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(7-methoxycoumarin-4-yl)acetyl-Pro-cyclohexylalanine-Gly-norvaline-His-Ala-Arg-NH2 + H2O
(7-methoxycoumarin-4-yl)acetyl-Pro-cyclohexylalanine-Gly + Nva-His-Ala-Arg-NH2
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-diaminipropionyl-Ala-Arg-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-diaminopropionyl-Ala-Arg-NH2 + H2O
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-DIAMIONOPROPIONYL-Ala-Arg-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-L-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-N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-[3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-Ala-Arg-NH2 + H2O
?
-
-
-
-
?
alpha1-proteinase inhibitor + H2O
?
-
-
-
-
?
bovine collagen I + H2O
?
cartilage aggrecan + H2O
?
-
-
-
?
Cartilage aggrecan + H2O
hydrolyzed cartilage aggrecan
-
cleavage at Glu373-Ala374 "aggrecanase" site in intraglobular domain
-
?
Dnp-Pro-Gln-Gly-Ile-Ala-Gly-Gln-(D)-Arg + H2O
?
-
-
-
-
?
epithelial cell-derived neutrophil activating peptide-78 + H2O
?
-
i.e. ENA-78, or CXCL5, a cytokine
-
-
?
estrogen receptor alpha + H2O
?
estrogen receptor beta + H2O
?
Fibrillar type I collagen + H2O
?
-
from human or guinea pig
-
-
?
Fibrillar type III collagen + H2O
?
-
-
-
-
?
guinea pig collagen type I + H2O
?
-
-
-
-
?
human collagen type I + H2O
?
-
-
-
-
?
human collagen type II + H2O
?
-
-
-
-
?
human collagen type III + H2O
?
-
-
-
-
?
interleukin-8 + H2O
?
-
-
-
-
?
macrophage inflammatory protein-1 (MIP-1) alpha + H2O
?
-
membrane-bound MMP-8 is a more potent MIP-1alpha-degrading enzyme than soluble MMP-8
-
-
?
Mca-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(Dnp)-NH2 + H2O
?
Mca-Lys-Pro-Leu-Gly + H2O
?
-
-
-
-
?
Mca-Lys-Pro-Leu-Gly-Leu-Dap(Dnp)-Ala-Arg-NH2 + H2O
?
Monomeric type I collagen + H2O
collagen type I fragment TCA + collagen type I fragment TCB
Monomeric type II collagen + H2O
collagen type II fragment TCA + collagen type II fragment TCB
Monomeric type III collagen + H2O
collagen type III fragment TCA + collagen type III fragmentTCB
TNF-alpha + H2O
?
-
MMP8 exhibits TNF-alpha-converting enzyme activity by cleaving the prodomain of TNF-alpha at residues A74-Q75 and A76-V77
-
?
type 1 collagen + H2O
?
-
degradation, production of 3/4(alphaA)-cleavage products
-
-
?
type III collagen + H2O
?
additional information
?
-
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-diaminopropionyl-Ala-Arg-NH2 + H2O
?
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-diaminopropionyl-Ala-Arg-NH2 + H2O
?
-
-
-
-
?
bovine collagen I + H2O
?
-
-
-
?
bovine collagen I + H2O
?
-
-
-
?
Collagen + H2O
?
-
-
-
-
?
Collagen + H2O
?
-
initiates degradation of native collagen
-
-
?
Collagen + H2O
?
-
type I and type II
-
-
?
Collagen + H2O
?
-
MMP-8 is the major collagenase in human dentin
-
-
?
Collagen + H2O
?
-
-
-
-
?
collagen type 1 + H2O
?
in dentin
-
-
?
collagen type 1 + H2O
?
demineralized dentine matrix (DDM) is collagen-rich
-
-
?
estrogen receptor alpha + H2O
?
-
-
-
-
?
estrogen receptor alpha + H2O
?
-
-
-
-
?
estrogen receptor beta + H2O
?
-
-
-
-
?
estrogen receptor beta + H2O
?
-
-
-
-
?
LIX + H2O
?
-
a murine ELR+ CXC chemokine
-
-
?
LIX + H2O
?
-
a murine ELR+ CXC chemokine, MMP-8 cleaves the 92-amino acid peptide LIX between Ser-Val at position 4-5 to generate a NH2-terminus at Val5 designated LIX (5-92), the binding site is located on the MMP-8 hemopexin C-domain
-
-
?
Mca-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(Dnp)-NH2 + H2O
?
-
-
-
?
Mca-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(Dnp)-NH2 + H2O
?
-
-
-
?
Mca-Lys-Pro-Leu-Gly-Leu-Dap(Dnp)-Ala-Arg-NH2 + H2O
?
-
-
-
?
Mca-Lys-Pro-Leu-Gly-Leu-Dap(Dnp)-Ala-Arg-NH2 + H2O
?
-
-
-
?
Monomeric type I collagen + H2O
collagen type I fragment TCA + collagen type I fragment TCB
-
from human
-
-
?
Monomeric type I collagen + H2O
collagen type I fragment TCA + collagen type I fragment TCB
-
from guinea pig
-
-
?
Monomeric type I collagen + H2O
collagen type I fragment TCA + collagen type I fragment TCB
-
best substrate, unlike EC 3.4.24.7 this enzyme cleaves type III collagen more slowly than type I
-
-
?
Monomeric type I collagen + H2O
collagen type I fragment TCA + collagen type I fragment TCB
-
catalyzes single cleavage in alpha-chain
-
-
?
Monomeric type II collagen + H2O
collagen type II fragment TCA + collagen type II fragment TCB
-
-
-
-
?
Monomeric type II collagen + H2O
collagen type II fragment TCA + collagen type II fragment TCB
-
-
three-quarter and one-quarter length fragments
?
Monomeric type III collagen + H2O
collagen type III fragment TCA + collagen type III fragmentTCB
-
-
-
-
?
Monomeric type III collagen + H2O
collagen type III fragment TCA + collagen type III fragmentTCB
-
unlike EC 3.4.24.7 this enzyme cleaves type III collagen more slowly than type I
three-quarter and one-quarter length fragments
?
Type I collagen + H2O
?
-
-
-
-
?
Type I collagen + H2O
?
-
mechanical strain preserves collagen fibrils in the presence of MMP-8
-
-
?
Type I collagen + H2O
?
-
-
-
-
?
type III collagen + H2O
?
-
-
-
-
?
type III collagen + H2O
?
-
mechanism of interaction and cleavage of human type III collagen by fibroblast MMP-8 using a panel of recombinant human type III collagens containing engineered sequences in the vicinity of the cleavage site around residue 1785, e.g. mutant FG-5015 I785P, overview
-
-
?
type III collagen + H2O
?
-
-
-
-
?
additional information
?
-
-
no hydrolysis of monomeric type IV or V collagen
-
-
?
additional information
?
-
-
expression of MMP-8 is positively associated with improved survival of the patients suffering squamous cell carcinoma of the tongue and the tendency is particularly prominent in females, MMP-8 has a protective, probably estrogen-related, role in mobile tongue carcinoma, overview
-
-
?
additional information
?
-
-
MMP-8 can degrade all the components of the extracellular matrix
-
-
?
additional information
?
-
-
MMP-8 is involved in abdominal aortic aneurysm rupture, overview
-
-
?
additional information
?
-
-
tobacco-related increase in MMP-8 levels may be involved in periodontal disease in tobacco smokers, MMP-8 is also involved in other tobacco-related inflammatory diseases such as vascular and pulmonary diseases
-
-
?
additional information
?
-
-
MP-8 is involved in the proteolytic cleavage of the tight junction protein occludin
-
-
?
additional information
?
-
development of a method for generating demineralized dentine matrix substrate (DDM), using EDTA or acetic acid, and maintaining MMP-8 bioactivity and no interference with later assays, overview
-
-
?
additional information
?
-
-
development of a method for generating demineralized dentine matrix substrate (DDM), using EDTA or acetic acid, and maintaining MMP-8 bioactivity and no interference with later assays, overview
-
-
?
additional information
?
-
-
expression of MMP-8 is positively associated with improved survival of the patients suffering squamous cell carcinoma of the tongue and the tendency is particularly prominent in females, MMP-8 has a protective, probably estrogen-related, role in mobile tongue carcinoma, overview
-
-
?
additional information
?
-
-
lipopolysaccharide responsiveness and neutrophil chemotaxis in vivo require polymorphonuclear MMP-8 activity, overview
-
-
?
additional information
?
-
-
no activity with the murine ELR+ CXC chemokines KC, MIP-2, and DCIP-1
-
-
?
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(1R)-[1-(4'-methoxybiphenyl-4-sulfonylamino)-2-methylpropyl]carboxylate
-
-
(1R)-[1-(4'-methoxybiphenyl-4-sulfonylamino)-2-methylpropyl]hydroxamate
-
-
(1R)-[1-(4'-methoxybiphenyl-4-sulfonylamino)-2-methylpropyl]phosphonate
-
binding structure at the S1' pocket, detailed mode of binding, overview
(1S)-[1-(4'-methoxybiphenyl-4-sulfonylamino)-2-methylpropyl]carboxylate
-
-
(1S)-[1-(4'-methoxybiphenyl-4-sulfonylamino)-2-methylpropyl]hydroxamate
-
-
(1S)-[1-(4'-methoxybiphenyl-4-sulfonylamino)-2-methylpropyl]phosphonate
-
binding structure at the S1' pocket, detailed mode of binding, overview
(2R,S)-HONH-Mal(Me/Bn)-1,2,9,10-tetrahydroisoquinolide
-
-
(2R,S)-HONH-Mal(Me/Bn)-alpha-naphthylamide
-
-
(2R,S)-HONH-Mal(Me/Bn)-NH-CH2CH2-Ph
-
-
(2R,S)-HONH-Mal(Me/Bn)-NH-CH2CH2CH2-Ph
-
-
(2R,S)-HONH-Mal(Me/Bn)-NH-CH2CH2CH2CH2-Ph
-
-
(2R,S)-HONH-Mal(Me/Bn)-NHBn
-
-
(2R,S)-HONH-Mal(Me/Bn)-NHBn-(p-COOH)
-
-
(2R,S)-HONH-Mal(Me/Bn)-NHPh
-
-
(2R,S)-HONH-Mal(Me/Bn)-Oet
-
-
(2R,S)-HONH-Mal(Me/i-Bu)-Oet
-
-
(2R,S)-HONH-Mal(NHAc/Bn)-NHBn
-
-
(2R,S)-HONH-Mal(OH/Bn)-NHBn
-
-
(2S,3R)-2-methyl-3-(2-methylpropyl)-1-(N-hydroxy)-4-(O-methyl)-L-tyrosine-N-methylamide
-
BB-16
(3R)-(+)-[2-(4-methoxybenzenesulfonyl)-1,2,3,4-tetrahydroisoquinoline-3-hydroxamate]
-
(3R)-1,2,3,4-tetrahydro-N-hydroxy-2-[(4-methoxyphenyl)sulfonyl]-3-isoquinolinecarboxamide
i.e. matrix metalloproteinase-8 Inhibitor I or M8I, administration of the MMP8 inhibitor immediately after reperfusion reduces brain damage
(3R)-N-hydroxy-2-(4-methoxyphenyl)sulfonyl-3,4-dihydro-1H-isoquinoline-3-carboxamide
-
(N-1(R)-carboxyethyl)-alpha-(S)-(4-phenyl-3-butynyl)glycyl-L-O-methyltyrosine, N-methylamide
-
SA751
(R)-2-(biphenyl-4-ylsulfonyl)-1,2,3,4-tetrahydroisoquinolin-3-carboxylic acid
-
(R)-[1-(4'-methoxybiphenyl-4-sulfonylamino)-2-methylpropyl] phosphonate
-
stereoselectivity, binding structure, molecular dynamic simulations of inhibitor bound to MMP-8, the 144-155 loop of the enzyme undergoes a drastic decrease of mobility once complexed with the enantiomer, overview
(S)-[1-(4'-methoxybiphenyl-4-sulfonylamino)-2-methylpropyl] phosphonate
-
stereoselectivity, binding structure, molecular dynamic simulations of inhibitor bound to MMP-8, the 144-155 loop of the enzyme undergoes a drastic decrease of mobility once complexed with the enantiomer, overview
2-((4'-morpholino-[1,1'-biphenyl]-4-yl) sulfonyl) benzoic acid
-
2-(arylsulfonyl)-1,2,3,4-tetrahydroisoquinoline-3-carboxylate
-
2-(arylsulfonyl)-1,2,3,4-tetrahydroisoquinoline-3-hydroxamate
-
batimastat
-
BB-94, peptidomimetic MMP inhibitor
benzyl 2-((4'-morpholino-[1,1'-biphenyl]-4-yl) sulfonyl) benzoate
-
benzyl 2-((4-bromophenyl) sulfonyl) benzoate
-
GM6001
-
an MMP inhibitor
HONH-iBM-L-Ala-Gly-NH2
-
-
HONH-iBM-L-Asn-NHBn(m-NH2)
-
-
HONH-iBM-NH-(CH2)7CH3
-
-
Ile-Pro-Glu-Asn-Phe-Phe-Gly
-
aggrecan as substrate
isovitexin
interacts with enzyme residues Val112, Ser218, Leu119, Glu118, Asn226, Ser225, Thr224, Asn184, Phe192, and Asp115, binding structure analysis, and modelling, overview
malonic acid hydroxamate
-
-
MMP-8 hemopexin C-domain
-
recombinantly expressed, in excess inhibits the processing of LIX cytokine by blocking the binding site, overview
-
N-hydroxy-2-((4'-morpholino-[1,1'-biphenyl]-4-yl) sulfonyl) benzamide
CAM12, the MMP-8 inhibitor CAM12 causes the same phenotype compared to MMP-8 knockout mice
N-hydroxy-2-(2-[[4-(4-methoxyphenoxy)phenyl]sulfonyl]phenyl)acetamide
-
-
N-hydroxy-N2-[(4'-methoxybiphenyl-4-yl)sulfonyl]-N2-(propan-2-yloxy)glycinamide
-
-
N-hydroxy-N2-[(4-phenoxyphenyl)sulfonyl]-N2-(propan-2-yloxy)glycinamide
-
-
N-hydroxy-N2-[(4-phenoxyphenyl)sulfonyl]valinamide
-
-
N-isobutyl-N-(4-methoxyphenylsulfonyl)glycyl hydroxamic acid
NNGH
N2-(biphenyl-4-ylsulfonyl)-N-hydroxy-N2-(propan-2-yloxy)glycinamide
-
-
N2-(biphenyl-4-ylsulfonyl)-N-hydroxyglycinamide
-
-
Thr-Glu-Gly-Glu-Ala-Arg-Gly
-
aggrecan as substrate
TIMP-1
-
TIMP-1 from brain is upregulated in in the infarcted tissue compared to healthy control areas, overview
-
TIMP-2
-
highly produced in brain microvessels
-
tissue inhibitor of matrix metalloproteinase-1
-
i.e. TIMP-1, inhibits MMP-8. Elevated levels of TIMP-1 in blood are associated with poor prognosis in many cancers. Genotyping and identification of different single nucleotide polymorphisms in male and female patients of head and neck squamous cell carcinoma
-
Tissue inhibitor of metalloproteinase-I
-
i.e. TIMP-I
-
vitexin
interacts with enzyme residues Leu193, Tyr219, Ala161, Asn218, His207, Glu198, Gly158, Pro217, His201, and Val194, binding structure analysis, and modelling, overview
MMP-8 inhibitor I
-
in the presence of specific MMP-8 I inhibitor formation of the occludin cleavage product is prevented
MMP-8 inhibitor I
-
modulation of 5-fluorouracil pharmacokinetic by irradiation is reversed by MMP-8 inhibitor
additional information
-
no inhibition by PMSF, pepstatin, N-ethylmaleimide, cystatin or E-64
-
additional information
-
resistant to inhibition by tissue inhibitor of metalloproteinase-1 and tissue inhibitor of metalloproteinase-2
-
additional information
-
inhibitor-induced conformational changes at the active site, structure-activity relationships, overview
-
additional information
Ficus deltoidea leaf extract inhibits matrix metalloproteinase-2, 8 and 9, molecular docking, molecular dynamics, molecular dynamic simulation analysis , overview. Computational docking analysis reveals that vitexin and isovitexin binds to the active site of the three tested MMPs
-
additional information
inhibitor syntheses, overview
-
additional information
-
inhibitor syntheses, overview
-
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malfunction
-
abrogation of MMP-8 activity by specific inhibitors as well as transfection with MMP-8 siRNA abolishes production of the cleavage fragment and occludin remained attached to the cell periphery
malfunction
-
MMP-8-/- mice with acute lung injury have greater increases in lung polymorphonuclear neutrophils (PMNs) and macrophage counts, measures of alveolar capillary barrier injury, lung elastance, and mortality than wild-type mice with acute lung injury
malfunction
intracerebroventricular microinjection of MMP8-specific shRNA lentivirus reduces the extent of ischemia-induced brain damage, as assessed by infarct volume, neurological score, microglial activation, and TNF-alpha expression. Administration of an MMP8 inhibitor (M8I) immediately after reperfusion reduced brain damage
malfunction
ischemia-reperfusion (I/R) injury leads to increased expression of intestinal and systemic MMP8. Inhibition of MMP8 prevents intestinal barrier dysfunction following I/R injury. MMP8-null mice have reduced intestinal permeability to FD-40 compared with wild-type mice. Wild-type mice treated with MMP8 inhibitor also have a significant reduction of intestinal neutrophil infiltration as compared with wild-type mice treated with vehicle. Claudin-3 expression is reduced after I/R injury, relative to the respective sham-treated animals, and this effect is ameliorated by either genetic ablation or pharmacologic inhibition of MMP8. Inhibition of MMP8 decreases neutrophil infiltration in the intestine and lung and prevents intestinal damage, myeloperoxidase activity is reduced, overview
malfunction
juvenile MMP8 null mice have greater mortality and higher bacterial burden than wild-type mice. Leukocyte counts and cytokine concentrations in the peritoneal fluid are increased in the MMP8 null mice relative to the wild-type mice. Peritoneal macrophages from MMP8 null mice have reduced phagocytic capacity compared to wild-type macrophages. There is no quantitative difference in NET formation, but fewer bacteria are adherent to NETs from MMP8 null animals
malfunction
-
ischemia-reperfusion (I/R) injury leads to increased expression of intestinal and systemic MMP8. Inhibition of MMP8 prevents intestinal barrier dysfunction following I/R injury. MMP8-null mice have reduced intestinal permeability to FD-40 compared with wild-type mice. Wild-type mice treated with MMP8 inhibitor also have a significant reduction of intestinal neutrophil infiltration as compared with wild-type mice treated with vehicle. Claudin-3 expression is reduced after I/R injury, relative to the respective sham-treated animals, and this effect is ameliorated by either genetic ablation or pharmacologic inhibition of MMP8. Inhibition of MMP8 decreases neutrophil infiltration in the intestine and lung and prevents intestinal damage, myeloperoxidase activity is reduced, overview
-
malfunction
-
juvenile MMP8 null mice have greater mortality and higher bacterial burden than wild-type mice. Leukocyte counts and cytokine concentrations in the peritoneal fluid are increased in the MMP8 null mice relative to the wild-type mice. Peritoneal macrophages from MMP8 null mice have reduced phagocytic capacity compared to wild-type macrophages. There is no quantitative difference in NET formation, but fewer bacteria are adherent to NETs from MMP8 null animals
-
physiological function
-
MMP-8 inactivates macrophage inflammatory protein-1alpha to reduce acute lung inflammation and injury in mice
physiological function
-
MMP-8 is involved in the proteolytic cleavage of the tight junction protein occludin, resulting in its disappearance from the cell periphery and cleavage to a lower-sized 50-kDa protein in infected human brain microvascular endothelial cells
physiological function
aortic rings isolated from MMP8 -/- apoE -/- mice have less endothelial cell sprouting, and endothelial cells in MMP8 -/- apoE -/- mice have a lower ability to migrate into Matrigel plugs and less capacity of proliferation and angiogenesis. MMP8 -/- apoE -/- and MMP8 +/+- apoE -/- mice fed a Western diet for 12 have small lesion size and less endothelial cells within atherosclerotic lesions
physiological function
knockdown of MMP-8 in human umbilical vein endothelial cells with MMP-8 shRNA lentivirus results in a decrease in in vitro capillary-like network formation, cell proliferation and migration, and impairs its capacity of in vivo angiogenesis. Less nuclear accumulation of beta-catenin and lower beta-catenin target gene expression levels are observed in the HuVECs expressing lower levels of endogenous MMP-8. MMP8 is expressed in microvessels within human atherosclerotic plaques and aneurysm. Knockdown of endogenous MMP-8 down-regulates platelet/endothelial cell adhesion molecule PECAM-1 expression by converting less angiotensin I to II, which is an inducer for PECAM-1 gene expression
physiological function
MMP-8 is upregulated in LPS-stimulated BV2 microglial cells and primary cultured microglia, and treatment with MMP-8 inhibitor or MMP-8 short hairpin RNA suppresses proinflammatory molecules, particularly TNF-alpha secretion. Treatment with MMP-8 inhibitor inhibits TNF-alpha-converting enzyme activity more efficiently than TAPI-0, a general TNF-alpha converting enzyme inhibitor. It inhibits MAPK phosphorylation, NF-kappaB/AP-1 activity, and reactive oxygen species production
physiological function
MMP-8 is upregulated in septic conditions, particularly in microglia. Administration of MMP-8 inhibitor or MMP-8 short hairpin RNA significantly inhibits microglial activation and expression/secretion of TNF-alpha in brain tissue, serum, and cerebrospinal fluid of lipopolysaccharid-induced septic mice
physiological function
matrix metalloproteinase-8 augments bacterial clearance in a juvenile sepsis model. Developmental age influences the role of MMP8 in sepsis, mechanism by which MMP8 influences outcomes in sepsis, analysis of local cytokine response in juvenile wild-type and MMP8 null mice with peritoneal sepsis, overview
physiological function
MMP-8 contributes to caries by degrading collagen
physiological function
MMP-8 is a collagen cleaving enzyme, produced by neutrophils and epithelial cells under inflammatory conditions, has been implicated in numerous tissue remodeling processes
physiological function
MMP-8 participates in cancer, arthritis, asthma, and failure of dental fillings
physiological function
neutrophil collagenase matrix metalloproteinase-8 (MMP8) belongs to the MMPs that have important roles in various inflammation-related disorders. MMP8 is a neuroinflammatory mediator in activated microglia by regulating TNF-alpha productivity. Pathogenetic role of MMP8
physiological function
role of matrix metalloproteinase-8 (MMP8) as a mediator of injury in intestinal ischemia and reperfusion. MMP8 is induced during intestinal injury
physiological function
role of salivary matrix metalloproteinase-8 (MMP-8) in chronic periodontitis diagnosis
physiological function
-
role of matrix metalloproteinase-8 (MMP8) as a mediator of injury in intestinal ischemia and reperfusion. MMP8 is induced during intestinal injury
-
physiological function
-
MMP-8 is a collagen cleaving enzyme, produced by neutrophils and epithelial cells under inflammatory conditions, has been implicated in numerous tissue remodeling processes
-
physiological function
-
matrix metalloproteinase-8 augments bacterial clearance in a juvenile sepsis model. Developmental age influences the role of MMP8 in sepsis, mechanism by which MMP8 influences outcomes in sepsis, analysis of local cytokine response in juvenile wild-type and MMP8 null mice with peritoneal sepsis, overview
-
additional information
MMP-8 differs from other MMPs in that it has an insertion that enlarges its active site
additional information
MMP-8 is critical for dexamethasone therapy in alkali-burned corneas under dry eye conditions. The anti-inflammatory effects of Dex are mediated through increased MMP-8 expression
additional information
-
MMP-8 is critical for dexamethasone therapy in alkali-burned corneas under dry eye conditions. The anti-inflammatory effects of Dex are mediated through increased MMP-8 expression
additional information
-
MMP-8 is critical for dexamethasone therapy in alkali-burned corneas under dry eye conditions. The anti-inflammatory effects of Dex are mediated through increased MMP-8 expression
-
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Hasty, K.A.; Jeffrey, J.J.; Hibbs, M.S.; Welgus, H.G.
The collagen substrate specificity of human neutrophil collagenase
J. Biol. Chem.
262
10048-10052
1987
Homo sapiens
brenda
Hasty, K.A.; Pourmotabbed, T.F.; Goldberg, G.I.; Thompson, J.P.; Spinella, D.G.; Stevens, R.M.; Mainardi, C.L.
Human neutrophil collagenase. A distinct gene product with homology to other matrix metalloproteinases
J. Biol. Chem.
265
11421-11424
1990
Homo sapiens
brenda
Knuper, S.; Krmer, S.; Reinke, H.; Tschesche, H.
Characterization and activation of procollagenase from human polymorphonuclear leucocytes. N-terminal sequence determination of the proenzyme and various proteolytically activated forms
Eur. J. Biochem.
189
295-300
1990
Homo sapiens
brenda
Fosang, A.J.; Last, K.; Neame, P.J.; Murphy, G.; Knuper, S.; Tschesche, H.; Hughes, C.E.; Caterson, B.; Hardingham, T.E.
Neutrophil collagenase (MMP-8) cleaves at the aggrecanase site E373-A374 in the interglobular domain of cartilage aggrecan
Biochem. J.
304
347-351
1994
Homo sapiens
brenda
Fasciglione, G.F.; Marini, S.; D'Alessio, S.; Politi, V.; Coletta, M.
pH- and temperature-dependence of functional modulation in metalloproteinases. A comparison between neutrophil collagenase and gelatinases A and B
Biophys. J.
79
2138-2149
2000
Homo sapiens
brenda
Betz, M.; Huxley, P.; Davies, S.J.; Mushtaq, Y.; Pieper, M.; Tschesche, H.; Bode, W.; Gomis-Ruth, F.X.
1.8-A crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate primed-side inhibitor with a distinct selectivity profile
Eur. J. Biochem.
247
356-363
1997
Homo sapiens
brenda
Arner, E.C.; Decicco, C.P.; Cherney, R.; Tortorella, M.D.
Cleavage of native cartilage aggrecan by neutrophil collagenase (MMP-8) is distinct from endogenous cleavage by aggrecanase
J. Biol. Chem.
272
9294-9299
1997
Homo sapiens
brenda
Marini, S.; Fasciglione, G.F.; de Sanctis, G.; D'Alessio, S.; Politi, V.; Coletta, M.
Cleavage of bovine collagen I by neutrophil collagenase MMP-8. Effect of pH on the catalytic properties as compared to synthetic substrates
J. Biol. Chem.
275
18657-18663
2000
Homo sapiens
brenda
Brandstetter, H.; Grams, F.; Glitz, D.; Lang, A.; Huber, R.; Bode, W.; Krell, H.W.; Engh, R.A.
The 1.8-A crystal structure of a matrix metalloproteinase 8-barbiturate inhibitor complex reveals a previously unobserved mechanism for collagenase substrate recognition
J. Biol. Chem.
276
17405-17412
2001
Homo sapiens
brenda
Gioia, M.; Fasciglione, G.F.; Marini, S.; D'Alessio, S.; De Sanctis, G.; Diekmann, O.; Pieper, M.; Politi, V.; Tschesche, H.; Coletta, M.
Modulation of the catalytic activity of neutrophil collagenase MMP-8 on bovine collagen I. Role of the activation cleavage and of the hemopexin-like domain
J. Biol. Chem.
277
23123-23130
2002
Homo sapiens
brenda
Graf von Roedern, E.; Brandstetter, H.; Engh, R.A.; Bode, W.; Grams, F.; Moroder, L.
Bis-substituted malonic acid hydroxamate derivatives as inhibitors of human neutrophil collagenase (MMP8)
J. Med. Chem.
41
3041-3047
1998
Homo sapiens
brenda
Matter, H.; Schwab, W.; Barbier, D.; Billen, G.; Haase, B.; Neises, B.; Schudok, M.; Thorwart, W.; Schreuder, H.; Brachvogel, V.; Lonze, P.; Weithmann, K.U.
Quantitative structure-activity relationship of human neutrophil collagenase (MMP-8) inhibitors using comparative molecular field analysis and X-ray structure analysis
J. Med. Chem.
42
1908-1920
1999
Homo sapiens (P22894), Homo sapiens
brenda
Gavuzzo, E.; Pochetti, G.; Mazza, F.; Gallina, C.; Gorini, B.; D'Alessio, S.; Pieper, M.; Tschesche, H.; Tucker, P.A.
Two crystal structures of human neutrophil collagenase, one complexed with a primed- and the other with an unprimed-side inhibitor: implications for drug design
J. Med. Chem.
43
3377-3385
2000
Homo sapiens (P22894), Homo sapiens
brenda
Brandstetter, H.; Engh, R.A.; Von Roedern, E.G.; Moroder, L.; Huber, R.; Bode, W.; Grams, F.
Structure of malonic acid-based inhibitors bound to human neutrophil collagenase. A new binding mode explains apparently anomalous data
Protein Sci.
7
1303-1309
1998
Homo sapiens
brenda
Wilson, W.R.; Schwalbe, E.C.; Jones, J.L.; Bell, P.R.; Thompson, M.M.
Matrix metalloproteinase 8 (neutrophil collagenase) in the pathogenesis of abdominal aortic aneurysm
Br. J. Surg.
92
828-833
2005
Homo sapiens
brenda
Khanna-Gupta, A.; Zibello, T.; Idone, V.; Sun, H.; Lekstrom-Himes, J.; Berliner, N.
Human neutrophil collagenase expression is C/EBP-dependent during myeloid development
Exp. Hematol.
33
42-52
2005
Homo sapiens
brenda
Fligiel, S.E.; Standiford, T.; Fligiel, H.M.; Tashkin, D.; Strieter, R.M.; Warner, R.L.; Johnson, K.J.; Varani, J.
Matrix metalloproteinases and matrix metalloproteinase inhibitors in acute lung injury
Hum. Pathol.
37
422-430
2006
Homo sapiens
brenda
Pelman, G.R.; Morrison, C.J.; Overall, C.M.
Pivotal molecular determinants of peptidic and collagen triple helicase activities reside in the S3 subsite of matrix metalloproteinase 8 (MMP-8): the role of hydrogen bonding potential of ASN188 and TYR189 and the connecting cis bond
J. Biol. Chem.
280
2370-2377
2005
Homo sapiens
brenda
Owen, C.A.; Hu, Z.; Lopez-Otin, C.; Shapiro, S.D.
Membrane-bound matrix metalloproteinase-8 on activated polymorphonuclear cells is a potent, tissue inhibitor of metalloproteinase-resistant collagenase and serpinase
J. Immunol.
172
7791-7803
2004
Homo sapiens, Mus musculus
brenda
Li, J.; Liao, E.Y.; Dai, R.C.; Wei, Q.Y.; Luo, X.H.
Effects of 17 beta-estradiol on the expression of interstitial collagenases-8 and -13 (MMP-8 and MMP-13) and tissue inhibitor of metalloproteinase-1 (TIMP-1) in ovariectomized rat osteoblastic cells
J. Mol. Histol.
35
723-731
2004
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
brenda
Sulkala, M.; Tervahartiala, T.; Sorsa, T.; Larmas, M.; Salo, T.; Tjaederhane, L.
Matrix metalloproteinase-8 (MMP-8) is the major collagenase in human dentin
Arch. Oral Biol.
52
121-127
2007
Homo sapiens
brenda
Tuomainen, A.M.; Nyyssoenen, K.; Laukkanen, J.A.; Tervahartiala, T.; Tuomainen, T.P.; Salonen, J.T.; Sorsa, T.; Pussinen, P.J.
Serum matrix metalloproteinase-8 concentrations are associated with cardiovascular outcome in men
Arterioscler. Thromb. Vasc. Biol.
27
2722-2728
2007
Homo sapiens
brenda
Liu, K.Z.; Hynes, A.; Man, A.; Alsagheer, A.; Singer, D.L.; Scott, D.A.
Increased local matrix metalloproteinase-8 expression in the periodontal connective tissues of smokers with periodontal disease
Biochim. Biophys. Acta
1762
775-780
2006
Homo sapiens
brenda
Korpi, J.T.; Kervinen, V.; Maeklin, H.; Vaeaenaenen, A.; Lahtinen, M.; Laeaerae, E.; Ristimaeki, A.; Thomas, G.; Ylipalosaari, M.; Astroem, P.; Lopez-Otin, C.; Sorsa, T.; Kantola, S.; Pirilae, E.; Salo, T.
Collagenase-2 (matrix metalloproteinase-8) plays a protective role in tongue cancer
Br. J. Cancer
98
766-775
2008
Homo sapiens, Mus musculus
brenda
Wilson, W.R.; Anderton, M.; Schwalbe, E.C.; Jones, J.L.; Furness, P.N.; Bell, P.R.; Thompson, M.M.
Matrix metalloproteinase-8 and -9 are increased at the site of abdominal aortic aneurysm rupture
Circulation
113
438-445
2006
Homo sapiens
brenda
Gutierrez-Fernandez, A.; Inada, M.; Balbin, M.; Fueyo, A.; Pitiot, A.S.; Astudillo, A.; Hirose, K.; Hirata, M.; Shapiro, S.D.; Noel, A.; Werb, Z.; Krane, S.M.; Lopez-Otin, C.; Puente, X.S.
Increased inflammation delays wound healing in mice deficient in collagenase-2 (MMP-8)
FASEB J.
21
2580-2591
2007
Mus musculus, Mus musculus C57/BL6J
brenda
Pochetti, G.; Gavuzzo, E.; Campestre, C.; Agamennone, M.; Tortorella, P.; Consalvi, V.; Gallina, C.; Hiller, O.; Tschesche, H.; Tucker, P.A.; Mazza, F.
Structural insight into the stereoselective inhibition of MMP-8 by enantiomeric sulfonamide phosphonates
J. Med. Chem.
49
923-931
2006
Homo sapiens
brenda
Aschi, M.; Besker, N.; Re, N.; Pochetti, G.; Coletti, C.; Gallina, C.; Mazza, F.
Stereoselectivity by enantiomeric inhibitors of matrix metalloproteinase-8: new insights from molecular dynamics simulations
J. Med. Chem.
50
211-218
2007
Homo sapiens
brenda
Tester, A.M.; Cox, J.H.; Connor, A.R.; Starr, A.E.; Dean, R.A.; Puente, X.S.; Lopez-Otin, C.; Overall, C.M.
LPS responsiveness and neutrophil chemotaxis in vivo require PMN MMP-8 activity
PLoS ONE
2
e312
2007
Mus musculus
brenda
Marcaccini, A.M.; Novaes, A.B.; Meschiari, C.A.; Souza, S.L.; Palioto, D.B.; Sorgi, C.A.; Faccioli, L.H.; Tanus-Santos, J.E.; Gerlach, R.F.
Circulating matrix metalloproteinase-8 (MMP-8) and MMP-9 are increased in chronic periodontal disease and decrease after non-surgical periodontal therapy
Clin. Chim. Acta
409
117-122
2009
Homo sapiens
brenda
Tsai, W.C.; Hsu, C.C.; Chang, H.N.; Lin, Y.C.; Lin, M.S.; Pang, J.H.
Ibuprofen upregulates expressions of matrix metalloproteinase-1, -8, -9, and -13 without affecting expressions of types I and III collagen in tendon cells
J. Orthop. Res.
28
487-491
2010
Rattus norvegicus
brenda
Cuadrado, E.; Rosell, A.; Penalba, A.; Slevin, M.; Alvarez-Sabin, J.; Ortega-Aznar, A.; Montaner, J.
Vascular MMP-9/TIMP-2 and neuronal MMP-10 up-regulation in human brain after stroke: a combined laser microdissection and protein array study
J. Proteome Res.
8
3191-3197
2009
Homo sapiens
brenda
Williams, K.E.; Olsen, D.R.
Matrix metalloproteinase-1 cleavage site recognition and binding in full-length human type III collagen
Matrix Biol.
28
373-379
2009
Homo sapiens
brenda
Pradhan-Palikhe, P.; Vesterinen, T.; Tarkkanen, J.; Leivo, I.; Sorsa, T.; Salo, T.; Mattila, P.S.
Plasma level of tissue inhibitor of matrix metalloproteinase-1 but not that of matrix metalloproteinase-8 predicts survival in head and neck squamous cell cancer
Oral Oncol.
46
514-518
2010
Homo sapiens
brenda
Mazzini, F.; Nuti, E.; Petri, A.; Rossello, A.
Immobilization of matrix metalloproteinase 8 (MMP-8) for online drug screening
J. Chromatogr. B
879
756-762
2011
Homo sapiens
brenda
Quintero, P.A.; Knolle, M.D.; Cala, L.F.; Zhuang, Y.; Owen, C.A.
Matrix metalloproteinase-8 inactivates macrophage inflammatory protein-1 alpha to reduce acute lung inflammation and injury in mice
J. Immunol.
184
1575-1588
2010
Mus musculus
brenda
Flynn, B.; Bhole, A.; Saeidi, N.; Liles, M.; Dimarzio, C.; Ruberti, J.
Mechanical strain stabilizes reconstituted collagen fibrils against enzymatic degradation by mammalian collagenase matrix metalloproteinase 8 (MMP-8)
PLoS ONE
5
e12337
2010
Homo sapiens
brenda
Hsieh, C.H.; Liu, C.Y.; Hsieh, Y.J.; Tai, H.C.; Wang, L.Y.; Tsai, T.H.; Chen, Y.J.
Matrix metalloproteinase-8 mediates the unfavorable systemic impact of local irradiation on pharmacokinetics of anti-cancer drug 5-Fluorouracil
PLoS ONE
6
e21000
2011
Rattus norvegicus
brenda
Schubert-Unkmeir, A.; Konrad, C.; Slanina, H.; Czapek, F.; Hebling, S.; Frosch, M.
Neisseria meningitidis induces brain microvascular endothelial cell detachment from the matrix and cleavage of occludin: A role for MMP-8
PLoS Pathog.
6
1-15
2010
Homo sapiens
brenda
Fang, C.; Wen, G.; Zhang, L.; Lin, L.; Moore, A.; Wu, S.; Ye, S.; Xiao, Q.
An important role of matrix metalloproteinase-8 in angiogenesis in vitro and in vivo
Cardiovasc. Res.
99
146-155
2013
Mus musculus (O70138), Homo sapiens (P22894), Homo sapiens
brenda
Thirkettle, S.; Decock, J.; Arnold, H.; Pennington, C.; Jaworski, D.; Edwards, D.
Matrix metalloproteinase 8 (collagenase 2) induces the expression of interleukins 6 and 8 in breast cancer cells
J. Biol. Chem.
288
16282-16294
2013
Homo sapiens (P22894), Homo sapiens
brenda
Lee, E.; Han, J.; Woo, M.; Shin, J.; Park, E.; Kang, J.; Moon, P.; Baek, M.; Son, W.; Ko, Y.; Choi, J.; Kim, H.
Matrix metalloproteinase-8 plays a pivotal role in neuroinflammation by modulating TNF-alpha activation
J. Immunol.
193
2384-2393
2014
Mus musculus (O70138), Mus musculus, Homo sapiens (P22894)
brenda
Hedenbjoerk-Lager, A.; Hamberg, K.; Paeaekkoenen, V.; Tjaederhane, L.; Ericson, D.
Collagen degradation and preservation of MMP-8 activity in human dentine matrix after demineralization
Arch. Oral Biol.
68
66-72
2016
Homo sapiens (P22894), Homo sapiens
brenda
Daly, M.C.; Atkinson, S.J.; Varisco, B.M.; Klingbeil, L.; Hake, P.; Lahni, P.; Piraino, G.; Wu, D.; Hogan, S.P.; Zingarelli, B.; Wong, H.R.
Role of matrix metalloproteinase-8 as a mediator of injury in intestinal ischemia and reperfusion
FASEB J.
30
3453-3460
2016
Mus musculus (O70138), Mus musculus C57BL/6 (O70138)
brenda
Gupta, N.; Gupta, N.; Gupta, A.; Khan, S.; Bansal, N.
Role of salivary matrix metalloproteinase-8 (MMP-8) in chronic periodontitis diagnosis
Front. Med.
9
72-76
2015
Homo sapiens (P22894), Homo sapiens
brenda
Bian, F.; Wang, C.; Tukler-Henriksson, J.; Pflugfelder, S.C.; Camodeca, C.; Nuti, E.; Rossello, A.; Li, D.Q.; de Paiva, C.S.
MMP-8 is critical for dexamethasone therapy in alkali-burned corneas under dry eye conditions
J. Cell. Physiol.
231
2506-2516
2016
Mus musculus (O70138), Mus musculus, Mus musculus C57BL/6 (O70138)
brenda
Atkinson, S.J.; Varisco, B.M.; Sandquist, M.; Daly, M.N.; Klingbeil, L.; Kuethe, J.W.; Midura, E.F.; Harmon, K.; Opaka, A.; Lahni, P.; Piraino, G.; Hake, P.; Zingarelli, B.; Mortenson, J.E.; Wynn, J.L.; Wong, H.R.
Matrix metalloproteinase-8 augments bacterial clearance in a juvenile sepsis model
Mol. Med.
22
455-463
2016
Mus musculus (O70138), Mus musculus, Mus musculus C57BL/6 (O70138)
brenda
Han, J.; Lee, E.; Moon, E.; Ryu, J.; Choi, J.; Kim, H.
Matrix metalloproteinase-8 is a novel pathogenetic factor in focal cerebral ischemia
Mol. Neurobiol.
53
231-239
2016
Mus musculus (O70138)
brenda
Abu Bakar, A.R.; Ripen, A.M.; Merican, A.F.; Mohamad, S.B.
Enzymatic inhibitory activity of Ficus deltoidea leaf extract on matrix metalloproteinase-2, 8 and 9
Nat. Prod. Res.
33
1765-1768
2019
Homo sapiens (P22894)
brenda
McNiff, M.L.; Haynes, E.P.; Dixit, N.; Gao, F.P.; Laurence, J.S.
Thioredoxin fusion construct enables high-yield production of soluble, active matrix metalloproteinase-8 (MMP-8) in Escherichia coli
Protein Expr. Purif.
122
64-71
2016
Homo sapiens (P22894)
brenda