3.4.24.35: gelatinase B
This is an abbreviated version!
For detailed information about gelatinase B, go to the full flat file.
Word Map on EC 3.4.24.35
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3.4.24.35
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mmp-2
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metalloproteinases
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zymography
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metastasis
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timp-1
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endothelial
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necrosis
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angiogenesis
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tnf
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artery
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fibrosis
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neutrophil
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chemokine
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infarct
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plaque
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monocyte
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vessel
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pulmonary
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myocardial
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cerebral
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mapks
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stroke
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erk
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transwell
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basement
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aortic
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invasiveness
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plasminogen
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blood-brain
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matrigel
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bcl-2
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nf-kappab
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airway
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upa
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osteoclast
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cox-2
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fibronectin
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aneurysm
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c-reactive
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mt1-mmp
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e-cadherin
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coronary
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tnf-alpha
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angiogenic
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atherosclerotic
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anti-metastatic
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tartrate-resistant
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urokinase-type
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drug development
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diagnostics
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elastin
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rankl
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medicine
- 3.4.24.35
- mmp-2
- metalloproteinases
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zymography
- metastasis
- timp-1
- endothelial
- necrosis
- angiogenesis
- tnf
- artery
- fibrosis
- neutrophil
- chemokine
- infarct
- plaque
- monocyte
- vessel
- pulmonary
- myocardial
- cerebral
- mapks
- stroke
- erk
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transwell
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basement
- aortic
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invasiveness
- plasminogen
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blood-brain
- matrigel
- bcl-2
- nf-kappab
- airway
- upa
- osteoclast
- cox-2
- fibronectin
- aneurysm
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c-reactive
- mt1-mmp
- e-cadherin
- coronary
- tnf-alpha
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angiogenic
- atherosclerotic
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anti-metastatic
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tartrate-resistant
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urokinase-type
- drug development
- diagnostics
- elastin
- rankl
- medicine
Reaction
Cleavage of gelatin types I and V and collagen types IV and V =
Synonyms
92 kDa gelatinase, 92 kDa type IV collagenase, 92 kDa type IV collagenase proMMP-9, 92-kDa Gelatinase, 92-kDa gelatinase B, 92-kDa Type IV collagenase, 95 kDa type IV collagenase/gelatinase, Collagenase IV, Collagenase type IV, gelatinase, gelatinase B, Gelatinase MMP 9, gelatinolytic enzyme, GELB, Macrophage gelatinase, matrix metallopeptidase 9, matrix metallopeptidase 9 gelatinase B, matrix metalloprotease-9, Matrix metalloproteinase 9, matrix metalloproteinase-9, metrix metalloproteinase-9, MMP 9, MMP-9, MMP9, neutrophil collagenase, pro-matrix metalloproteinase-9, progelatinase, Type IV collagen metalloproteinase, Type IV collagenase, Type IV collagenase/gelatinase, Type V collagenase
ECTree
3.4.24.35 gelatinase BAdvanced search results
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Source Tissue on EC 3.4.24.35 - gelatinase B
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SOURCE TISSUE 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SOURCE
increased enzyme expression, the positive ratio of MMP-9 tends to increase from Grade II to Grade IV glioma and strong positive MMP-9 staining is more frequently detected in high-grade glioma, association between matrix metalloproteinase-9 expression and survival of patients
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bone marrow-derived cells are the major source of MMP-9 in the ischemic brain
localized mainly in the cytoplasm of neoplastic astrocytes
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expression and activity of MMP-9 during premature rupture of chorioamniotic membranes, secretion of proMMP-9 from the amniochorion after application of lipopolysacchride to either sides of the membrane is increased, overview
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coronary arteritis is induced by Lactobacillus casei cell wall extract injection
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demineralized dentin matrix, extraction is best at acidic conditions of pH 2-3 compared to pH 7.4-EDTA-containing extracts
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MMP-9 is expressed at very low levels in endometrioid adenocarcinoma cells
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MMP-9 protein is localized at the leading-edge keratinocytes in front of the migrating epidermal layer
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expression analysis of MMP 9 in benign, premalignant and malignant laryngeal lesions, e.g. carcinoma and dysplasia, the enzyme is upregulated in malignant tissue, immunohistochemic analysis, overview
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the level of MMP-9 activity in lens epithelial cells is highest in eyes with cortical cataract
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atrophic acnd nonatrophic oral lichen planus
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MMP-9 is expressed at very low levels in serous cystoadenocarcinoma cells
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transfected with a construct expressing enzyme. Enzyme overexpressing cells show a significantly reduced collagen gel contraction
Mycobacterium tuberculosis stimulates matrix metalloproteinases secretion in the host. Analysis of the patterns of matrix metalloproteinase 9 (MMP-9) and 2 (MMP-2) isoforms in sputum samples, overview. Variations in MMP-9 isoforms are observed, which coincide with the progression of tuberculosis infection
additional information
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a macrophage cell line established by immortalization of bone marrow macrophages from C57BL/6 mice with J2 recombinant retrovirus-expressing v-myc/v-raf oncogenes
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a macrophage cell line established by immortalization of bone marrow macrophages from C57BL/6 mice with J2 recombinant retrovirus-expressing v-myc/v-raf oncogenes
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enzyme expression is slightly induced by HIV and strongly induced by TNF alpha, while matrix metalloproteinase MMP-2 and tissue inhibitor of metalloproteinase-1 and tissue inhibitor of metalloproteinase-2 are only slightly affected. Astrocytes are a major source of enzyme in the inflamed brain
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murine melanoma cell line, with platelet-activating factor-induced experimental pulmonary metastasis, which is inhibited by both NF-jB and c-jun inhibitors and completelyby MMP-9 inhibitor
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plasma active MMP-9 and TIMP-1 are measured at three time-points in 163 individuals, thereof 129 males and all with average age of 62.8 years. Active MMP-9 and TIMP-1 are similar irrespective of the months of the year the sample, and are thus independent of season and storage time
serum MMP9 levels are significantly associated with hyperlipidaemia
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articular chondrocyte of the late-stage osteoarthritis cartilage with surface fibrillation and chondrocyte clusters, not in healthy chondrocytes, overview
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stage II/III rectal carcinoma, expression analysis, the MMP-9 expression is related to tumor growth, overview
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from SC40-transformed cells, normal alveolar macrophages, phorbol ester-differentiated monocytic leukemia U937 cells, fibrosarcoma HT1080 cells, cultured keratinocytes
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enzyme protein is present in cells within granulomas and in scattered epitheloid cells
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proteolytic activity and expression of gelatinase B in serum of gastric cancer patients and their correlation with the stage of the tumor
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unstimulated/resident and inflammatory, peritoneal leukocytes, constitutive expression
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unstimulated/resident and inflammatory, peritoneal leukocytes, constitutive expression
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method development and evaluation for immunostaining MMP-9 in mouse lung paraffin-embedded tissue utilizing human ovary as a control, overview. MMP-9 localization in lung tissue of a murine model of allergic asthma induced by chicken ovalbumin. The murine model of allergic asthma consists of a tissue inhibitor of metalloproteinase (TIMP)-1 genetic knockout backcrossed over 10 generations from 129/sv mice on a C57Bl/6 background
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method development and evaluation for immunostaining MMP-9 in mouse lung paraffin-embedded tissue utilizing human ovary as a control, overview. MMP-9 localization in lung tissue of a murine model of allergic asthma induced by chicken ovalbumin. The murine model of allergic asthma consists of a tissue inhibitor of metalloproteinase (TIMP)-1 genetic knockout backcrossed over 10 generations from 129/sv mice on a C57Bl/6 background
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increased MMP-9 activity and expression during ventilator-induced lung injury, overview
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secretion of MMP-9, transcription factor NF-kappaB is important in MMP gene regulation in macrophage cells
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secretion of MMP-9 in the early phase of peritonitis, no MMP-9 production in unstimulated macrophages
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macrophages contribute significantly to the elevated levels of MMP-9 in dystrophic muscle
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secretion of MMP-9 in the early phase of peritonitis, no MMP-9 production in unstimulated macrophages
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treatment of blood-derived mast cells with TNF-alpha significantly increases expression of enzyme mRNA and upregulates enzyme activity. TNF-alpha also increases the invasiveness of mast cells across Matrigel-coated membranes. INF-gamma is inhibitory to enzyme mRNA and protein expression
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distribution of MMP9 in both emigrating and migrating neural crest cells, overview
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distribution of MMP9 in both emigrating and migrating neural crest cells, overview
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secretion of MMP-9, high MMP-9 expression in the early phase and especially in the late phase of peritonitis
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secretion of MMP-9, high MMP-9 expression in the early phase and especially in the late phase of peritonitis
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gene MMP9 is significantly upregulated in 23-wk-old (laying phase) chicken ovaries compared with 6-wk-old ovaries (prepubertal phase). In reproductively active chicken ovary, the enzyme expression level increases during follicular maturation. Enzyme MMP9 mRNA expression continues to rise in postovulatory follicle 1 and postovulatory follicle 2 after ovulation
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gene MMP9 is significantly upregulated in 23-wk-old (laying phase) chicken ovaries compared with 6-wk-old ovaries (prepubertal phase). In reproductively active chicken ovary, the enzyme expression level increases during follicular maturation. Enzyme MMP9 mRNA expression continues to rise in postovulatory follicle 1 and postovulatory follicle 2 after ovulation
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infundibulum, magnum, isthmus, and shell gland. Developmental changes, overview
Gallus gallus Hy-Line Brown
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infundibulum, magnum, isthmus, and shell gland. Developmental changes, overview
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in zymosan-treated mice inducing peritonitis, MMP-9 and ZIMP-1 are located in the peritoneal fluid and plasma at the time of peritoneal neutrophil infiltration and persist there until time of monocyte/macrophage influx
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in zymosan-treated mice inducing peritonitis, MMP-9 and ZIMP-1 are located in the peritoneal fluid and plasma at the time of peritoneal neutrophil infiltration and persist there until time of monocyte/macrophage influx
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no association between plasma MMP-9 activity and the concentrations of lead in whole blood or plasma, overview
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in zymosan-treated mice inducing peritonitis, MMP-9 and ZIMP-1 are located in the peritoneal fluid and plasma at the time of peritoneal neutrophil infiltration and persist there until time of monocyte/macrophage influx
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in zymosan-treated mice inducing peritonitis, MMP-9 and ZIMP-1 are located in the peritoneal fluid and plasma at the time of peritoneal neutrophil infiltration and persist there until time of monocyte/macrophage influx
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668514, 668996, 670741, 684107, 697548, 701178, 708232, 708245, 708784, 708814, 709619, 709819, 710177, 710452, 710542, 710584
additional information
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active host MMP-9 is expressed in walls and fluids of hydatid cysts of parasite Echinococcus granulosus in the environment of granulomatous reaction, immunohistochemic analysis, positive reaction to MMP-9 is found in cyst-surrounding cells, epithelioid and giant cells, and in the germinal layer of cyst wall, overview
additional information
immunohistochemic localization analysis, overview
additional information
quantitative enzyme tissue expression analysis in the chicken oviduct during maturation
additional information
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quantitative enzyme tissue expression analysis in the chicken oviduct during maturation
additional information
Gallus gallus Hy-Line Brown
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quantitative enzyme tissue expression analysis in the chicken oviduct during maturation
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additional information
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immunohistochemic localization analysis, overview
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additional information
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MMP-9 is not expressed in mucinous and clear cell adenocarcinoma cells
additional information
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levels of MMP-9 in choriodecidua and amnion increases 4 and 8fold, respectively, after simultaneous infection with Escherichia coli added to either the amniotic or the choriodecidual face or to both
additional information
enzyme immunohistochemic analysis of 237 samples, overview
additional information
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enzyme immunohistochemic analysis of 237 samples, overview
additional information
enzyme MMP-9 is released in the inactive form as proenzyme and can be secreted in physical association with its specific tissue inhibitor (TIMP-1) by monocyte/macrophage cells as proMMP-9/TIMP-1 complex or as TIMP-1 free protein by tertiary granules of neutrophil cells
additional information
quantitative real time PCR enzyme expression analysis and immunohistochemic analysis in glioblastoma, MMP-9 activity is constitutively heightened in tissue samples from primary glioblastoma multiforme, the most common and aggressive malignant primary brain tumor in humans
additional information
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MMP-9 co-localizes with macrophages and neutrophils in gastritic stomach, overview
additional information
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MMP-9 co-localizes with macrophages and neutrophils in gastritic stomach, overview
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additional information
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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
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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
