matrix metalloproteinase


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matrix metalloproteinase

endopeptidase subfamily that hydrolyze extracellular proteins, especially collagens and elastin. By regulating the integrity and composition of the extracellular matrix, these enzymes play a pivotal role in the control of signals elicited by matrix molecules that regulate cell proliferation, differentiation, and death.

matrix metalloproteinase

A family of 25 zinc-dependent extracellular endopeptidases, which differ widely in substrate preferences (e.g., collagens, elastins, proteoglycans). MMPs are often present in disease and development; they are critical to tissue remodeling and expressed in certain malignancies, intimately linked to invasion and metastasis, an activity which is specifically blocked by tissue inhibitors of metalloproteinases (TIMPs). MMPs are also linked to tissue damage in interstitial lung disease, diffuse alveolar damage, and pulmonary lymphangioleiomyomatosis. MMPs are either secreted or membrane-bound (MT-MMPs) and anchored to the cell membrane by transmembrane and intracytoplasmic domains.

Matrix metalloproteinases
• Collagenases—digest triple-helical fibrillar collagens, major components of bone and cartilage. Members: MMP-1, MMP-8, MMP-13, MMP-18, MMP-14, MMP-2 (list differs from MESH, see there).

• Gelatinases—Digest type IV collagen and gelatin. Members: MMP-2, MMP-9.

• Stromelysins—Digest extracellular matrix proteins but not triple-helical collagens. Members: MMP-3, MMP-10, MMP-11.

• Membrane-type MMPs have a furin cleavage site (which is also seen in MMP-11, a stromelysin). Members: MMP-14 to MMP-17, MMP-24, MMP-25.

ma·trix me·tal·lo·pro·tein·ase

(mā'triksmĕ-tal'ō-prō'tē-nās)
A subfamily of endopeptidases that hydrolyze extracellular proteins, especially collagens and elastin. By regulating the integrity and composition of the extracellular matrix, these enzymes play a pivotal role in the control of signals elicited by matrix molecules that regulate cell proliferation, differentiation, and death.
References in periodicals archive ?
Matrix components are regulated by matrix metalloproteinases (MMPs) such as MMP2, MMP9 (9).
Current mechanistic insights into the roles of matrix metalloproteinases in tumour invasion and metastasis.
[12.] Chaussain-Miller C1, Fioretti F, Goldberg M, Menashi S (2006) The role of matrix metalloproteinases (MMPs) in human caries, Journal of Dental Research 85:22-32.
Matrix metalloproteinases are vital in the invasive and metastatic properties of cancer cells, and their expression (particularly MMP-2 and MMP-9) is promoted in a range of carcinomas (Deryugina and Quigley, 2006).
Matrix metalloproteinases: evolution, gene regulation and functional analysis in mouse models.
Nagase, "Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure function, and biochemistry," Circulation Research, vol.
Inflammatory cytokines are potent activators of matrix metalloproteinases (MMPs) which belong to a family of endopeptidases with proteolytic activity.
Inoki et al., "Brevican is degraded by matrix metalloproteinases and aggrecanase-1 (ADAMTS4) at different sites," The Journal of Biological Chemistry, vol.
Campbell, "Regulation of matrix metalloproteinases and their inhibitor genes in lipopolysaccharide-induced endotoxemia in mice," The American Journal of Pathology, vol.
ECM and basal membrane destruction by matrix metalloproteinases (MMPs), the zinc dependent endopeptidases, are important steps for tumor invasion and metastasis.
Harper et al., "Temporal study of the activity of matrix metalloproteinases and their endogenous inhibitors during wound healing," Journal of Cellular Biochemistry, vol.

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