3.4.24.65: macrophage elastase
This is an abbreviated version!
For detailed information about macrophage elastase, go to the full flat file.
Word Map on EC 3.4.24.65
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3.4.24.65
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metalloproteinases
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mmp-9
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pulmonary
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emphysema
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collagen
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alveolar
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elastin
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fibrosis
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smoke
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airway
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timp-1
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cigarette
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lavage
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bronchoalveolar
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endothelial
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metastasis
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aortic
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tnf
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artery
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chemokine
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monocyte
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smoking
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plaque
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aneurysm
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angiogenesis
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atherosclerotic
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zymography
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smoke-induced
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elastolytic
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proteinases
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plasminogen
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asthma
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rupture
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angiostatin
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bal
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instil
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urokinase-type
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matrilysin
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airspace
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mt1-mmp
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cs-induced
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elastases
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smoke-exposed
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emphysematous
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diagnostics
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drug development
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elastase-induced
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collagenase-3
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cs-exposed
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airflow
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medicine
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pharmacology
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matrix-degrading
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analysis
- 3.4.24.65
- metalloproteinases
- mmp-9
- pulmonary
- emphysema
- collagen
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alveolar
- elastin
- fibrosis
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smoke
- airway
- timp-1
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cigarette
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lavage
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bronchoalveolar
- endothelial
- metastasis
- aortic
- tnf
- artery
- chemokine
- monocyte
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smoking
- plaque
- aneurysm
- angiogenesis
- atherosclerotic
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zymography
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smoke-induced
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elastolytic
- proteinases
- plasminogen
- asthma
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rupture
- angiostatin
- bal
-
instil
-
urokinase-type
- matrilysin
-
airspace
- mt1-mmp
-
cs-induced
- elastases
-
smoke-exposed
-
emphysematous
- diagnostics
- drug development
-
elastase-induced
- collagenase-3
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cs-exposed
-
airflow
- medicine
- pharmacology
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matrix-degrading
- analysis
Reaction
Hydrolysis of soluble and insoluble elastin. Specific cleavages are also produced at -Ala14-/-Leu- and -Tyr16-/-Leu- in the B chain of insulin =
Synonyms
HME, hMMP-12, human macrophage elastase, Human macrophage metalloelastase, human metalloelastase, Macrophage elastase, macrophage matrix metalloproteinase, macrophage metalloelastase, macrophage-specific metalloelastase, matrix metalloproteinase 12, Matrix metalloproteinase-12, ME, Metalloelastase, MME, MMP-12, MMP12, More, mouse macrophage metalloelastase, rHME
ECTree
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
analysis
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the enzyme can be utilized for pharmacological evaluation of anti-inflammatory mechanisms of action
diagnostics
drug development
medicine
pharmacology
diagnostics
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MMP12 is a no effect level oral cancer marker in neck tissue and gingiva
diagnostics
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overexpression of HME is strongly correlated with the reduced angiogenesis and vascular invasion of gastric carcinoma, and may serve as a useful predictive indicator in patients with this disease
drug development
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the enzyme is a target in treatment of degradative disease processes in the skin
medicine
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abnormal expression of HME may contribute to destructive processes such as pulmonary empysema and vascular aneurysm formation
medicine
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inhibition of MMP-12 may be a potential modality for the treatment of rheumatoid arthritis
medicine
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role in idiophathic diseases, may be even more important in the causation of inflammatory bowel disease than MMP-3, markedly upregulated in a T-cell-mediated model in inflammatory bowel disease, local immune response can increase MMP-12 expression in resident lamina propria macrophages
medicine
chronic cigarette smoke exposure leads to macrophage accumulation and restores adipose MMP12 activity, thereby suppressing adipose tissue mass and vascularity
medicine
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expression of macrophage metalloelastase improves the overall antitumor efficacy of oncolytic adenovirus in subcutaneous HCT116 xenografts. In a liver metastatic colorectal cancer model, intra-tumoral treatment of primary tumors from HT29 cells with macrophage metalloelastase monotherapy or with oncolytic adenovirus inhibits tumor growth. Combination therapy shows no increased mortality in comparison with either monotherapy alone. In a metastatic animal model, macrophage metalloelastase, as a monotherapy or in combination with oncolytic virus, does not increase tumor invasiveness
medicine
expression of MME12 inversely correlates with the expression of basic fibroblast growth factor and tumor angiogenesis in a model of murine colon cancer
medicine
in human ejaculate, MMP-12 concentrations are significantly higher in leucocytospermic samples than in nonleucocytospermic ones. The MMP-12 levels between the normozoospermic samples, oligoasthenoteratozoospermic samples and azoospermic samples do not differ. MMP-12 levels correlate with the presence of peroxidase-positive leucocytes. No correlation with CD 14 positive monocytes/macrophages is detected
medicine
in MMP-12 deficient mice, deficiency has no significant effect on total body weight or on subcutaneous or gonadal adipose tissue mass. Adipocyte and blood vessel size and density in subcutaneous and gonadal adipose tissues of obese mice are also comparable in MMP-12 deficient and control mice. Macrophage infiltration in subcutaneous and gonadal adipose tissues is not affected by MMP-12 deficiency, but the amount of crown-like structures is significantly lower. MMP-12 deficiency does not affect elastin content in the extracellular matrix of subcutaneous or gonadal adipose tissue
medicine
the enzyme is a potential target in treatment of cystic fibrosis
pharmacology
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MMP-12 might be a target for the therapy against allergic bronchial asthma
pharmacology
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MMP-12 plays a predominant role in the inflammatory process induced by cigarette smoke, and therefore is potentially an important therapeutic target for the treatment of chronic obstructive pulmonary diseases
