MMP2
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Matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase), also known as MMP2, is a human gene.
Proteins of the matrix metalloproteinase (MMP) family are 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. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. This gene encodes an enzyme which degrades type IV collagen, the major structural component of basement membranes. The enzyme plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response. Mutations in this gene have been associated with Winchester syndrome, Torg syndrome and nodulosis-arthropathy-osteolysis syndrome (NAO syndrome).[1]
References
Further reading
- Massova I, Kotra LP, Fridman R, Mobashery S (1998). "Matrix metalloproteinases: structures, evolution, and diversification". FASEB J. 12 (12): 1075–95. PMID 9737711.
- Nagase H, Woessner JF (1999). "Matrix metalloproteinases". J. Biol. Chem. 274 (31): 21491–4. PMID 10419448.
- Goffin F, Frankenne F, Béliard A; et al. (2002). "Human endometrial epithelial cells modulate the activation of gelatinase a by stromal cells". Gynecol. Obstet. Invest. 53 (2): 105–11. PMID 11961384.
- Hrabec E, Naduk J, Strek M, Hrabec Z (2007). "[Type IV collagenases (MMP-2 and MMP-9) and their substrates--intracellular proteins, hormones, cytokines, chemokines and their receptors]". Postepy Biochem. 53 (1): 37–45. PMID 17718386.