JavaScript is disabled in your browser. Please enable JavaScript to view this website.

MMP2

GeneName

MMP2

Summary

MMP2, also known as MMP-2 or matrix metalloproteinase-2, is a 74 kDa enzyme that is secreted into the extracellular space and plays a vital role in the degradation of the extracellular matrix. It is involved in various biological processes such as angiogenesis, cell migration, and tissue remodelling. MMP2 exhibits endopeptidase activity, including metallopeptidase and fibronectin binding, and is localised in multiple cellular compartments including the extracellular matrix, plasma membrane, and cytoplasm. Its activity is regulated by zinc ion binding and it participates in the collagen catabolic process, contributing to the dynamic regulation of tissue architecture and repair.

Importance

MMP2 is relevant to: - Tumour progression and metastasis through its role in extracellular matrix remodelling and facilitating cell migration - Cardiovascular health as it is involved in blood vessel maturation and angiogenesis - Wound healing and tissue repair due to its function in collagen degradation and tissue remodelling - Neurodegenerative diseases, where it may influence neuronal survival and plasticity through its involvement in the response to oxidative stress and other stimuli

Top Products

For researchers investigating MMP2, we highly recommend the top-selling recombinant antibody, Anti-MMP2 antibody [EPR1184] (ab92536). This antibody has been validated for use in Western blotting (WB), immunocytochemistry (ICC), and flow cytometry (FC), making it a versatile tool for various experimental needs. With 562 citations, it is well-regarded in the research community, reflecting its reliability and effectiveness in MMP2 detection. This product offers the batch-to-batch consistency that is essential for reproducible results in your studies. The Recombinant human MMP2 protein (Active) ELISA Kit (ab280347) is an excellent option for researchers looking to measure MMP2 levels in their samples.

Abcam Product Citation Summary

The data indicates a significant focus on the role of MMP2 in various human cancers, particularly hepatocellular carcinoma, with multiple studies employing different Abcam antibodies for detection. The applications primarily involve Western blotting and immunohistochemistry, highlighting MMP2's involvement in processes such as cell migration, invasion, and tumor angiogenesis. Additionally, studies in mouse models provide insights into the mechanisms of pulmonary fibrosis and cardiac fibrosis, suggesting a broader relevance of MMP2 in both human and animal models of disease.

Abcam Product Citation Table

ab100606
Human
Cancer microtissues
29112150
ab100606
Human
Hepatocellular carcinoma cells
26177288
ab100606
Human
Hep3b and HepG2 cells
32420351
ab86607
Human
IHC
Tumor tissues
31754182
ab86607
Human
WB
Aneurysmal tissue
32111073
ab86607
Mouse
WB
Myofibroblast differentiation
28098218
ab92536
Human
WB
HeLa cells
29267213
ab92536
Mouse
WB
Heart tissue
29977226
ab92536
Mouse
IHC
Liver metastases
27086923
ab97779
Human
WB
Cervical cancer cells
31138113
ab97779
Human
WB
Hepatocellular carcinoma
31387619

Domain

The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Function

Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues in association with MMP14.

PEX, the C-terminal non-catalytic fragment of MMP2, possesses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. Ligand for integrinv/beta3 on the surface of blood vessels.

Isoform 2

Mediates the proteolysis of CHUK/IKKA and initiates a primary innate immune response by inducing mitochondrial-nuclear stress signaling with activation of the pro-inflammatory NF-kappaB, NFAT and IRF transcriptional pathways.

Involvement in disease

Multicentric osteolysis, nodulosis, and arthropathy

MONA

An autosomal recessive syndrome characterized by severe multicentric osteolysis with predominant involvement of the hands and feet. Additional features include coarse face, corneal opacities, patches of thickened, hyperpigmented skin, hypertrichosis and gum hypertrophy.

None

The disease is caused by variants affecting the gene represented in this entry.

Post-translational modifications

Phosphorylation on multiple sites modulates enzymatic activity. Phosphorylated by PKC in vitro.

The propeptide is processed by MMP14 (MT-MMP1) and MMP16 (MT-MMP3). Autocatalytic cleavage in the C-terminal produces the anti-angiogenic peptide, PEX. This processing appears to be facilitated by binding integrinv/beta3.

Sequence Similarities

Belongs to the peptidase M10A family.

Tissue Specificity

Produced by normal skin fibroblasts. PEX is expressed in a number of tumors including gliomas, breast and prostate.

Cellular localization

Alternative names

CLG4A, MMP2, 72 kDa type IV collagenase, 72 kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, TBE-1, MMP-2

swissprot:P08253 omim:120360 entrezGene:4313

Other research areas