Ubiquitin-like modifier involved in formation of autophagosomal vacuoles. Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. In response to cellular stress and upon mitochondria fission, binds C-18 ceramides and anchors autophagolysosomes to outer mitochondrial membranes to eliminate damaged mitochondria. While LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation.
Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade components of the extracellular matrix (ECM) and play essential roles in various physiological processes such as morphogenesis, differentiation, angiogenesis and tissue remodeling, as well as pathological processes including inflammation, arthritis, cardiovascular diseases, pulmonary diseases and tumor invasion. Macrophage metalloelastase, also known as Matrix metalloproteinase-12, Macrophage elastase, MMP12, and MMP-12, is a secreted protein which belongs to thepeptidase M10A family. MMP12 is a macrophage-secreted elastase that is highly induced in the liver and lung in response to S. mansoni eggs and contains four hemopexin-like domains. MMP12 is a proteolytic enzyme responsible for cleavage of plasminogen to angiotensin, which has an angiostatic effect. It may be involved in tissue injury and remodeling and has significant elastolytic activity. It may be related to prognosis in breast cancer patients. MMP12 promotes fibrosis by limiting the expression of specific ECM-degrading MMPs. Like MMP12, MMP13 expression is highly dependent on IL-13 and type II-IL-4 receptor signaling. MMP12 is a potent proinflammatory and oncogenic molecule. MMP12 up-regulation plays a critical role in emphysema to lung cancer transition that is facilitated by inflammation.
Matrix metalloproteinases (MMPs) are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix (ECM). MMP-16 (MT3-MMP) is found in brain, lung, placenta, smooth muscle cells, and malignant tumor tissues including oral melanoma and renal carcinoma . MMP-16 has been shown to activate proMMP-2 and degrade various ECM components including native collagens. MMP-16 has been proposed to possess the potential to directly enhance the growth and invasiveness of cells in vivo, two critical processes for development and carcinogenesis . Structurally, MMP-16 consists of the following domains: a pro domain containing the furin cleavage site, a catalytic domain containing the zinc-binding site, a hinge region, a hemopexin-like domain, a transmembrane domain, and a cytoplamasic tail . The structure of the catalytic domain in complex with a hydroxamate inhibitor has been solved . The rhMMP-16PC consists of the pro and catalytic domains, which can be activated by treatment with furin.
MMP-19 (Matrix metalloprotease 19, also MMP-18 and MMP RASI) is a 55-59 kDa member of the peptidase M10A family of enzymes. It is widely expressed, being secreted by stratum basale keratinocytes, smooth muscle cells, epiphysial cartilage chondrocytes and monocytes/macrophages. MMP-19 has multiple substrates, including components of the basement membrane (type IV collagen, laminin, nidogen), fibronectin, aggrecan plus COMP, and IGFBP3, this latter cleavage resulting in the release of active IGF-I. Studies involving MMP-19 demonstrate an antiangiogenic function. This is attributable to the processing of plasminogen, generating angiostatin-like molecules, and the creation of an environment that promotes the ECM retention of soluble VEGF.
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