MMP2

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Identifiers
EC number	3.4.24.24
CAS number	146480-36-6
Alt. names
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway

Matrix metalloproteinase-2 (MMP-2), also known as gelatinase A, is an enzyme that in humans is encoded by the MMP2 gene. MMP-2 is part of the matrix metalloproteinase (MMP) family, a group of enzymes involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis.

Function

MMP-2 plays a critical role in the degradation of collagen types IV, V, VII, and X, which are major components of the extracellular matrix. This activity is crucial during tissue remodeling and repair processes. MMP-2 is also involved in the cleavage of other substrates, including laminin, elastin, and fibronectin, which facilitates cell migration and tissue remodeling.

Gene and Expression

The MMP2 gene is located on chromosome 16 in humans. The expression of MMP-2 is regulated by various growth factors and cytokines, including transforming growth factor beta (TGF-β) and tumor necrosis factor alpha (TNF-α). MMP-2 is produced as a zymogen called pro-MMP-2, which is activated when cleaved by other MMPs such as MMP-14.

Clinical Significance

Abnormal regulation of MMP-2 has been linked to a variety of diseases. Overexpression of MMP-2 has been observed in various types of cancer, where it helps cancer cells to invade adjacent tissues and spread to other parts of the body. Inhibition of MMP-2 activity is therefore considered a therapeutic target for the prevention of tumor metastasis.

MMP-2 is also implicated in cardiovascular diseases, such as atherosclerosis and aneurysm, where excessive matrix degradation can lead to tissue breakdown and disease progression.

See Also

• Matrix metalloproteinase
• Extracellular matrix
• Metastasis