MMP-2

Official Full Name

matrix metallopeptidase 2

Organism

Homo sapiens

GeneID

4313

Background

This gene is a member of the matrix metalloproteinase (MMP) gene family, that are zinc-dependent enzymes capable of cleaving components of the extracellular matrix and molecules involved in signal transduction. The protein encoded by this gene is a gelatinase A, type IV collagenase, that contains three fibronectin type II repeats in its catalytic site that allow binding of denatured type IV and V collagen and elastin. Unlike most MMP family members, activation of this protein can occur on the cell membrane. This enzyme can be activated extracellularly by proteases, or, intracellulary by its S-glutathiolation with no requirement for proteolytical removal of the pro-domain. This protein is thought to be involved in multiple pathways including roles in the nervous system, endometrial menstrual breakdown, regulation of vascularization, and metastasis. Mutations in this gene have been associated with Winchester syndrome and Nodulosis-Arthropathy-Osteolysis (NAO) syndrome. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Oct 2014]

Synonyms

CLG4; MONA; CLG4A; MMP-2; TBE-1; MMP-II;

Bio Chemical Class

mRNA target

Protein Sequence

MEALMARGALTGPLRALCLLGCLLSHAAAAPSPIIKFPGDVAPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFFGLPQTGDLDQNTIETMRKPRCGNPDVANYNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFTMGGNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTYTKNFRLSQDDIKGIQELYGASPDIDLGTGPTPTLGPVTPEICKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSASTLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC

Open

Approved Drug

1 +

Clinical Trial Drug

5 +

Discontinued Drug

10 +

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Detailed Information

The specific functions of MMP-2 can be summarized as degrading the active components of extracellular matrix membranes, degrading cell adhesion, acting on extracellular components or other protein components to initiate potential biological functions, and directly or indirectly involved in embryonic development, tissue models remodeling and wound repair. The activity of MMP-2 is highly regulated by post-transcriptional levels. Under physiological conditions, MMP-2 is often secreted as an inactive zymogen and stored in the cytoplasm. MMP-2 is activated by cleavage of its own protein, cleavage of MMP-9 or extracellular inflammatory mediators, and its activity can be inhibited by tissue inhibitor of metalloprotease (TIMP).

Biological Function of MMP-2

As an important component of the MMPs family, MMP-2 is a gelatinase that mainly degrades type IV collagen in the basement membrane, destroys the integrity of the basement membrane, promotes the metastasis of tumor cells, and invades lymphatic vessels and small blood vessels. In addition, MMP- 2 can also hydrolyze other biologically active molecules such as growth factors and cytokines. Other members of the MMPs family, such as proMMP-1, pro-MMP-2, and pro-MMP-13, can be hydrolyzed into activated forms for biological effects. MMP-2 can also act on non-matrix proteins, such as endothelin-1 and calcitonin gene-related peptides, thereby promoting vasoconstriction. The C-terminal non-catalytic fragment of MMP2 gene possesses anti-angiogenic and anti-tumor properties.

MMP2 activates the mitochondrial-nuclear stress signal, induces the activation signal of nuclear transcription factor B, and activates the T cell nuclear factor interferon regulatory factor, thereby affecting the transcriptional pathway. The study found that MMP2 can be expressed in the eye sclera of animals such as human pheasant, and its gene mutation or abnormal expression will affect the remodeling of scleral tissue, such as scleral collagen thinning and extracellular matrix protease abnormalities.

Overexpression of MMP2 may affect the refraction of scleral tissue in patients with diopter changes, which may lead to pathological myopia, and its pathological changes are important factors for the continuous decline of visual acuity in pathological myopia. Inhibition of the increased expression of MMP2 in scleral tissue can limit the persistence of visual acuity in patients with pathological myopia. In-depth study found that the inhibition of MMP2 gene expression in scleral fibroblasts retinal pigment epithelial cells can effectively control the changes in diopter of patients with pathological myopia, so MMP2 gene may be used as a target for the prevention and treatment of pathological myopia.

MMP-2 Figure 1. Schematic model showing the distribution and functions of MMP9 and MMP2 in tumor cell proliferation and colonization within the osseous microenvironment. (Liu, B., et al. 2016)

MMP-2 and Tumor

Studies have shown that MMP-2 genes and proteins are differentially expressed in tumors of various origins. The expression rate of MMP-2 in malignant tumors such as ovarian cancer and lung cancer is related to clinical stage and tissue grade. The breast cancer cell lines MCF7 and MDA-MB-23l were found to increase the expression of MMP-2 in tumor cells. Studies have shown that MMP-2 is not expressed or under expressed in normal breast or benign tumors, while MMP-2 expression and activity in breast cancer tissues are significantly enhanced. The results showed that the positive expression rate of MMP-2 in breast cancer was significantly higher than that in benign breast lesions. Studies have shown that MMP-2 plays an important role in cancer cell shedding, migration, invasion and metastasis. MMPS, especially MMP-2, plays a key role in tumor cell-mediated degradation of extracellular matrix.

References:

Liu, B. , Cui, J. , Sun, J. , Li, J. , Han, X. , & Guo, J. , et al. (2016). Immunolocalization of mmp9 and mmp2 in osteolytic metastasis originating from mda-mb-231 human breast cancer cells. Molecular Medicine Reports.
Shrestha, B. , Bajracharya, D. , Byatnal, A. A. , Kamath, A. , & Radhakrishnan, R. . (2016). May high mmp-2 and timp-2 expressions increase or decrease the aggressivity of oral cancer?. Pathology & Oncology Research, 23(1), 1-10.
Deng, J. , Chen, W. , Du, Y. , Wang, W. , Zhang, G. , & Tang, Y. , et al. (2017). Synergistic efficacy of cullin1 and mmp-2 expressions in diagnosis and prognosis of colorectal cancer. Cancer Biomarkers, 1-8.

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