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
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instil
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urokinase-type
- matrilysin
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airspace
- mt1-mmp
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cs-induced
- elastases
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smoke-exposed
-
emphysematous
- diagnostics
- drug development
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elastase-induced
- collagenase-3
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cs-exposed
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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
3.4.24.65 macrophage elastaseAdvanced search results
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Natural Substrates Products on EC 3.4.24.65 - macrophage elastase
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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
extracellular matrix protein + H2O
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may be required for macrophages to penetrate basement membranes and remodel injured tissue during inflammation
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Elastin + H2O
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MMP-12 is active against multiple extracellular protein substrates such as elastin, its effect on elastin is central to emphysema in the lung and photoaging of skin, its expression in the skin increases on photodamaged skin and upon aging
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Elastin + H2O
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a key structural component of the lung extracellular matrix
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additional information
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able to degrade all components of extracellular matrix
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?
additional information
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able to degrade all components of extracellular matrix
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?
additional information
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important role in inflammatory processes contributing to tissue remodelling
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?
additional information
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macrophage-derived overexpression of MMP-12 causes accelerated atherosclerosis. Overexpression of human MMP-12 in macrophages of rabbits results in enhanced atherosclerosis
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additional information
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MMP-12 exacerbates atherosclerosis, emphysema, aortic aneurysm, rheumatoid arthritis, and inflammatory bowel disease
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additional information
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the enzyme induces inflammation in murine airways after direct instillation eliciting the inflammatory response by neutrophil influx, cytokine release, and gelatinase activation, and delayed response by macrophage recruitment, overview
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additional information
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the enzyme induces inflammation in murine airways after direct instillation eliciting the inflammatory response by neutrophil influx, cytokine release, and gelatinase activation, and delayed response by macrophage recruitment, resident alveolar macrophages and recruited neutrophils do not play a role in the delayed macrophage recruitment induced by MMP-12, overview
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additional information
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the enzyme plays an important role in inflammatory processes and is involved in a number of physiological or pathological situations, such as conversion of plasminogen into angiostatin, allergic airway inflammation, vascular remodeling or alteration, as well as emphysema
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additional information
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HME has the ability to convert plasminogen into angiostatin, an essential and potent inhibitor of endothelial cell proliferation and tumor angiogenesis
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additional information
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the catalytic domain of MMP-12 is unique among MMPs in that it is very highly active on numerous substrates including elastin
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additional information
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the catalytic domain of MMP-12 is unique among MMPs in that it is very highly active on numerous substrates including elastin
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additional information
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MMP-12 does not appear to be involved in the fibrogenic pathway of bleomycin-induced lung injury. MMP-12 deficiency does not influence the bleomycin-induced raise of neither TGF-beta-1 nor TIMP-1 in lung, which are described as important pro-fibrogenic effectors
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additional information
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protease-activated receptor 1, PAR-1, controls MMP-12 release
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additional information
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the enzyme is important for allowing macrophage migration through extracellular matrix, and probably plays an important role in the causation of inflammatory bowel disease, IBD, MMP-12 expression is increased in ulcerative colitis and in Crohns disease
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additional information
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MMP12 has a direct bactericidal activity but is unable to kill certain bacteria such as those that have the ability to escape the phagosome, which is exerted by the C-terminal domain, that also alone shows bacterial killing activity
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additional information
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MMP12 is involved in bacterial clearance. Intracellular stores of MMP12 are mobilized to macrophage phagolysosomes after the ingestion of bacterial pathogens. Once inside phagolysosomes, MMP12 adheres to bacterial cell walls where it disrupts cellular membranes resulting in bacterial death. The bacterial killing requires the SR20 sequence, 344-SRNQLFLFKDEKYWLINNLV-363, which alone is also active, but shorter four-amino-acid peptides, Ser-Gly-Arg-Gln, Lys-Asp-Asp-Lys and Lys-Asp-Glu-Lys, do not show antimicrobial activity, suggesting that the loop structure of the protein is required for bacterial killing
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additional information
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the catalytic domain of MMP-12 is unique among MMPs in that it is very highly active on numerous substrates including elastin
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?
additional information
?
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the catalytic domain of MMP-12 is unique among MMPs in that it is very highly active on numerous substrates including elastin
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?
additional information
?
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protease-activated receptor 1, PAR-1, controls MMP-12 release
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?
additional information
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the enzyme is involved in the development of chronic obstructive pulmonary disease and airway inflammation and is associated with allergic bronchial asthma, phenotype, overview
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