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Information on EC 3.4.24.35 - gelatinase B and Organism(s) Rattus norvegicus and UniProt Accession P50282
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3.4.24.35 gelatinase BSpecify your search results
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- 3.4.24.35
- mmp-2
- metalloproteinases
-
zymography
- metastasis
- timp-1
- endothelial
- necrosis
- angiogenesis
- tnf
- artery
- fibrosis
- neutrophil
- chemokine
- infarct
- plaque
- monocyte
- vessel
- pulmonary
- myocardial
- cerebral
- mapks
- stroke
- erk
-
transwell
-
basement
- aortic
-
invasiveness
- plasminogen
-
blood-brain
- matrigel
- bcl-2
- nf-kappab
- airway
- upa
- osteoclast
- cox-2
- fibronectin
- aneurysm
-
c-reactive
- mt1-mmp
- e-cadherin
- coronary
- tnf-alpha
-
angiogenic
- atherosclerotic
-
anti-metastatic
-
tartrate-resistant
-
urokinase-type
- drug development
- diagnostics
- elastin
- rankl
- medicine
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
mmp-9, matrix metalloproteinase-9, matrix metalloproteinase 9, gelatinase b, matrix metallopeptidase 9, matrix metalloprotease-9, mmp 9, 92-kda gelatinase, 92 kda gelatinase, 92-kda type iv collagenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
92 kDa gelatinase
-
-
-
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92-kDa Gelatinase
-
-
-
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92-kDa Type IV collagenase
-
-
-
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95 kDa type IV collagenase/gelatinase
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-
-
-
Collagenase IV
-
-
-
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Collagenase type IV
-
-
-
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Gelatinase MMP 9
-
-
-
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GELB
-
-
-
-
Macrophage gelatinase
-
-
-
-
Matrix metalloproteinase 9
matrix metalloproteinase-9
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MMP 9
-
-
-
-
MMP-9
-
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Type IV collagen metalloproteinase
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-
-
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Type IV collagenase
-
-
-
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Type IV collagenase/gelatinase
-
-
-
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Type V collagenase
-
-
-
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Matrix metalloproteinase 9
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
-
-
CAS REGISTRY NUMBER
COMMENTARY
146480-36-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Gelatin + H2O
?
-
-
683051, 683412, 683427, 683874, 700147, 701422, 708304, 709595, 709614, 709646, 709682, 709920, 709948, 710106, 710575, 710585, 710695
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-
?
additional information
?
-
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independent of its proteolytic function, enzyme has a biphasic effect on smooth muscle cell-mediated collagen gel contraction
-
-
?
additional information
?
-
-
astrocyte-released MMP-9 is involved in interleukin-1beta induced neurotoxicity, probably via urokinase plasminogen activator, overview
-
-
?
additional information
?
-
-
inhibition of MMP-9 prevents neutrophilic inflammation in ventilator-induced lung injury, VILI, and pulmonary hemorrhage, overview
-
-
?
additional information
?
-
-
myogenic reactivity, inhibited in small renal arteries isolated from nonpregnant rats treated with recombinant human relaxin, is completely restored by incubation with MMP-9, MMP-9 rather than MMP-2 plays a central role in the vasodilatory effect of short-term relaxin administration, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
independent of its proteolytic function, enzyme has a biphasic effect on smooth muscle cell-mediated collagen gel contraction
-
-
?
additional information
?
-
-
astrocyte-released MMP-9 is involved in interleukin-1beta induced neurotoxicity, probably via urokinase plasminogen activator, overview
-
-
?
additional information
?
-
-
inhibition of MMP-9 prevents neutrophilic inflammation in ventilator-induced lung injury, VILI, and pulmonary hemorrhage, overview
-
-
?
additional information
?
-
-
myogenic reactivity, inhibited in small renal arteries isolated from nonpregnant rats treated with recombinant human relaxin, is completely restored by incubation with MMP-9, MMP-9 rather than MMP-2 plays a central role in the vasodilatory effect of short-term relaxin administration, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adiponectin
-
adiponectin can markedly suppress protein expression and activity of MMP9 in brain, induced by 1 h ischemia followed by 23 h reperfusion
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SB-3CT
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MMP9-specific inhibitor, MMP9 activity is reduced with SB-3CT resulting in reduced brain injury
additional information
-
no inhibition by amiloride or plasminogen activator/plasmin inhibitor D-Phe-Pro-Arg-chloromethylketone dihydrochloride
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
chymase
-
chymase converts promatrix metalloproteinase-9 to matrix metalloproteinase-9
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fibronectin
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fibronectin enhances, in a PKC-dependent manner, the net activity of MMP-9, but not its expression
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lipopolysaccharide
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lipopolysaccharide challenge (0.001 mg/ml) increases the protein level of MMP-9 and induces the activity of MMP-9 in H9c2 cardiomyoblasts through ERK1/2 signaling pathway
4-aminophenylmercuric acetate
-
1 mM 4-aminophenylmercuric acetate-mediated activation of MMP-9 provokes autocatalytic cleavage of recombinant MMP-9
4-aminophenylmercuric acetate
-
after treatment with 4-aminophenylmercuric acetate, affinity-purified W-256 cell gelatinase is converted to a final processed form of 66000 Da
additional information
an increase in hypoxia-inducible factor-1alpha is followed by a significant increase in MMP-9 gene expression at 4 h at 24 h post-traumatic brain injury, traumatic brain injury increases MMP-9 mRNA and protein levels in cortical and hippocampal regions early at 4 h post-traumatic brain injury, persisting for 5 days
-
additional information
-
implantation of 9L glioma cells into brain increases the expression of MMP-9, overview
-
additional information
-
MMP-9 is induced in small renal arteries by recombinant human relaxin, up-regulation of 70%
-
additional information
-
benzo[a]pyrene increases the mRNA level of matrix metalloproteinase 9
-
additional information
-
high glucose (25 mM) induces expression of MMP-9
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
MMP-9 activity in relaxin-treated and untreated renal artery, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
transfected with a construct expressing enzyme. Enzyme overexpressing cells show a significantly reduced collagen gel contraction
additional information
-
increased MMP-9 activity and expression during ventilator-induced lung injury, overview
additional information
-
MMP-9 is increased in tumor cells, no expression in healthy/untreated brain tissue, brain expression analysis after implantation of 9L glioma cells, overview
additional information
-
MMP-9 activity is increased in fibroblasts when the cells are in contact with fibronectin and laminin, while in myoblasts, enhanced activity of the secreted enzyme occurs only in presence of collagen
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
mice that lack matrix metalloproteinase-9 display delayed wound healing associated with delayed reepithelization and disordered collagen fibrillogenesis
metabolism
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activities of MMP-9 synthesized by fibroblasts tend to be regulated by the specific extracellular protein the cells are in contact with, whereas the gelatinolytic actions of proteases produced by myoblasts are more responsive to the mechanical deformation
physiological function
physiological function
-
matrix metalloproteinase-9 controls N-methyl-D-aspartate receptor surface diffusion through integrin beta1 signaling, enzymatic activity of MMP-9 increases lateral diffusion of NR1- N-methyl-D-aspartate receptors without cleavage of NR subunits, MMP-9 does not affect GluR2-alpha-amino-3-hydroxy-5-methyl-4-isoxazole-propionic acid receptor surface diffusion, MMP-9 affects N-methyl-D-aspartate receptors lateral diffusion via integrin signaling
physiological function
-
MMP-9 is involved in both bacterial translocation and polymorphonuclear neutrophil granulocytes transmigration in rat severe acute pancreatitis
physiological function
-
MMP-9 is required for tissue remodeling in response to natural hydroxyapatite
physiological function
-
MMP-9 is the key factor involved in blood-brain barrier disruption and subsequent brain injury after photothrombotic cerebral ischemia in rats
physiological function
-
MMP-9 plays a causative role in blood-brain barrier disruption after peripheral thermal injury
physiological function
-
MMP-9- mediated occludin degradation represents an important mechanism for blood brain barrier disruption in ischemic stroke
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MMP9_RAT
708
0
78611
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
135000
-
neutrophil gelatinase-associated lipocalin-MMP-9 complex, SDS-PAGE
150000
-
gelatinolytic activity of MMP-9 is observed at two molecular weights, 150000 Da and 92000 Da, the 150000 Da band represents a complex of MMP-9 with itself, other matrix metallproteinases, or other molecules such as TIMPs or inflammatory molecules
86000
92000
86000
-
x * 92000, pro-MMP-9, SDS-PAGE, x * 86000, activated MMP-9, SDS-PAGE
86000
-
x * 92000, pro-MMP9, SDS-PAGE, x * 86000, activated MMP-9, SDS-PAGE
92000
-
gelatinolytic activity of MMP-9 is observed at two molecular weights, 150000 Da and 92000 Da, the 92000 Da form corresponds to the MMP-9 pro form
92000
-
x * 92000, pro-MMP-9, SDS-PAGE, x * 86000, activated MMP-9, SDS-PAGE
92000
-
x * 92000, pro-MMP9, SDS-PAGE, x * 86000, activated MMP-9, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
elevated plasma levels of MMP-9 are correlated with brain levels within 24 h of acute cerebral ischemia in rats
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expression of MMP9 protein and mRNA increases in rat brain tissue after cardiopulmonary resuscitation
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F(ab')2 fragments or stimulation with lipopolysaccharide have no effect on MMP-9 production
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in the extract from the small intestine 24 h after indomethacin administration, the MMP-9 activation is significantly attenuated by 10 mg/kg 2-[4-(5-fluoro-3-methylbenzo[b]thiophen-2-yl)sulfonamido-3-methanesulfonylphenyl] thiazole-4-carboxylic acid
-
ischemia and reperfusion induce an upregulation of MMP-9 in the ischemic hemispheric microvessels
-
low-energy laser irradiation (wavelength of 810 nm with continuous waves at 100 mW output power) facilitates MMP-9 expression in rats 7 days after treatment
-
MMP-9 activity is increased in fibroblasts when the cells are in contact with fibronectin and laminin, while in myoblasts, enhanced activity of the secreted enzyme occurs only in presence of collagen
-
MMP-9 activity is significantly increased to 5.0 and 6.1times of the normal intestinal value 12 and 24 h after indomethacin administration, respectively
-
MMP-9 is markedly increased in both the bronchoalveolar lavage fluid and in the lung parenchyma of bleomycin-treated rats, especially in the early phase with the peak on the 4th day
-
MMP-9 protein activity is detected as early as 2 h after the focal ischemic insult (focal cerebral ischemia by photothrombosis), it rapidly increases at 6 h after ischemia, and reaches a maximum level 48 h after the ischemic event. Thereafter, the MMP-9 level abruptly decreases and returns to the baseline at 72 h after the insult
-
monomeric alpha-synuclein dose-dependently increases MMP-9 activity as well as mRNA level from cultured rat primary astrocytes and microglial cells (about 3fold stimulation at 200 nM). Same concentration of alpha-synuclein aggregates do not induce MMP-9 activity
-
normobaric hyperoxia inhibits MMP-9-mediated occludin degradation in the ischemic hemispheric microvessels
-
orthodontic pressure induces gene transcription MMP-9 in pressure gingival soft tissue
-
polyclonal immunoglobulins (IVIg) induce expression of MMP-9 in microglia
-
the broad-spectrum matrix metalloproteinase inhibitor doxycycline reduces pulmonary expression of active MMP-9
-
the levels of MMP-9 and reactive oxygen species in the gut of rats with severe acute pancreatitis are significantly higher than those of the rats treated with anti-rat polymorphonuclear neutrophil granulocytes serum or BB-94
-
there are significant increases in MMP-9 protein expression and enzyme activity 7 h after thermal injury
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
endogenous urokinase plasminogen activator from cultured hepatic stellate cells significantly induces the active forms of enzyme and matrix metalloproteinase MMP-2 in cirrhotic tissue slices. Transfection of hepatic stellate cells with urokinase plasminogen activator gene results in overactivation of enzyme and matrix metalloproteinases MMP-3 and MMP-2
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Defawe, O.D.; Kenagy, R.D.; Choi, C.; Wan, S.Y.; Deroanne, C.; Nusgens, B.; Sakalihasan, N.; Colige, A.; Clowes, A.W.
MMP-9 regulates both positively and negatively collagen gel contraction: a nonproteolytic function of MMP-9
Cardiovasc. Res.
66
402-409
2005
Rattus norvegicus
Gonzalez-Cuevas, J.; Bueno-Topete, M.; Armendariz-Borunda, J.
Urokinase plasminogen activator stimulates function of active forms of stromelysin and gelatinases (MMP-2 and MMP-9) in cirrhotic tissue
J. Gastroenterol. Hepatol.
21
1544-1554
2006
Rattus norvegicus
Kim, J.H.; Suk, M.H.; Yoon, D.W.; Lee, S.H.; Hur, G.Y.; Jung, K.H.; Jeong, H.C.; Lee, S.Y.; Lee, S.Y.; Suh, I.B.; Shin, C.; Shim, J.J.; In, K.H.; Yoo, S.H.; Kang, K.H.
Inhibition of matrix metalloproteinase-9 prevents neutrophilic inflammation in ventilator-induced lung injury
Am. J. Physiol. Lung Cell Mol. Physiol.
291
L580-L587
2006
Rattus norvegicus
Jeyabalan, A.; Novak, J.; Doty, K.D.; Matthews, J.; Fisher, M.C.; Kerchner, L.J.; Conrad, K.P.
Vascular matrix metalloproteinase-9 mediates the inhibition of myogenic reactivity in small arteries isolated from rats after short-term administration of relaxin
Endocrinology
148
189-197
2007
Rattus norvegicus
Zhao, J.X.; Yang, L.P.; Wang, Y.F.; Qin, L.P.; Liu, D.Q.; Bai, C.X.; Nan, X.; Shi, S.S.; Pei, X.J.
Gelatinolytic activity of matrix metalloproteinase-2 and matrix metalloproteinase-9 in rat brain after implantation of 9L rat glioma cells
Eur. J. Neurol.
14
510-516
2007
Rattus norvegicus
Thornton, P.; Pinteaux, E.; Allan, S.M.; Rothwell, N.J.
Matrix metalloproteinase-9 and urokinase plasminogen activator mediate interleukin-1-induced neurotoxicity
Mol. Cell. Neurosci.
37
135-142
2008
Rattus norvegicus
Ding, J.Y.; Kreipke, C.W.; Schafer, P.; Schafer, S.; Speirs, S.L.; Rafols, J.A.
Synapse loss regulated by matrix metalloproteinases in traumatic brain injury is associated with hypoxia inducible factor-1alpha expression
Brain Res.
1268
125-134
2009
Rattus norvegicus (P50282)
Chen, B.; Liao, W.Q.; Xu, N.; Xu, H.; Wen, J.Y.; Yu, C.A.; Liu, X.Y.; Li, C.L.; Zhao, S.M.; Campbell, W.
Adiponectin protects against cerebral ischemia-reperfusion injury through anti-inflammatory action
Brain Res.
1273
129-137
2009
Rattus norvegicus
Reddy, A.B.; Ramana, K.V.; Srivastava, S.; Bhatnagar, A.; Srivastava, S.K.
Aldose reductase regulates high glucose-induced ectodomain shedding of tumor necrosis factor (TNF)-alpha via protein kinase C-delta and TNF-alpha converting enzyme in vascular smooth muscle cells
Endocrinology
150
63-74
2009
Rattus norvegicus
De Stefano, D.; Nicolaus, G.; Maiuri, M.C.; Cipolletta, D.; Galluzzi, L.; Cinelli, M.P.; Tajana, G.; Iuvone, T.; Carnuccio, R.
NF-kappaB blockade upregulates Bax, TSP-1, and TSP-2 expression in rat granulation tissue
J. Mol. Med.
87
481-492
2009
Rattus norvegicus
Kwon, I.; Kim, E.H.; del Zoppo, G.J.; Heo, J.H.
Ultrastructural and temporal changes of the microvascular basement membrane and astrocyte interface following focal cerebral ischemia
J. Neurosci. Res.
87
668-676
2009
Rattus norvegicus
Dai, J.; Louedec, L.; Philippe, M.; Michel, J.B.; Houard, X.
Effect of blocking platelet activation with AZD6140 on development of abdominal aortic aneurysm in a rat aneurysmal model
J. Vasc. Surg.
49
719-727
2009
Rattus norvegicus
Cheng, Y.C.; Chen, L.M.; Chang, M.H.; Chen, W.K.; Tsai, F.J.; Tsai, C.H.; Lai, T.Y.; Kuo, W.W.; Huang, C.Y.; Liu, C.J.
Lipopolysaccharide upregulates uPA, MMP-2 and MMP-9 via ERK1/2 signaling in H9c2 cardiomyoblast cells
Mol. Cell. Biochem.
325
15-23
2009
Rattus norvegicus
Ranasinghe, H.S.; Williams, C.E.; Christophidis, L.J.; Mitchell, M.D.; Fraser, M.; Scheepens, A.
Proteolytic activity during cortical development is distinct from that involved in hypoxic ischemic injury
Neuroscience
158
732-744
2009
Rattus norvegicus
Meng, D.; Lv, D.D.; Zhuang, X.; Sun, H.; Fan, L.; Shi, X.L.; Fang, J.
Benzo[a]pyrene induces expression of matrix metalloproteinases and cell migration and invasion of vascular smooth muscle cells
Toxicol. Lett.
184
44-49
2009
Rattus norvegicus
Romana-Souza, B.; Santos, J.S.; Monte-Alto-Costa, A.
Beta-1 and beta-2, but not alpha-1 and alpha-2, adrenoceptor blockade delays rat cutaneous wound healing
Wound Repair Regen.
17
230-239
2009
Rattus norvegicus
Piao, M.S.; Lee, J.K.; Park, C.S.; Ryu, H.S.; Kim, S.H.; Kim, H.S.
Early activation of matrix metalloproteinase-9 is associated with blood-brain barrier disruption after photothrombotic cerebral ischemia in rats
Acta Neurochir. (Wien)
151
1649-1653
2009
Rattus norvegicus
Lee, T.Y.; Lee, K.J.; Baik, H.S.
Expression of IL-1beta, MMP-9 and TIMP-1 on the pressure side of gingiva under orthodontic loading
Angle Orthod.
79
733-739
2009
Rattus norvegicus
He, Z.J.; Huang, Z.T.; Chen, X.T.; Zou, Z.J.
Effects of matrix metalloproteinase 9 inhibition on the blood brain barrier and inflammation in rats following cardiopulmonary resuscitation
Chin. Med. Sci.
122
2346-2351
2009
Rattus norvegicus
Sochor, M.; Richter, S.; Schmidt, A.; Hempel, S.; Hopt, U.T.; Keck, T.
Inhibition of matrix metalloproteinase-9 with doxycycline reduces pancreatitis-associated lung injury
Digestion
80
65-73
2009
Rattus norvegicus
Yamaguchi, M.; Hayashi, M.; Fujita, S.; Yoshida, T.; Utsunomiya, T.; Yamamoto, H.; Kasai, K.
Low-energy laser irradiation facilitates the velocity of tooth movement and the expressions of matrix metalloproteinase-9, cathepsin K, and alpha(v) beta(3) integrin in rats
Eur. J. Orthod.
32
131-139
2010
Rattus norvegicus
Zambuzzi, W.F.; Paiva, K.B.; Menezes, R.; Oliveira, R.C.; Taga, R.; Granjeiro, J.M.
MMP-9 and CD68(+) cells are required for tissue remodeling in response to natural hydroxyapatite
J. Mol. Histol.
40
301-309
2009
Rattus norvegicus
Liu, W.; Hendren, J.; Qin, X.J.; Shen, J.; Liu, K.J.
Normobaric hyperoxia attenuates early blood-brain barrier disruption by inhibiting MMP-9-mediated occludin degradation in focal cerebral ischemia
J. Neurochem.
108
811-820
2009
Rattus norvegicus
Pul, R.; Kopadze, T.; Skripuletz, T.; Voss, E.V.; Kieseier, B.C.; Stangel, M.
Polyclonal immunoglobulins (IVIg) induce expression of MMP-9 in microglia
J. Neuroimmunol.
217
46-50
2009
Rattus norvegicus
Michaluk, P.; Mikasova, L.; Groc, L.; Frischknecht, R.; Choquet, D.; Kaczmarek, L.
Matrix metalloproteinase-9 controls NMDA receptor surface diffusion through integrin beta1 signaling
J. Neurosci.
29
6007-6012
2009
Rattus norvegicus
Reyes, R.; Guo, M.; Swann, K.; Shetgeri, S.U.; Sprague, S.M.; Jimenez, D.F.; Barone, C.M.; Ding, Y.
Role of tumor necrosis factor-alpha and matrix metalloproteinase-9 in blood-brain barrier disruption after peripheral thermal injury in rats
J. Neurosurg.
110
1218-1226
2009
Rattus norvegicus
Kakimoto, K.; Takai, S.; Murano, M.; Ishida, K.; Yoda, Y.; Inoue, T.; Jin, D.; Umegaki, E.; Higuchi, K.
Significance of chymase-dependent matrix metalloproteinase-9 activation on indomethacin-induced small intestinal damages in rats
J. Pharmacol. Exp. Ther.
332
684-689
2010
Rattus norvegicus
Pavlaki, M.; Giannopoulou, E.; Niarakis, A.; Ravazoula, P.; Aletras, A.J.
Walker 256 cancer cells secrete tissue inhibitor of metalloproteinase-free metalloproteinase-9
Mol. Cell. Biochem.
328
189-199
2009
Rattus norvegicus
Siskova, Z.; Yong, V.W.; Nomden, A.; van Strien, M.; Hoekstra, D.; Baron, W.
Fibronectin attenuates process outgrowth in oligodendrocytes by mislocalizing MMP-9 activity
Mol. Cell. Neurosci.
42
234-242
2009
Rattus norvegicus
Joo, S.H.; Kwon, K.J.; Kim, J.W.; Kim, J.W.; Hasan, M.R.; Lee, H.J.; Han, S.H.; Shin, C.Y.
Regulation of matrix metalloproteinase-9 and tissue plasminogen activator activity by alpha-synuclein in rat primary glial cells
Neurosci. Lett.
469
352-356
2010
Rattus norvegicus
Park, K.P.; Rosell, A.; Foerch, C.; Xing, C.; Kim, W.J.; Lee, S.; Opdenakker, G.; Furie, K.L.; Lo, E.H.
Plasma and brain matrix metalloproteinase-9 after acute focal cerebral ischemia in rats
Stroke
40
2836-2842
2009
Rattus norvegicus
Mikami, Y.; Dobschuetz, E.V.; Sommer, O.; Wellner, U.; Unno, M.; Hopt, U.; Keck, T.
Matrix metalloproteinase-9 derived from polymorphonuclear neutrophils increases gut barrier dysfunction and bacterial translocation in rat severe acute pancreatitis
Surgery
145
147-156
2009
Rattus norvegicus
Kim, J.Y.; Choeng, H.C.; Ahn, C.; Cho, S.H.
Early and late changes of MMP-2 and MMP-9 in bleomycin-induced pulmonary fibrosis
Yonsei Med. J.
50
68-77
2009
Rattus norvegicus
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