2016
DOI: 10.4103/2348-1471.171916
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Matrix metalloproteinases: A double edge sword

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“…MMPs are a family of enzymes and 23 types have been described in humans. They are dependent on calcium and zinc for activity and are characterized by having four domains in their composition: the peptide-signal domain, the propeptide domain (composed of cysteine with its sulfhydryl groups), a catalytic domain (with zinc at the site of catalytic activity together with histidine and calcium residues), and a hemopexin-type domain that serves to bind to the substrate and which is the site where specific tissue inhibitors bind [30] (Figure 3).…”
Section: Methodsmentioning
confidence: 99%
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“…MMPs are a family of enzymes and 23 types have been described in humans. They are dependent on calcium and zinc for activity and are characterized by having four domains in their composition: the peptide-signal domain, the propeptide domain (composed of cysteine with its sulfhydryl groups), a catalytic domain (with zinc at the site of catalytic activity together with histidine and calcium residues), and a hemopexin-type domain that serves to bind to the substrate and which is the site where specific tissue inhibitors bind [30] (Figure 3).…”
Section: Methodsmentioning
confidence: 99%
“…MMPs can be activated in vivo by proteases and other MMPs, in vitro by chemical agents such as modifiers of the sulfhydryl groups, chaotropic agents, and reactive oxygen, as well as physical agents such as low pH and heat [30, 34, 39].…”
Section: Methodsmentioning
confidence: 99%