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Literature summary for 3.4.24.65 extracted from

  • He, J.Q.; Campagne, M.L.
    Macrophage metalloelastase: stretching therapeutic opportunities (2009), J. Mol. Cell Biol., 1, 55-57.
    View publication on PubMed
Search for more literature for 3.4.24.65

Protein Variants

Protein Variants Comment Organism
additional information mice lacking MMP12 have impaired ability to destroy bacteria in the phagolysosomes and die as a result of uncontrolled spread of the infection. The increased mortality is observed when the bacteria are injected through the airway, but not when the bacteria are injected into the blood Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
additional information MMP inhibitors applied in animal models of emphysema are successful in reducing lung inflammation Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Mus musculus
-
-
intracellular
-
 Mus musculus 5622
-
additional information MMP12, in contrast to other MMPs, can act intracellularly rather than extracellularly. The majority of MMP12 is secreted, MMP12 might then bind to the bacteria outside the cell prior to phagocytosis Mus musculus
-
-
phagolysosome
-
 Mus musculus 32010
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ dependent on Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mus musculus 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 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification MMP12 is produced and secreted as a latent pro-enzyme. The pro-domain keeps pro-MMP12 in a catalytically inactive state. After cleavage of the pro-domain, MMP12 becomes proteolytically active. MMP-12 undergoes further processing leading to C-terminal domain shedding, resulting in the mature active form of MMP12 Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
epithelium
-
 Mus musculus
-
lung preferential expression of MMP12 in lung macrophages. MMP12 is predominantly produced by airway epithelia and alveolar macrophages Mus musculus
-
macrophage alveolar Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Elastin + H2O
-
 Mus musculus ?
-
 ?
Fibronectin + H2O
-
 Mus musculus ?
-
 ?
Gelatin + H2O
-
 Mus musculus ?
-
 ?
additional information 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 Mus musculus ?
-
 ?
additional information MMP12, through the catalytic domain, can cleave a variety of substrates in addition to elastin such as type IV collagen, fibronectin, and gelatin in in vitro assays Mus musculus ?
-
 ?
Type IV collagen + H2O
-
 Mus musculus ?
-
 ?

Subunits

Subunits Comment Organism
More pro-MMP-12 contains an N-terminal pro-domain, a catalytic domain, and a C-terminal hemopexin-like domain. The pro-domain is cleaved during maturation. The catalytic domain is essential for the substrate-converting activities of MMPs. Since MMP12 without C-terminal domain is still enzymatically active, the MMP12 C-terminal domain seems not to be required for substrate catalysis. A peptide sequence in the C-terminal domain is responsible for the anti-bacterial activity of MMP-12, but the catalytic domain is not required for the bactericidal property of MMP12, overview Mus musculus

Synonyms

Synonyms Comment Organism
macrophage metalloelastase
-
 Mus musculus
MMP12
-
 Mus musculus
More MMP12 is a member of the MMP family Mus musculus

General Information

General Information Comment Organism
malfunction MMP12 is implicated in inflammatory respiratory disorders such as asthma, pulmonary fibrosis and chronic obstructive pulmonary disease, with a critical role of MMP12 in the development of emphysema. MMP inhibitors applied in animal models of emphysema are successful in reducing lung inflammation Mus musculus
physiological function MMP12 is a lead player in the direct killing of bacteria sequestered in the phagolysosomes. MMP12 aggregates onto the bacteria that are trapped inside the phagolysosomes and disrupts the cell wall constituents, resulting in bacterial death, overview Mus musculus