Refers to a multi-gene family of zinc-depended endopeptidases which have the ability to degrade almost every component of the extracellular matrix.
Matrix metalloproteinases are divided into subclasses: collagenases, gelatinases, stromelysins, and matrilysins.
Several MMPs that degrade extracellular matrix are associated with tumor growth, and angiogenesis.
Malignant cells overexpress proteases and/or can induce expression of these enzymes in neighboring cells, degrading the basement membrane and invading surrounding tissues.
Extracellular matrix proteolytic activity is required for cancer cells to invade nearby blood vessels, and then extravasate to invade distant tissue to form a new metastatic site.
MMP-3, and MMP can cleave E-cadherin and release soluble E-cadherin and disrupts cell cell interactions leading to disruption of cell adhesion and increase in cellular migration.
MMPs may alter epithelial cells into mesenchymal cells, manifesting a transition of to
a metastatic process.
Matrix metalloproteinases (MMPs) are enzymes that modify or degrade the extracellular matrix.
MMPs may modulate immunity and inflammation during tumorigenesis.
MMPs may cleave cytokines, cytokine receptors and chemokines.
MMP-7 is required to release tumor necrosis factor-alpha from its membrane bound form.
MMP-9 expression is upregulated in neutrophils, macrophages and lymphocytes and may play a role in tumor associated inflammation.
Its activity can be inhibited by endogenous inhibitors known as tissue inhibitors of metalloproteases (TIMPs).