MMP7

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MMP7

A gene on chromosome 11q21-q22 that encodes matrix metalloproteinase 7, which degrades proteoglycans, fibronectin, elastin and casein and activates procollagenase. It is involved in breaking down the extracellular matrix in physiological processes—e.g., embryonic development, reproduction, tissue remodelling and wound healing. It differs from most MMP family members as it lacks a conserved C-terminal protein domain.
 
Molecular pathology
Defects in MMP7 have been linked to arthritis and metastasis.
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References in periodicals archive ?
Matrix metalloproteinases (MMPs) are special class of proteases that are categorized in five groups as per their substrate specificity: collagenases (MMP-1, -8 and -13), gelatinases (MMP-2 and -9), stromelysins (MMP-3, -10, and -11), matrilysins (MMP-7) and membrane-type (MMP-14 to -17, -24 and -25).
Excessive matrix metalloproteinase-7 (MMP-7) expression has been reported in various premalignant and malignant tumors of the gastrointestinal system, especially in cancers of the esophagus (4), gastric (5), colon (6), and pancreas (7).
Twenty-four MMPs have been identified, including collagenases (MMP-1, 8, 13, and 18), gelatinases (MMP-2 and 9), stromelysins (MMP-3 and 10), matrilisins (MMP-7 and 26), and membrane-type MMPs (MMP-14, 15, 16, 17, 24, and 25), among other types.
Depending on the substrate specificity and structure, MMPs are divided into several subgroups: collagenases (e.g., MMP-1), gelatinases (e.g., MMP-2 and MMP-9), stromelysins (e.g., MMP-3 and MMP-10), matrilysins (e.g., MMP-7 and MMP-26), and membrane-type matrix metalloproteinase-1 (MT1-MMP).
Known as matrilysin-1, MMP-7 is the smallest member in the MMP family.
Among the MMPs, MMP-7, known as matrilysin, has a broad spectrum of proteolytic activity capable of cleaving various types of extracellular matrix [15].
By using this methodology, no appreciable bands either compatible with MMP-3 or MMP-7 molecular weights were revealed in supernatant samples of cultures derived from MDE and healthy areas (data not shown).
We aimed to investigate the clinical characteristics of anetoderma patients and to correlate these findings with immunohistochemical changes in the MMPs that most effectively degrade elastic tissue (MMP-2, MMP-7, MMP-9, and MMP-12) and their physiologic inhibitors (TIMP-1 and TIMP-2) [14, 16].
MMP-7 is another metalloproteinase that has a broad substrate specificity for ECM proteins including gelatin and type IV collagen, while MMP-12 is a key macrophage-derived enzyme that has a role in adipose tissue remodeling [5, 6].
Matrilysins (MMP-7 and MMP26) are the smallest members of the family that lack the hemopexin-like domain.
Incluyen tambien la MMP-3, -10 y -11, el grupo de matrilisinas que carece del dominio de hemopexina y al cual pertenecen la MMP-7 y -26 (31,32).