breast cancer and increases overall survival compared with treatment with bisphosphonates alone
-
TIMP-2
-
determination in cell culture medium
-
TIMP-2
-
highly produced in brain microvessels
-
tissue inhibitor of matrix metalloproteinase-1
-
is not influenced by substance P
-
tissue inhibitor of matrix metalloproteinase-1
-
-
-
additional information
-
no inhibition of MMP-1 by BAY 12-9566, quantitative structure-activity relationship analysis of some 5-amino-2-mercapto-1,3,4-thiadiazole based inhibitors, overview
-
additional information
-
human tissue factor pathway inhibitor-2 does not bind or inhibit activated matrix metalloproteinase-1
-
additional information
-
sulfur based inhibitors
-
additional information
-
the JNK inhibitor SP600125 inhibits rapamycin-induced MMP-1 gene transactivation and AP-1/DNA interactions, overview
-
additional information
-
panduratin A, isolated from Kaempferia pandurata, suppresses MMP-1 expression and enhances the expression of type-1 procollagen in UV-irradiated skin fibroblasts, overview
-
additional information
-
after hyperglycaemic treatment of keratinocytes, expression of matrix metalloproteinase-1 and alpha2beta1 integrin is significantly downregulated
-
additional information
-
not inhibitory: tissue inhibitor of matrix metalloproteinase-1
-
additional information
-
human fibroblast inhibitor effective against all vertebrate collagenases tested
-
additional information
platelet-derived growth factor (PDGF) treatment recruits BSMCs to injured sites and strengthens the effect of BMSCs on skin wound by suppressing activity of MMP-1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00002
(3-[(2-hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-phenyl)-carbamic acid tert-butyl ester
-
-
0.000162
2-[benzyl([[(2-methylphenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
-
pH 6.0, 37°C
0.000143
2-[benzyl([[(4-chlorophenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
-
pH 6.0, 37°C
0.000135
2-[benzyl([[(4-fluorophenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
-
pH 6.0, 37°C
0.00017
2-[benzyl([[(4-methylphenyl)sulfonyl]amino]carbonyl)amino]-N-hydroxyacetamide
-
pH 6.0, 37°C
0.000057
3-[((1R,4S)-7,7-Dimethyl-2-oxo-bicyclo[2.2.1]hept-1-ylmethanesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000027
3-[(2,4-Dinitro-phenylsulfanyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.00005
3-[(2,5-Dichloro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000031
3-[(2-Hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-benzoic acid
-
-
0.00005
3-[(3-Chloro-4-ethylamino-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.00003
3-[(3-Chloro-4-nitro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000024
3-[(4-Bromo-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000023
3-[(4-Chloro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000021
3-[(4-Fluoro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000089
3-[(5-Dimethylamino-naphthalene-1-sulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000077
3-[(Heptadecachlorooctane-1-sulfonyl)-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000018
3-[3-(2,4-Dichloro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
0.000036
3-[3-(3,4-Dichloro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
0.000026
3-[3-(3-Chloro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
0.000024
3-[3-(4-Chloro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
0.00004
3-[3-(4-Chloro-phenylsulfonyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
0.000021
3-[3-(4-Fluoro-phenyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
0.000047
3-[3-(4-Fluoro-phenylsulfonyl)-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
0.000032
3-[3-Benzoyl-1-(4-nitro-benzyl)-ureido]-N-hydroxy-propionamide
-
-
0.000025
3-[Benzenesulfonyl-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000057
3-[[3-[3-(4-chloro-phenylsulfonyl)-ureido]-benzenesulfonyl]-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000055
3-[[3-[3-(4-fluoro-phenylsulfonyl)-ureido]-benzenesulfonyl]-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000056
3-[[4-[3-(4-chloro-phenylsulfonyl)-ureido]-benzenesulfonyl]-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.000055
3-[[4-[3-(4-fluoro-phenylsulfonyl)-ureido]-benzenesulfonyl]-(4-nitro-benzyl)-amino]-N-hydroxy-propionamide
-
-
0.00003
4-[(2-Hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-benzoic acid
-
-
0.002
C3H7-POOH-Ile-Trp-NHMe
-
phosphonamidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
0.5
ClCH2CO-(N-OH)Leu-Ala-Gly-NH2
-
25°C, pH 7.4, Tris buffer
2.5
ClCH2CO-(N-OH)Phe-Ala-Ala-NH2
-
25°C, pH 7.4, Tris buffer
0.0000128 - 0.0000603
CT 1746
0.0105
epigallocatechin gallate
pH 7.5, 25°C
0.004
EtO-POOH-CH2-Leu-Trp-NHMe
-
pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
0.12
EtO-POOH-Ile-Ala-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
0.5
EtO-POOH-Ile-Ala-Gly-Gln-Arg-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt, weak inhibition
0.27
EtO-POOH-Ile-Ala-Gly-Glu-Arg(NO2)-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt, weak inhibition
0.4
EtO-POOH-Ile-Ala-Gly-Glu-Arg-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt, weak inhibition
0.045
EtO-POOH-Ile-Leu-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
0.012
EtO-POOH-Ile-Trp-NHMe
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
0.002
EtO-POOH-Ile-Tyr(OBzl)-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
0.02
EtO-POOH-Ile-Tyr-Gly
-
phosphoramidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine, substrate Ac-Pro-Leu-Gly-SCH(iBu)CO-Leu-Leu-GlyOEt
0.00135
fisetin
pH 7.5, 40°C
0.3
hexyl-POOH-O-Leu-Trp-NHMe
-
pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
0.000039
N-2-methylphenylsulfonylureido-N-(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
pH 6.0, 37°C
0.000036
N-2-methylphenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
pH 6.0, 37°C
0.000038
N-2-methylphenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37°C
0.000029
N-2-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37°C
0.000015
N-2-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37°C
0.000024
N-4-chlorophenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
pH 6.0, 37°C
0.000024
N-4-chlorophenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37°C
0.00019
N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine
-
pH 6.0, 37°C
0.00002
N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37°C
0.00023
N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine
-
pH 6.0, 37°C
0.000014
N-4-chlorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37°C
0.000025
N-4-fluorophenylsulfonylureido-N-(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
pH 6.0, 37°C
0.000021
N-4-fluorophenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
pH 6.0, 37°C
0.0002
N-4-fluorophenylsulfonylureido-N-[(10,11,dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine
-
pH 6.0, 37°C
0.000021
N-4-fluorophenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37°C
0.000013
N-4-fluorophenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37°C
0.000017
N-4-fluorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37°C
0.00018
N-4-fluorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine
-
pH 6.0, 37°C
0.000011
N-4-fluorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37°C
0.000032
N-4-methylphenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
pH 6.0, 37°C
0.00003
N-4-methylphenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37°C
0.000018
N-4-methylphenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37°C
0.000024
N-4-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine hydroxamate
-
pH 6.0, 37°C
0.000015
N-4-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37°C
0.000043
N-Hydroxy-3-[(2-nitro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
0.00005
N-Hydroxy-3-[(3-nitro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
0.000032
N-Hydroxy-3-[(4-iodo-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
0.000023
N-Hydroxy-3-[(4-methoxy-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
0.00005
N-Hydroxy-3-[(4-nitro-benzenesulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
0.000035
N-Hydroxy-3-[(4-nitro-benzyl)-(2,4,6-trimethyl-benzenesulfonyl)-amino]-propionamide
-
-
0.000028
N-Hydroxy-3-[(4-nitro-benzyl)-(2-nitro-phenylsulfanyl)-amino]-propionamide
-
-
0.000006
N-Hydroxy-3-[(4-nitro-benzyl)-(3-trifluoromethyl-benzenesulfonyl)-amino]-propionamide
-
-
0.000024
N-Hydroxy-3-[(4-nitro-benzyl)-(4-nitro-phenylsulfanyl)-amino]-propionamide
-
-
0.000069
N-Hydroxy-3-[(4-nitro-benzyl)-(nonachlorobutane-1-sulfonyl)-amino]-propionamide
-
-
0.000055
N-Hydroxy-3-[(4-nitro-benzyl)-(quinoline-8-sulfonyl)-amino]-propionamide
-
-
0.00003
N-Hydroxy-3-[(4-nitro-benzyl)-(toluene-4-sulfonyl)-amino]-propionamide
-
-
0.000002
N-Hydroxy-3-[(4-nitro-benzyl)-pentafluorobenzenesulfonyl-amino]-propionamide
-
-
0.000027
N-Hydroxy-3-[(4-nitro-benzyl)-phenylmethanesulfonyl-amino]-propionamide
-
-
0.000023
N-Hydroxy-3-[(4-nitro-benzyl)-trichloromethanesulfonyl-amino]-propionamide
-
-
0.000022
N-Hydroxy-3-[(4-nitro-benzyl)-trifluoromethanesulfonyl-amino]-propionamide
-
-
0.000055
N-hydroxy-3-[(4-nitro-benzyl)-[3-(3-o-tolylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
0.00005
N-hydroxy-3-[(4-nitro-benzyl)-[3-(3-p-tolylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
0.000062
N-hydroxy-3-[(4-nitro-benzyl)-[3-(3-phenylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
0.00007
N-hydroxy-3-[(4-nitro-benzyl)-[4-(3-o-tolylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
0.000057
N-hydroxy-3-[(4-nitro-benzyl)-[4-(3-p-tolylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
0.000069
N-hydroxy-3-[(4-nitro-benzyl)-[4-(3-phenylsulfonyl-ureido)-benzenesulfonyl]-amino]-propionamide
-
-
0.000082
N-Hydroxy-3-[(naphthalene-1-sulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
0.000065
N-Hydroxy-3-[(naphthalene-2-sulfonyl)-(4-nitro-benzyl)-amino]-propionamide
-
-
0.000069
N-Hydroxy-3-[1-(4-nitro-benzyl)-3-o-tolylsulfonyl-ureido]-propionamide
-
-
0.000042
N-Hydroxy-3-[1-(4-nitro-benzyl)-3-p-tolylsulfonyl-ureido]-propionamide
-
-
0.000052
N-Hydroxy-3-[1-(4-nitro-benzyl)-3-phenylsulfonyl-ureido]-propionamide
-
-
0.000038
N-Hydroxy-3-[dimethylsulfamoyl-(4-nitro-benzyl)-amino]-propionamide
-
-
0.000087
N-Hydroxy-3-[methanesulfonyl-(4-nitro-benzyl)-amino]-propionamide
-
-
0.000025
N-phenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine hydroxamate
-
pH 6.0, 37°C
0.000015
N-phenylsulfonylureido-N-[(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37°C
0.000013
N-phenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine hydroxamate
-
pH 6.0, 37°C
0.002
phthaloyl-Gly-PSI[POOHNH]-Ile-Trp-(S)NHCH-(Me)Ph
-
phosphonamidate inhibitor, pH 6.5, 25 °C, 50 mM HEPES buffer, 10 mM CaCl2, 1 mM 4,4'-dithiodipyridine
0.00149
quercetin
pH 7.5, 40°C
0.0000108 - 0.0001893
Ro31-9790
0.00005
[4-[(2-hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-phenyl]-carbamic acid tert-butyl ester
-
-
0.000024
[5-[(2-hydroxycarbamoyl-ethyl)-(4-nitro-benzyl)-sulfamoyl]-2-methoxy-phenyl]-carbamic acid tert-butyl ester
-
-
additional information
additional information
-
0.0000128
CT 1746
-
exon 5 mutant enzyme
0.0000603
CT 1746
-
wild-type enzyme
0.0000108
Ro31-9790
-
wild-type enzyme
0.0001893
Ro31-9790
-
exon 5 mutant enzyme
additional information
additional information
-
Ki-values above 250 nM are determined for N-4-fluorophenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine, N-4-chlorophenylsulfonylureido-N-(5H-dibenzo[a,d]cyclohepten-5-yl)-glycine, N-phenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine, N-4-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine, N-4-fluorophenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine, N-4-methylphenylsulfonylureido-N-[(5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine, N-4-fluorophenylsulfonylureido-N-(10,11,dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)-glycine, N-4-chlorophenylsulfonylureido-N-(10,11,dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)-glycine, N-4-methylphenylsulfonylureido-N-[(10,11,dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)methylen]-glycine, N-4-fluorophenylsulfonylureido-N-[(10,11,dihydro-5H-dibenzo[a,d]cyclohepten-5-yl)ethylene]-glycine
-
additional information
additional information
-
inhibition kinetics using diverse variants of 5-amino-2-mercapto-1,3,4-thiadiazoles, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
MMP-1 is upregulated by TGF-beta, EGF and IL-1beta
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
cell line JJ, increased MMP1 expression in chondrosarcoma, mechanism, overview
brenda
-
mucosa, immunohistochemic analysis of MMP-1 and TIMP-1 levels, overview. Overall plasma levels of MMP-1 and TIMP-1 in ulcerative colitis patients are significantly higher than those of the control group
brenda
-
acceleration of matrix metalloproteinase-1 production by oxidized low-sensity lipoprotein and 4-hydroxynonenal
brenda
-
-
brenda
-
primary
brenda
-
MMP-1 is expressed by migrating enterocytes bordering intestinal ulcers. In the fetal gut model, MMP-1 expression by migrating enterocytes is detected
brenda
-
-
brenda
-
-
brenda
-
primary epithelial ovarian tumor cell
brenda
-
MMP-14 is expressed and active in cultured ES2 cells. ES2 cells also exhibit MMP-dependent invasion of and proliferation within three-dimensional collagen gels
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
immortalized human keratinocyte cells
brenda
-
MMP-10 and MMP-1 are up-regulated in HaCaT II-4 cells
brenda
-
the MMP-1 levels are altered in the left ventricle and serum in case of hypertrophy through hyperthyroid conditions with 3,5,3'-triiodo-L-thyroine or dexamethasone application, tissue distribution, overview
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
glycine-extended gastrin renders colon cancer cells more invasive by increasing MMP-I expression via the putative glycine-extended gastrin receptor
brenda
-
primary, monocyte-derived
brenda
-
high MMP-1 level
brenda
-
-
brenda
-
Muller glia cell line
brenda
-
saphenous vein smooth muscle
brenda
-
-
brenda
-
-
brenda
-
UM1 and UM2 are oral tongue squamous cell carcinoma cell lines
brenda
-
ovarian clear cell carcinoma cell
brenda
-
-
brenda
-
-
brenda
-
follicular expression of MMP-1 increases following the gonadotropin surge. Abundance of MMP-1 mRNA increases at 6, 12, and 48 h post-gonadotropin releasing hormone injection. MMP-1 is localized to granulosal and thecal layers of preovulatory follicles. MMP-1 is increased in bovine preovulatory follicles following the gonadotropin surge
brenda
-
enzyme expression is significantly stronger in the epithelium than in the stroma
brenda
-
brenda
-
the mean salivary MMP-1 concentration in patients with chronic periodontitis is significantly higher before and after treatment with aprotinin, as compared to healthy subjects
brenda
-
-
brenda
-
disruption of caveolae by addition of methyl-beta-cyclodextrin results in a dramatic decline in both motility and invasion abilities of cells with concomitant increase in secreted MMP-2 expression and expression levels of MMP-1 and MMP-9
brenda
-
disruption of caveolae by addition of methyl-beta-cyclodextrin results in a dramatic decline in both motility and invasion abilities of cells with concomitant increase in secreted MMP-2 expression and expression levels of MMP-1 and MMP-9
brenda
-
SCL-1 cell. MMP-1 is upregulated 4 h after UVA and 16 h after UVB irradiation of tumor cells. Incubation of cells with the MEK1/2 inhibitor U0126 or the p38 inhibitor SB202190 abolishes the UVA and UVB mediated induction of MMP-1
brenda
-
a human chondrosarcoma cell line
brenda
-
rheumatoid
brenda
-
-
brenda
-
fibroblast-like, from rheumatoid arthritis patients
brenda
-
-
brenda
-
from Achilles tendon, immunohistochemic analysis of MMP-1, overview
brenda
-
leg ulcer tissue from patients with chronic venous insufficiency
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
-
brenda
-
in the center of granulomas
brenda
-
MMP-1 is upregulated in the infarcted tissue compared to healthy control areas
brenda
-
-
brenda
recombinant enzyme
brenda
-
purified MMP-1 from synovial fibroblasts
brenda
-
recombinant MMP-1
brenda
-
of interleukin-1-treated dermal fibroblasts
brenda
-
of rheumatoid synovial cells stimulated with rabbit macrophage-conditioned medium
brenda
-
-
95818, 95824, 95829, 95833, 95834, 655414, 656898, 683988, 699874, 708511, 708788, 709025, 709482, 717074 brenda
-
brenda
-
-
brenda
-
brenda
-
fibroblasts
brenda
-
dermal
brenda
dermal fibroblast
brenda
-
gingival
brenda
-
overexpression of phospholipid-hydroperoxide glutathione peroxidase in human dermal fibroblasts abrogates UVA irradiation-induced expression of interstitial collagenase/matrix metalloproteinase-1 by suppression of phosphatidylcholine hydroperoxide-mediated NFkappaB activation and interleukin-6 release
brenda
-
primary cultured corneal and tenon's fibroblast
brenda
-
production of MMP-1 by keloid fibroblasts is 6fold greater than that of normal dermal fibroblasts. The production of MMP-1 is decreased by addition of TGF-beta1 to cultured keloid fibroblasts, while it is increased when anti-TGF-beta1 antibody is added to the culture
brenda
-
dermal, quantitative MMP-1 expression analysis by RT-PCR
brenda
-
from lung
brenda
-
healthy dermal fibroblasts and cultured Xeroderma pigmentosum-C fibroblasts, increased MMP1 expression in cultured XP-C fibroblasts results from MMP1 mRNA accumulation and enhanced transcriptional activity of the MMP1 gene promoter, overview
brenda
-
NHDFs and NB1RGBs
brenda
-
primary lung fibroblast cell lines
brenda
-
dermal, primary
brenda
-
gingival, gingival fibroblasts produce MMP-1 in response to inflammatory cytokines, such as TNF and interleukin-1
brenda
-
synovial fibroblast
brenda
-
expression of MMP-1 is markedly increased by both onion extract and quercetin in vitro in human skin fibroblasts
brenda
primary human neonatal dermal fibroblasts
brenda
-
-
brenda
-
expression of MMP-1 is markedly increased by both onion extract and quercetin in vivo in hairless mice
brenda
-
-
brenda
-
brenda
-
fibroblasts
brenda
-
-
brenda
-
connective tissue
brenda
-
-
brenda
-
after hyperglycaemic treatment, expression of matrix metalloproteinase-1 and alpha2beta1 integrin is significantly downregulated
brenda
-
epidermal, primary, from foreskin
brenda
-
-
brenda
-
alveolar mucosa expression from HIV1+ smokers with early emphysema is significantly higher than in HIV1- smokers with early emphysema. Among the HIV- groups, compared with HIV1- healthy nonsmokers, smoking do not increase aqlveolar mucosa MMP-1 gene expression in HIV1- healthy smokers and HIV1- smokers with early emphysema, independent of whether emphysema is present or not. HIV1+ individuals with early emphysema have significantly increased expression of MMP-1 compared with all 3 groups of HIV1- individuals, including those with early emphysema
brenda
-
-
brenda
-
treatment of with 30 mM of 15-deoxy-DELTA12,14-prostaglandin J2 increases the expression of heme oxygenase-1, which precedes the induction of matrix metalloproteinases. The 15-deoxy-DELTA12,14-prostaglandin J2-induced upregulation of MMP-1 is abrogated by the heme oxygenase-1 inhibitor zinc protoporphyrin IX as well as introduction of heme oxygenase-1 short interfering RNA. Heme oxygenase-1 inducers, such as cobalt protoporphyrin IX and hemin, upregulate the expression of MMP-1. Overexpression of heme oxygenase-1 in the MCF-7 cells causes the induction of MMP-1 expression. Treatment with the heme oxygenase-1 inhibitor zinc protoporphyrin IX abolishes the migrative phenotype of 15-deoxy-DELTA12,14-prostaglandin J2-treated MCF-7 cells
brenda
-
-
brenda
-
treatment of with 30 mM of 15-deoxy-DELTA12,14-prostaglandin J2 increases the expression of heme oxygenase-1, which precedes the induction of matrix metalloproteinases. The 15-deoxy-DELTA12,14-prostaglandin J2-induced upregulation of MMP-1 is abrogated by the heme oxygenase-1 inhibitor zinc protoporphyrin IX as well as introduction of heme oxygenase-1 short interfering RNA. Heme oxygenase-1 inducers, such as cobalt protoporphyrin IX and hemin, upregulate the expression of MMP-1
brenda
-
VMM5 cells, VMM12cells and VMM39. Constitutive overexpression of collagenase 1 is mediated by the ERK pathway in invasive melanoma cells
brenda
-
of invasive melanomas
brenda
of bone marrow
brenda
-
of bone marrow
-
brenda
-
-
brenda
-
primary
brenda
-
-
brenda
-
expression profile of MMPs/TIMP-1 after myocardial infarction, angiotensin II receptor blockade improves MMPs/TIMP-1 balance, overview
brenda
-
collagen-induced arthritis hind paw sections as a model of human rheumatoid arthritis
brenda
-
collagen-induced arthritis hind paw sections as a model of human rheumatoid arthritis
-
brenda
-
immunohistochemic analysis of MMP-1 and TIMP-1 levels, overview. Overall plasma levels of MMP-1 and TIMP-1 in ulcerative colitis patients are significantly higher than those of the control group
brenda
-
no differences in MMP-1 in the plasma of hypertensive versus normotensive subjects
brenda
-
-
brenda
-
MMP-1 is progressively decreased from prostate intraepithelial neoplasia to prostate carcinoma
brenda
-
-
brenda
-
-
95823, 95824, 95825, 95829, 95832, 683221, 683451, 683988, 708425, 708788, 709482, 709591, 717678 brenda
-
brenda
-
from the lateral thoracic area of a 230 day fetal calf
brenda
-
cell culture
brenda
-
all-trans retinoic acid suppresses matrix metalloproteinase activity in diabetic skin
brenda
-
from mammary plastic surgery, MMP1 expression is increased in Xeroderma pigmentosum, a rare, recessively inherited genetic disease characterized by skin cancer proneness and premature aging in photoexposed area, overview
brenda
-
cell culture
brenda
-
-
brenda
-
-
brenda
-
brenda
-
cell culture
brenda
-
-
-
brenda
Frog
-
-
brenda
Frog
-
backskin
brenda
-
tail
brenda
-
presence of high glucose levels and interferon gamma in culture medium have a synergistic effect on the expression of matrix metalloproteinases MMP-1, MMP-9 and interleukin-1beta. High glucose also enhances interferon gamma-induced priming effect on lipopolysaccharide-stimulated MMP-1 secretion. High glucose and interferon gamma exert the synergistic effect on MMP-1 expression by enhancing STAT1 phosphorylation and STAT1 transcriptional activity
brenda
-
mononuclear phagocytes
brenda
-
-
brenda
-
MMP-1 is upregulated by EGF
brenda
additional information
-
MMP-1 expression analysis in gingival tissue, overview
brenda
additional information
-
MMP-1 is downregulated 4fold during trophoblast differentiation, reduced MMP-1 expression in pre-eclampsia and fetal growth restriction
brenda
additional information
-
overexpression of both ADAMTS1 and MMP-1 together increases osteolytic bone metastases, while overexpression of ADAMTS or MMP-1 alone has no effect
brenda
additional information
-
selective cell-dependent MMP secretion
brenda
additional information
-
MMP-1A is strongly expressed in tumor and arthritis specimens, expression patterns of MMP-1A in a variety of healthy, cancerous and arthritic murine tissues, overview
brenda
additional information
-
MMP-1A is strongly expressed in tumor and arthritis specimens, expression patterns of MMP-1A in a variety of healthy, cancerous and arthritic murine tissues, overview
-
brenda
additional information
detection of collagen deposition and MMP-1 secretion in rat-1 fibroblasts
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
malfunction
-
hsa-miR-222 regulates UM1 cancer cell invasion, at least in part, by indirectly regulating MMP1 expression through targeting superoxide dismutase SOD2 mRNA, overview
malfunction
-
hypoxia and specifically HIF-1a increase CXCR4 and MMP1 expression in JJ cell line and chondrosarcoma invasion in vitro
malfunction
-
inflammatory tissue destruction is central to pathology in cerebral tuberculosis with microglial-derived matrix metalloproteinases playing a key role in driving such damage
malfunction
-
MMP-1 is downregulated 4fold during trophoblast differentiation, reduced MMP-1 expression in pre-eclampsia and fetal growth restriction
malfunction
-
MMP-1 is involved in photoaging of the skin
malfunction
-
MMP-1A is strongly expressed in tumor and arthritis specimens
malfunction
-
periodontal disease is characterized by increased expression and activity of matrix metalloproteinases and insufficient expression/activity of their inhibitors, tissue inhibitors of matrix metalloproteinases, TIMPs. This altered MMP-TIMP balance results in progressive destruction of gingival and periodontal extracellular matrix
malfunction
the catalytically domain of MMP-1 (MMP-1 CAT) alone does not cleave collagen
malfunction
-
MMP-1A is strongly expressed in tumor and arthritis specimens
-
metabolism
-
altering the binding of at least two transcription factors, c-Jun and SP1, proteasome inhibition results in increased production of MMP-1 and decreases synthesis of type I collagen in human dermal fibroblasts. Differential effects of proteasome inhibition and TGF-beta on MMP-1 and MMP-2, overview
metabolism
-
effects of baicalin on the total protein amount and collagen I mRNA expression in periodontal ligament cells, and the regulatory effects on MMP-1/TIMP-1 expression, overview
metabolism
-
interleukin-6 and high glucose synergistically upregulate MMP-1 expression by U-937 cell mononuclear phagocytes via ERK1/2 and JNK pathways and c-Jun, MMP-1 regulation, overview
metabolism
-
matrix metalloproteinase-1 is regulated in tuberculosis by a p38 MAPK-dependent, p-aminosalicylic acid-sensitive signaling cascade. The p38 MAPK pathway regulates the divergence between MMPs and TIMP-1, overview
metabolism
astragaloside IV controls collagen reduction in photoaging skin by improving transforming growth factor-beta/Smad signaling suppression and inhibiting matrix metalloproteinase-1. Transforming growth factor beta type II protein and COL1 mRNA decreased but MMP-1 and Smad7 levels increased in the photoaging model group, which is reversed by topical application of AST. AST prevents collagen reduction from UV irradiation in photoaging skin
metabolism
matrix metalloproteinase 1 and collagens play a key role in platelet-derived growth factor (PDGF) and stromal cell-derived factor-1 (SDF-1) promotion of the skin wound repairing effect of bone mesenchymal stem cells. Bone marrow mesenchymal stem cells (BMSCs) are applied to treatment of skin wounds. PDGF treatment recruits BSMCs to injured sites and strengthens the effect of BMSCs on skin wound by suppressing activity of MMP-1. SDF-1 treatment increases the treating effect of BMSCs on skin injury through the deposition of collagen I and collagen III. Phenotypes, overview
metabolism
methotrexate (MTX) significantly reduces collagen type I production in different strains of fibroblasts derived from neonatal, adult, and hypertrophic scar tissues, while under the same experimental conditions, it increases the expression of MMP-1. Possible involvement of MTX-induced extracellular signal-regulated kinase 1/2 (ERK1/2) pathway in MMP-1 production. Activation of ERK1/2 pathway plays an important role in MTX-induced MMP-1 expression in primary human dermal fibroblasts
metabolism
the expression profiles of multiple and possibly redundant matrix-remodeling proteases (e.g., collagenases) differ strongly in health, disease, and development. Matrix metalloproteinases MMP-1 and MMP-13 cause distinct extracellular matrix (ECM) degradation, bringing about significantly distinct cellular phenotypes
metabolism
the expression profiles of multiple and possibly redundant matrix-remodeling proteases (e.g., collagenases) differ strongly in health, disease, and development. Matrix metalloproteinases MMP-1 and MMP-13 cause distinct extracellular matrix (ECM) degradation, bringing about significantly distinct cellular phenotypes
metabolism
-
matrix metalloproteinase 1 and collagens play a key role in platelet-derived growth factor (PDGF) and stromal cell-derived factor-1 (SDF-1) promotion of the skin wound repairing effect of bone mesenchymal stem cells. Bone marrow mesenchymal stem cells (BMSCs) are applied to treatment of skin wounds. PDGF treatment recruits BSMCs to injured sites and strengthens the effect of BMSCs on skin wound by suppressing activity of MMP-1. SDF-1 treatment increases the treating effect of BMSCs on skin injury through the deposition of collagen I and collagen III. Phenotypes, overview
-
physiological function
-
both plasma and mucosal levels of MMP-1 and TIMP-1 are independently correlated with ulcerative colitis, overview
physiological function
-
increased expression of MMPs by toll-like receptor activation may be involved in infection-associated inflammation, cell migration and tissue remodelling in human skin
physiological function
-
lithium-induced MMP-1 may participate in the reinforcement of endothelial cell senescence revealing a novel mechanism for lithium-induced tissue remodeling
physiological function
-
lithium-induced MMP-1 may participate in the reinforcement of endothelial cell senescence revealing a novel mechanism for lithium-induced tissue remodeling
physiological function
-
matrix metalloproteinase-1 degrades the extracellular matrix and is implicated in tuberculosis-driven tissue destruction, signaling pathways regulating macrophage MMP-1 in human pulmonary tuberculosis, overview
physiological function
-
matrix metalloproteinases and the tissue inhibitors of MMPs, TIMPs, play a pivotal role in matrix remodeling following myocardial infarction, the MMPs/TIMP-1 balance is perturbed after myocardial infarction. Oral valsartan, but not PD123319 limits infarct size, normalized MMPs/TIMP-1 balance and restores FN level
physiological function
-
matrix metalloproteinases play a pivotal role in tissue remodeling and destruction in inflammation-associated diseases such as cardiovascular disease and periodontal disease
physiological function
-
MMP-1 is a zinc-dependent endopeptidase capable of degrading all components of the extracellular matrix
physiological function
-
MMP-1 is implicated in the degradation of human skin matrix proteins such as collagen and other components of extracellular matrix
physiological function
-
MMP-1 is increased in inflammatory conditions leading to destruction of extracellular matrix
physiological function
-
MMP-1 is involved in in inflammatory atherosclerotic lesions and is known to be implicated in the vascular remodeling events preceding plaque rupture, the most common cause of acute myocardial infarction
physiological function
-
MMP-1 is involved in spontaneous resorption of disc herniation after sciatica, overview. MMP-3 appears to play a greater role than MMP-1 in disc herniation resorption
physiological function
-
MMP-1 or interstitial collagenase unwinds native type I collagen and initiate its degradation
physiological function
-
MMP-1 promotes osteoclastic bone resorption and bone metastases, the breast cancer cell produced MMP-1 is involved in the activation of the epidermal growth factor ligands that activate NF-kappaB ligand RANKL, via its central osteoclastogenic pathway receptor activator, to promote breast cancer osteolysis, molecular mechanism, overview
physiological function
-
proteasome inhibition, e.g. by inhibitor bortezomib, in vitro decreases type I collagen and enhances MMP-1 production by human fibroblasts, thus favoring an antifibrotic fibroblast phenotype. These effects are dominant over the pro-fibrotic phenotype induced by transforming growth factor-beta
physiological function
-
role for MMP-1 in the TGF-beta- and EGF-stimulated collagen remodeling process
physiological function
-
throughout the process of invading and remodelling spiral arteries, extracellular matrix must be broken down and matrix metalloproteinases are major participants in this disintegration
physiological function
-
transfection of a plasmid expression of MMP-1 into myocard after infarction increases myocyte shortening and reduces Na+-Ca2+ exchange current, it decreases myocardial fibrosis and improves cardiac remodeling and function
physiological function
-
MT1-MMP is identified as the dominant and direct-acting protease responsible for the type I collagenolytic activity mediated by both mouse and human pulmonary fibroblasts. MT1-MMP is shown to be essential for pulmonary fibroblast migration within three-dimensional (3-D) hydrogels of cross-linked type I collagen that recapitulate ECM barriers encountered in the in vivo environment
physiological function
-
MT1-MMP is identified as the dominant and direct-acting protease responsible for the type I collagenolytic activity mediated by both mouse and human pulmonary fibroblasts. MT1-MMP is shown to be essential for pulmonary fibroblast migration within three-dimensional (3-D) hydrogels of cross-linked type I collagen that recapitulate ECM barriers encountered in the in vivo environment
physiological function
MMP-1 is one of the key regulators of the overall quantity of type I procollagen deposited by fibroblasts during scar formation. It increases collagen degradation in the extracellular matrix (ECM)
physiological function
the protease drives morphological, biochemical, and viscoelastic changes in the extracellular matrix (ECM) leading to unique ECM-cell crosstalk, complexity and selectivity of collagenase-associated degradation mechanisms during tissue remodeling. Matrix metalloproteinases MMP-1 and MMP-13 cause distinct extracellular matrix (ECM) degradation, bringing about significantly distinct cellular phenotypes. Specific influences of the highly abundant collagenases on fibroblast-ECM crosstalk, overview
physiological function
the protease drives morphological, biochemical, and viscoelastic changes in the extracellular matrix (ECM) leading to unique ECM-cell crosstalk, complexity and selectivity of collagenase-associated degradation mechanisms during tissue remodeling. Matrix metalloproteinases MMP-1 and MMP-13 cause distinct extracellular matrix (ECM) degradation, bringing about significantly distinct cellular phenotypes. Specific influences of the highly abundant collagenases on fibroblast-ECM crosstalk, overview
additional information
-
c-Jun is a key subunit of AP-1 known to be essential for MMP-1 transcription
additional information
genetic variants of a common functional polymorphism in the matrix metalloproteinase-1 gene promoter do not account for the itchy skin phenotype in epidermolysis bullosa
additional information
-
Rac1 signaling results in accumulation of type I collagen due to decreased collagenase activity, overview
additional information
ability of MMP-1 to unwind triple-helical collagen, collagenolytic matrix metalloproteinase structure-function relationships, molecular dynamics studies, overview. Conformational selection mechanism for collagenolysis with full-length MMPs. Dynamic crosscorrelation analysis of MMP-1 with THP, modelling. Molecular dynamics simulations are utilized to dock MMP-1 with the cleavage site region in type III collagen
additional information
although collagenolytic matrix metalloproteinases (MMPs) possess common domain organizations, there are subtle differences in their processing of collagenous triple-helical substrates
additional information
detection of collagen deposition and MMP-1 secretion in rat-1 fibroblasts, macrorheological properties and morphologies of natural and MMP-degraded ECMs
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DELTA243-340
-
about 10% increase in turnover number and 9% increase in Km-value compared to wild-type enzyme with fTHP-3 as substrate
DELTA243-450
-
the KM-value for the alpa1(I)772-786 triple-helical peptide is 3.3fold higher than that of the wild-type enzyme, the turnover number for this substrate is 2.5fold higher
E200A
catalytically inactive, but correctly folded mutant enzyme. MMP-1(Glu200Ala) has an intact HPX domain. The mutant can orient and help unwind the collagen triple helix, while the catalytic MMP-1 domain (MMP-1 CAT) cleaves the triple helix
L338A/H339A
site-directed mutagenesis, the mutant shows an increased collagenase activity, the MMP-1 L338A/H339A mutant corresponds to the appearance of a unique anticorrelated motion and decreased correlated motions
R183Q/W184W/T185T/N186K/N187D/F188T/R189T/E190G/Y191T
-
mutation reduces collagenolytic activity about 10fold
V94G
constitutively active MMP-1 mutant. Expression of MMP-1 V94G in young skin in organ culture causes fragmentation and ultrastructural alterations of collagen fibrils similar to those observed in aged human skin in vivo. Expression of MMP-1 V94G in dermal fibroblasts cultured in three-dimensional collagen lattices causes substantial collagen fragmentation, which is markedly reduced by MMP-1 siRNA-mediated knockdown or MMP inhibitor MMI270. Fibroblasts cultured in MMP-1 V94G-fragmented collagen lattices display many alterations observed in fibroblasts in aged human skin, including reduced cytoplasmic area, disassembled actin cytoskeleton, impaired TGF-beta pathway, and reduced collagen production
Y191T
-
mutation reduces collagenolytic and gelatinolytic activity about 5fold
additional information
-
although increased MMP-1 levels are usually associated with angiogenesis in enabled proliferative endothelial cells, the exogenous addition of activated MMP-1 on lithium-arrested endothelial cells increases the number of endothelial cells positive for the senescent-associated-beta-galactosidase marker. Conversely, downregulation of MMP-1 expression by small interfering RNAs blunts the lithium-dependent increase in senescent-associated-beta-galactosidase positive cells. Lithium-induced MMP-1 expression is mediated neither by GSK3beta inhibition nor beta-catenin stabilization, lithium-dependent cell cycle arrest and the cell senescent phenotype in aortic endothelial cells are not triggered by inhibition of the inositol phosphate cycle. Induction molecular mechanism, overview
additional information
-
construction of a chimeric enzyme, the exon 5 chimera, consisting primarily of MMP-1, with the region coded for by exon 5 replaced with the equivalent region of MMP-3, a noncollagenolytic MMP. Unlike MMP-3, the exon 5 chimera is capable of cleaving type I collagen, but the activity is only 2.2% of the trypsin-activated MMP-1. The kinetics for exon 5 chimera cleavage of two synthetic substrates display an MMP-3 phenotype, however, cleavage of gelatin is slightly impaired as compared to the parent enzymes. The KI-values for the exon 5 chimera complexed with synthetic inhibitors and N-terminal TIMP-2 show a more MMP-3-like behaviour. The exon 5 mutant shows a 2.9fold in the ratio of turnover number to Km-value with (7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Leu-(3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2
additional information
-
introduction of various lengths of MMP-1 segments into MMP-3, i.e. stromelysin 1, starting from the C-terminal end. MMP-3/MMP-1 chimeras and variants are overexpressed in Escherichia coli, folded from inclusion bodies and isolated as zymogens. The nine residues 183RWTNNFREY191 located between the fifth beta-strand and the second alpha-helix in the catalytic domain of MMP-1 are critical for the expression of collagenolytic activity
additional information
-
MMP-1 enzyme inhibition and downregulation by short hairpin RNA, shRNA, reducing collagenase activity and angiogenesis of melanoma cells, but has no effect on primary tumor growth, xenograft modeling
additional information
-
acid sphingomyelinase-deficient human fibroblasts fail to phosphorylate extracellular signal-regulated kinase, ERK, or upregulate MMP-1 mRNA and protein expression upon stimulation with interleukin-1 beta, overview. Transfection of acid sphingomyelinase restores MMP-1 production, while inhibition of acid sphingomyelinase with imipramine completely abrogates MMP-1 induction
additional information
-
development of a piezoelectric immunosensor for matrix metalloproteinase-1 detection based on multilayered ultra-thin films composed by precursor layers of cationic poly(dimethyldiallylammonium) chloride and anionic poly(styrenesulfonate) with bound monolayer of antibodies, Layer by Layer self assembly technique, evaluation, overview
additional information
-
disruption of the proximal AP-1-binding site in the promoter of MMP-1 severely impair MMP-1 transcription in response to bortezomib
additional information
identification of a common functional polymorphism in the matrix metalloproteinase-1 gene promoter, 1G or 2G at nucleotide -1607, in individuals with epidermolysis bullosa pruriginosa compared with non-itchy dominant dystrophic epidermolysis bullosa, recessive dystrophic epidermolysis bullosa and healthy controls, overview. Genetic variants of a common functional polymorphism in the matrix metalloproteinase-1 gene promoter do not account for the itchy skin phenotype, overview
additional information
-
overexpression of both ADAMTS1 and MMP-1 together increases osteolytic bone metastases, while overexpression of ADAMTS or MMP-1 alone has no effect
additional information
-
transfection of oral tongue squamous cell carcinoma cells with microRNA candidates, including hsa-miR-222, reduces the expression of MMP1 and SOD2 in the cells, direct targeting of hsa-miR-222 to specific sequences located in the 3'-untranslated regions of both MMP1 and SOD2, overview
additional information
incorporation of peptoid residues into collagen model triple-helical peptides and examination of MMP activities toward the peptomeric chimeras
additional information
-
generation of specific recombinant human monoclonal antibody SP3, which is specific to the murine MMP-1 catalytic domain
additional information
-
generation of specific recombinant human monoclonal antibody SP3, which is specific to the murine MMP-1 catalytic domain
-
additional information
-
transfection of rat myocard with a plasmid encoding MMP-1, DNA release and MMP1 expression, effects on myocard remodeling, overview. MMP-1 expression increases myocyte shortening and reduces Na+-Ca2+ exchange current, it decreases myocardial fibrosis and improves cardiac remodeling and function
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
activation of toll-like receptors TLR2, TLR3 or TLR5 increased the expression of MMP-1. MMP-1 and MMP-9 in human epidermal keratinocytes are induced by Pam3CSK4, Poly(I:C) and flagellin, which are ligands for TLR2, TLR3 and TLR5, respectively, overview. The induction of MMP-1 by the receptor ligands is inhibited by pretreatment with BAY11-7082, a NF-kappaB inhibitor, or SP600125, a JNK inhibitor. p38 MAPK activation negatively regulates MMP-1 induction by TLR2 or TLR5 activation, but not by TLR3 activation
-
bortezomib specifically increases the steady-state mRNA levels of MMP-1 and enhances the binding of c-Jun to the promoter of MMP-1. Disruption of the proximal AP-1-binding site in the promoter of MMP-1 severely impairs MMP-1 transcription in response to bortezomib. By altering the binding of at least two transcription factors, c-Jun and SP1, proteasome inhibition results in increased production of MMP-1 and decreases synthesis of type I collagen in human dermal fibroblasts
-
both the MMP-1 and TIMP-1 mRNA expression level are dramatically downregulated by baicalin
-
curcumin at the concentration of 2.5-5 mg/ml specifically downregulates MMP-1 mRNA in BT-483 and MDA-MB-231 breast cancer cell lines. Cell growth and proliferation is inhibited in presence of curcumin, overview
-
curcumin, a potent inhibitor for AP-1, or simvastatin inhibit the expression of MMP-1. Suppression of c-Jun expression by RNA interference significantly inhibits MMP-1 expression
-
dexamethasone suppression of MMP-1 gene expression
-
dexamethasone, and less potent also interleukin-1Ra and TNF, decrease levels of pro-MMP-1
-
enhanced collagen degradation, in case of epithelial-to-mesenchymal transition stimulated by transforming growth factor-beta as well as epidermal growth factor receptor, is coupled to a significant increase in matrix metalloproteinase MMP-1 expression and is involved a proteolytic axis composed of plasmin, MMP-10, ec 3.4.24.22, and MMP-1
-
expression of MMP-1 in cartilages and synovial tissues is suppressed by the treatment of curcumin and indomethacin. Production of MMP-1 is inhibited by curcumin in tumor necrosis factor-alpha-stimulated rheumatoid arthritis fibroblast-like synoviocytes and chondrocytes in a dose-dependent manner putatively through the inhibition of PKCdelta and the JNK/c-Jun signaling pathway, overview
-
expression of MMP-1 is markedly increased by both onion extract and quercetin in vitro in human skin fibroblasts
-
expression of MMP-1 is markedly increased by both onion extract and quercetin in vivo in hairless mice
-
fucoidan treatment significantly inhibits the expression of MMP-1
-
hypoxia and specifically HIF-1a increase CXCR4, its ligand SDF1, and MMP1 expressions in JJ cell line and chondrosarcoma invasion in vitro, which can be inhibited by siRNA directed at HIF-1a or CXCR4, the CXCR4 inhibitor AMD3100, as well as with ERK inhibitor U0126 and ERK siRNA. Hypoxia increases MMP1 mRNA expression 9fold which is further increased to 23fold by SDF1 stimulation
-
ibuprofen upregulates expressions of matrix metalloproteinase-1, as well as MMP-8, MMP-9, and MMP-13, without affecting expressions of types I and III collagen in tendon cells
-
increased MMP1 expression in JJ cell line can be inhibited by siRNA directed at HIF-1a or CXCR4, the CXCR4 inhibitor AMD3100, as well as with ERK inhibitor U0126 and ERK siRNA
-
induction of MMP-1 by UV-A irradiation treatment of cultured human dermal fibroblasts
-
inhibition of MMP-1 expression by extracts of Kaempferia pandurata, overview
-
inhibititory effects of potent antioxidant astaxanthin on the MMP-1 induction by UV-A irradiation, overview
-
interleukin-6, high glucose, and lipopolysaccharide act in concert and synergistically upregulate MMP-1 expression by U-937 mononuclear phagocytes via ERK1/2 and JNK pathways and c-Jun, mechanism, overview. c-Jun is a key subunit of AP-1 known to be essential for MMP-1 transcription
-
lithium specifically induces a rapid and pronounced up-regulation of MMP-1 at the mRNA and protein levels, whereas the induction of two the other senescent cell markers plasminogen activator inhibitor-1 and interleukin-8 is either delayed or weak, respectively. Lithium affects MMP-1 expression mainly at the transcriptional level but neither the AP1/Ets regulatory sites nor the redox sensitive -1607/2G site in MMP-1 promoter are involved in lithium-dependent MMP-1 regulation
-
matrix metalloproteinase-1 expression is induced by interleukin-1beta requiring acid sphingomyelinase, overview
-
methotrexate (MTX) increases the expression of MMP-1 in primary human neonatal, adult, and hypertrophic scar fibroblasts by 1.5fold 72 h after treatment with 50-500 ng/ml MTX
MMP-1 expression and secretion is induced by infection with Mycobacterium tuberculosis by 57.8%, the specific inhibitor TIMP-1 expression is also induced by 243.7%. The MMP-1 induction is specifically inhibited by 4-aminosalicyclic acid via inhibiting a p38 MAPK-prostaglandin signaling cascade, overview
-
MMP-1 expression is induced by UV-B irradiation, the induction is inhibited by extracts of Kaempferia pandurata, as are phosphorylation of MAP kinases ERK, JNK, and p38, overview
-
MMP-1 is 4.1fold induced by infection with Mycobacterium tuberculosis. Conditioned medium from Mycobacterium tuberculosis-infected human monocytes stimulates greater MMP-1 gene expression in human microglial cells than direct infection, overview. The induction is suppressed by dexamethasone. TNF-alpha and interleukin-1beta are necessary but not sufficient for upregulating MMP-1 secretion. NF-kappaB and AP-1 c-Jun/FosB heterodimers regulate induction of MMP-1 secretion by conditioned medium from Mycobacterium tuberculosis and are upregulated in granulomas from patients with cerebral tuberculosis. CoMTb upregulates MMP-1 gene expression and secretion in microglia
-
MMP-1 is downregulated 4fold during trophoblast differentiation, reduced MMP-1 expression in pre-eclampsia and fetal growth restriction
-
MMP-1 is induced in gingival fibroblasts in response to inflammatory cytokines, such as TNF and interleukin-1. TNF treatment of human gingival fibroblasts significantly induces the expression of MMP-1 severalfold, while enamel matrix derivative alone has no effect
-
MMP-1 is upregulated after stroke in brain in the infarcted tissue compared to healthy control areas, overview
-
phorbol 12-myristate 13-acetate and interleukin-1beta significantly stimulate the production of MMP-1 by periodontal ligament cells at both the transcriptional and the translational level
-
production of MMP-1 is inhibited by curcumin in collagen-induced arthritis hind paw sections in a dose-dependent manner putatively through the inhibition of PKCdelta and the JNK/c-Jun signaling pathway, overview
Rac1 inhibitor NSC23766 suppresses MMP1 in dermal fibroblasts, and half-lives of type I collagen protein are increased
-
recombinantly overexpressed RhoB enhances migration and MMP1 expression of prostate cancer DU145 cells, overview
-
SB203580 and PD98059 suppress MMP-1 secretion
-
TNF-alpha and IL-1beta stimulate production of MMPs through the activation of mitogen-activated protein kinases, NF-kappaB and AP-1
-
UV-B irradiation induces MMP-1 expression and secretion. Inhibitory effects of Costaria costata fucoidan on UVB-induced MMP-1 promoter, mRNA, and protein expression in vitro by 41.8% at 10 ng/ml, 57.7% at 100 ng/ml, and 70% at 0.001 mg/ml compared to UV-B irradiation alone, overview
-
UVA and UVB irradiation of dermal fibroblasts in vitro or human skin in vivo induces MMP-1 expression. MMP-1 expression and secretion induced by UV-B irradiation is inhibited by trans-zeatin, a cytokinin from Zea mays, and by PD98059, an ERK inhibitor, by SP600125, a JNK inhibitor and by SB203580, a p38 MAPK inhibitor. trans-Zeatin also inhibits UVB-induced ERK, JNK, p38 MAPK and c-Jun phosphorylation
-
production of MMP-1 is inhibited by curcumin in collagen-induced arthritis hind paw sections in a dose-dependent manner putatively through the inhibition of PKCdelta and the JNK/c-Jun signaling pathway, overview
-
production of MMP-1 is inhibited by curcumin in collagen-induced arthritis hind paw sections in a dose-dependent manner putatively through the inhibition of PKCdelta and the JNK/c-Jun signaling pathway, overview
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.