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Literature summary for 3.4.24.80 extracted from

  • Ikonomidis, J.S.; Nadeau, E.K.; Akerman, A.W.; Stroud, R.E
    ; Mukherjee, R.; Jones, J.A. Regulation of membrane type-1 matrix metalloproteinase activity and intracellular localization in clinical thoracic aortic aneurysms (2017), J. Thorac. Cardiovasc. Surg., 153, 537-546 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
additional information phosphorylation of MT1-MMP mediates its activity through directing cellular localization Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
plasma membrane
-
Mus musculus 5886
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ a zinc-dependent endopeptidase Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
proMMP-2 + H2O Mus musculus activation MMP-2 + MMP-2 pro-peptide
-
?

Organism

Organism UniProt Comment Textmining
Mus musculus P53690
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein enzyme MT1-MMP is subject to protein kinase C (PKC)-mediated regulation via reversible phosphorylation, which alters intracellular trafficking and activity with thoracic aortic aneurysm (TAA). Phosphorylation of MT1-MMP mediates its activity through directing cellular localization Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
aorta aortic fibroblasts Mus musculus
-
fibroblast aortic fibroblasts Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
proMMP-2 + H2O activation Mus musculus MMP-2 + MMP-2 pro-peptide
-
?

Synonyms

Synonyms Comment Organism
membrane type-1 matrix metalloproteinase
-
Mus musculus
membrane type-1 MMP
-
Mus musculus
MMP14
-
Mus musculus
MT1-MMP
-
Mus musculus

General Information

General Information Comment Organism
physiological function membrane type-1 MMP (MT1-MMP) is elevated during thoracic aortic aneurysm (TAA) development in mouse models, and plays an important role in the activation of MMP-2 and the release of matrix bound TGF-beta. Enzyme MT1-MMP is subject to protein kinase C (PKC)-mediated regulation via reversible phosphorylation, which alters intracellular trafficking and activity with TAA. MT1-MMP abundance increases in aortas from both TAA groups. Active MMP-2 is increased only in large TAAs. Abundance of phosphorylated MT1-MMP and activated-PKC-delta is enhanced in small versus large TAAs. Phosphorylation of MT1-MMP mediates its activity through directing cellular localization, shifting its role from MMP-2 activation to intracellular signaling Mus musculus