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
-
cs-exposed
-
airflow
- medicine
- pharmacology
-
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
3.4.24.65 macrophage elastaseAdvanced search results
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results (Source Tissue
Source Tissue on EC 3.4.24.65 - macrophage elastase
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SOURCE TISSUE 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SOURCE
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MMP-12/tissue inhibitor of metalloproteinase-1 ratio is significantly increased in the CSF of Angiostrongylus cantonensis-infected mice from day 10 p.i., and reaches high levels on days 20 and 25 p.i. MMP-12 production is correlated with elastin degradation, eosinophil count, blood-CSF barrier permeability and pathological changes in the subarachnoid space
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metalloproteinase 12 (MMP-12) is induced in chondrocytes during fetal development and malignant transformation
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HME protein levels are 4.50-7.15fold increased in gastric carcinoma samples compared with the non-cancerous controls
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irregular glomerular basement membrane that characterizes Alport syndrome may be mediated, in part, by focal degradation of glomerular basement membrane due to MMP dysregulation, in particular, MMP-12
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only in glomerulonephritic ICGN strain, not in non-glomerulonephritic mouse (immunohistochemistry)
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ICGN strain, small amounts during early pogression of renal disease, increasing amounts with progressing renal disease (immunohistochemistry)
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HME is expressed in chronic gastritis with atypical hyperplasia and normal gastric epithelium mucosa. HME protein levels are 4.50-7.15fold increased in gastric carcinoma samples compared with the non-cancerous controls
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mainly expressed by inflammatory macrophages in the rhematoid arthritis synovial membrane. Rheumatoid synovial tissue contains higher levels of MMP-12 messenger RNA than does osteoarthritis synovial tissue. Macrophage-derived MMP-12 may play an important role in the destructive process in rheumatoid arthritis
additional information
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the catalytic domain of human recombinant MMP-12 expressed in Escherichia coli
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patients with chronic obstructive pulmonary disease produce greater quantities of MMP-12 than controls, which may be a critical step in the pathogenesis of chronic obstructive pulmonary disease and emphysema
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increased expression of alveolar mucosa macrophage MMP-12 in HIV-healthy smokers compared to HIV1- healthy nonsmokers. MMP-12 expression is further significantly increased in HIV1- smokers with early emphysema in comparison with both HIV1- healthy nonsmokers and HIV1- healthy smokers. Expression of alveolar mucosa MMP-12 is further increased in HIV1+ smokers with early emphysema over and above the increase in HIV1- smokers with early emphysema
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MMP-12 suppresses the growth of lung metastases. Mice deficient in macrophage elastase develop significantly more gross Lewis lung carcinoma pulmonary metastases than wild-type counterparts
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preferential expression of MMP12 in lung macrophages. MMP12 is predominantly produced by airway epithelia and alveolar macrophages
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tissue culture medium of colchicin-treated inflammatory peritoneal macrophages
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serum-free culture medium conditioned by thioglycollate-elicited peritoneal exudative macrophages
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MMP12 is an enzyme predominantly expressed in mature tissue macrophages
additional information
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enzyme expression analysis in bones and cartilage of healthy subjects and patients with osteoarthritis (OA), overview. During disease progression, MMP-12 is expressed at the sides of the cartilage and bone erosion and in the bone cysts. Furthermore, it is traced in the osteocytes of the subchondral bone. Osteoblast-like cells and bone lining cells express MMP-12 during the stage of severe OA. MMP-12 expression is positively correlated with the age and the BMI of OA patients
additional information
alveolar type II cells and macrophages but not neutrophils are the main sources of MMP-12 in the lungs of mice with Streptococcus pneumoniae infection
additional information
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alveolar type II cells and macrophages but not neutrophils are the main sources of MMP-12 in the lungs of mice with Streptococcus pneumoniae infection
additional information
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alveolar type II cells and macrophages but not neutrophils are the main sources of MMP-12 in the lungs of mice with Streptococcus pneumoniae infection
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