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.
References in periodicals archive ?
In addition to regulation by proinflammatory cytokines, both intracellular catalytic and noncatalytic actions of MMPs, such as MMP-7, also contribute to inflammatory response, leading to cell death [39].
MMP-7 has been shown to be upregulated in the lungs in IPF, particularly in alveolar macrophages and hyperplastic epithelial cells [10].
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).
Grupo Colagenases MMP Nome enzimatico MMP-1 Colagenase intersticial MMP-8 Neutrofilo colagenase MMP-13 Colagenase-3 Gelatinases MMP-2 Gelatinase A MMP-9 Gelatinase B Estromalisinas MMP-3 Estromalisina-1 MMP-10 Estromalisina-2 MMP-11 Estromalisina-3 MMPs tipo MMP-14 MT1-MMP membrana MMP-16 MT3-MMP MMP-17 MT4-MMP MMP-24 MT5-MMP MMP-25 MT6-MMP Outras MMP-7 Matrilisina MMP-26 Matrilisina-2 MMP-12 Macrofago metaloelastase
It achieved this by reducing the expression of MMP-1, MMP-2, and MMP-7, by blocking MAPK signaling by inhibiting the phosphorylation of ERIC and p38 MAPK, by inhibition of AP-1 activation, and by inducing focal adhesion formation and modulating vinculin localization and expression.
MMP-7 is a member of the MMP gene family, which is currently composed of 23 members in humans.
MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP12, and MMP-13 were simultaneously measured using the Fluorokine MultiAnalyte Profiling assays (R&D Systems) on a Luminex 100 Bioanalyzer (Luminex.
MMP-7 promotes prostate cancer-induced osteolysis via the solubilization of RANKL.
The overexpression of MMP-7, MMP-10, and MMP-12 in colon cancer patients' sera correlates with a dismal prognosis [7] and high serum MMP-1 level showed a trend for short overall survival in non-small cell lung cancer patients [8].
MMP-7 is secreted as a precursor (pro-MMP-7) that is activated by 4-aminophenylmercuric acetate and trypsin in a stepwise manner (17).
Similar to MMP-9, MMP-7 is produced in vulnerable regions of the atherosclerotic plaque; however, MMP-7 has a distribution that is distinct from that of MMP-9 in the lesions and also differs in substrate specificity (18).