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 (mĭ-tăl′ə-prōt′n-ās′, -āz′, -prō′tē-nās′, -nāz′)
Any of a group of proteolytic enzymes whose catalytic activity depends on the presence of a metal ion in the active site, especially any of those (called "matrix metalloproteinases") that degrade proteins in the extracellular matrix.
References in periodicals archive ?
Wang et al., "The cysteine-rich domain of snake venom metalloproteinases is a ligand for von Willebrand factor A domains: Role in substrate targeting," The Journal of Biological Chemistry, vol.
In this paper we explore the literature regarding the pathophysiology of myocardial IRI, focusing on the possible role of the calpain system, oxidative-nitrosative stress, and matrix metalloproteinases. We discuss these mechanisms within the broad scenario of IRI, also discussing the medicolegal issues related to sudden deaths occurring during the acute phase of myocardial infarct following reperfusion interventions.
Strenuous exercise induces an increase in the pro-inflammatory cytokines.1 The production of inflammatory and pro-inflammatory mediators2 and matrix metalloproteinases (MMPs)3 are increased during exercise activity.
The dentin becomes increasingly exposed in advanced stages and exposes the organic matrix to breakdown by host-derived enzymes, such as matrix metalloproteinases (MMPs) present in dentin and saliva.
Matrix Metalloproteinases (MMPs) may fall into this category of both useful markers and targets in CKD disease.
Only a few studies have reported alterations in urine levels of matrix metalloproteinases and tissue inhibitor of metalloproteinases in patients with type 1 diabetes mellitus and these studies have conflicting results.
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).
[1.] Nagase H, Visse R, Murphy G (2006) Structure and function of matrix metalloproteinases and TIMPs.
Matrix metalloproteinases (MMPs), extracellular-degrading proteases, contribute to metastatic and invasive cancer cells properties; their expression (particularly MMP-9 and MMP-2) is increased in carcinomas (Stamenkovic, 2000) MMPs activity can be specically inhibited by a group of structurally related, endogenous inhibitors known as tissue inhibitors of metalloproteases (TIMPs) (Al-Olayan et al., 2014).
Tryptase activates thrombin receptors and the zymogen forms of metalloproteinases (MMPs), including collagenase, gelatinase, and stromelysin, and degrades fibronectin, vitronectin, and neuropeptides, thus promoting arterial dissection and thrombosis.
Matrix metalloproteinases: evolution, gene regulation and functional analysis in mouse models.
ECM and basal membrane destruction by matrix metalloproteinases (MMPs), the zinc dependent endopeptidases, are important steps for tumor invasion and metastasis.
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