MMP14

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MMP14

A gene on chromosome 14q11-q12 that encodes matrix metalloproteinase 14, which specifically activates progelatinase A. It may be involved in actin cytoskeleton reorganisation by cleaving PTK7. Unlike other matrix metalloproteinases, which are secreted as inactive proproteins and activated when cleaved by extracellular proteinases, MMP14 is a transmembrane protein that is activated from its precursor by furin endopeptidase cleavage.

Molecular pathology
MMP14 may trigger invasion by tumour cells by activating progelatinase A on the surface of tumour cells.

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References in periodicals archive ?

It was reported that the activation of MMP-2 in cervical cancer tissue could be mediated by a functional complex consisting of [alpha](v)[beta]3 integrin/membrane type-1 metalloproteinase-2 (MT1-MMP)/tissue inhibitor of metalloproteinase-2 (TIMP-2) on tumor cell surface (24).

Glycoprotein nonmetastatic melanoma protein B accelerates tumorigenesis of cervical cancer in vitro by regulating the Wnt/[beta]-catenin pathway

Fetal insulin and IGF-II contribute to gestational diabetes mellitus (GDM)-associated up-regulation of membrane-type matrix metalloproteinase 1 (MT1-MMP) in the human feto-placental endothelium.

Altered Matrix Metalloproteinases Expression in Placenta from Patients with Gestational Diabetes Mellitus

Membrane-type 1 matrix metalloprotease (MT1-MMP) enables invasive migration of glioma cells in central nervous system white matter.

Effects of Caffeic Acid Phenethyl Ester on Retinal Damage After Traumatic Brain Injury/Efectos del Ester Fenetilico del Acido Cafeico en el Dano de la Retina Despues de Una Lesion Cerebral Traumatica

Galvez, "Matrixmetalloproteinases:New routes to the use of MT1-MMP as a therapeutic target in angiogenesis-related disease," Current PharmaceuticalDesign, vol.

Construction and Evaluation of the Tumor-Targeting, Cell-Penetrating Multifunctional Molecular Probe iCREKA

Thompson, "High threshold of integrin inhibition required to block collagen I-induced membrane type-1 matrix metalloproteinase (MT1-MMP) activation of matrix metalloproteinase 2 (MMP-2)," Cancer Cell International, vol.

Establishment of a Model of Microencapsulated SGC7901 Human Gastric Carcinoma Cells Cocultured with Tumor-Associated Macrophages

Depending on the substrate specificity and structure, MMPs are divided into several subgroups: collagenases (e.g., MMP-1), gelatinases (e.g., MMP-2 and MMP-9), stromelysins (e.g., MMP-3 and MMP-10), matrilysins (e.g., MMP-7 and MMP-26), and membrane-type matrix metalloproteinase-1 (MT1-MMP).

IL-1[beta]-Induced Matrix Metalloprotease-1 Promotes Mesenchymal Stem Cell Migration via PAR1 and G-Protein-Coupled Signaling Pathway

[16], who developed a radiolabelled peptide probe by adding a Cys residue at the N-terminus of the peptide MT1-AF7p to allow facile radiolabelling of the thiol moiety by N-(m-[[sup.123/125]I]iodophenyl) maleimide ([123/125I]IPM) for SPECT/CT imaging in HT1080-tumour-bearing mice (HT1080 is a human fibrosarcoma cell line known to highly express MT1-MMP); the radiolabelled probe was therefore similar to DOTA-AF7p but with IPM instead of DOTA.

MT1-MMP as a PET Imaging Biomarker for Pancreas Cancer Management

Galvez, "Matrix metalloproteinases: new routes to the use of MT1-MMP as a therapeutic target in angiogenesis-related disease," Current Pharmaceutical Design, vol.

Selected Metabolic Markers in Girls with Turner Syndrome: A Pilot Study

MT1-MMP has been shown to enhance the basic fibroblast growth factor- (bFGF-) induced CNV in vivo [11].

Effect of Collagen Cross-Linking on Alkali Burn-Induced Corneal Neovascularization in Rabbits

Characterization of the distinct collagen binding and cleveage mechanisms of matrix metalloproteinase 2 and 14 (gelatinase A and MT1-MMP): the different roles of the MMP hemopexin C domains and the MMP-2 fibronectin type II modules in collagen triple helicase activities.

Matrix metalloproteinases in urinary system tumours. Part I - Matrix metalloproteinases in renal cell carcinoma

The vascular reactivity and time-course changes of collagen type I, MMP-2, membrane type 1-MMP (MT1-MMP), and tissue inhibitor of metalloproteinase-2 (TIMP-2) protein expression in mesenteric arteries were evaluated.

Estrogen deficiency modifies matrix metalloproteinases activity and vascular function of mesenteric arteries in female rats

Tissue sections (7 pm) from middermal elastolysis or healthy control skins were used for immunohistochemical analysis of MMP-3, MMP9, MMP-2, MMP-1, TIMP-2, and MT1-MMP (MMP-14).

Middermal Elastolysis: Dermal Fibroblasts Cooperate with Inflammatory Cells to the Elastolytic Disorder