Matrix metalloproteinases (MMPs) are neutral proteinases that are involved in the breakdown and remodeling of the extracellular matrix (ECM) under a variety of physiological and pathological conditions , such as morphogenesis , differentiation , angiogenesis , and tissue remodeling , as well as pathological processes including inflammation , arthritis , cardiovascular diseases , pulmonary diseases , and tumor invasion. MMP9 , also known as 92-kDa gelatinase B/type IV collagenase , is secreted from neutrophils , macrophages , and some transformed cells , and is the most complex family member in terms of domain structure and regulation of its activity. It plays an important role in tissue remodeling in normal and pathological inflammatory processes. MMP-9 is a major secretion product of macrophages and a component of cytoplasmic granules of neutrophils and is particularly important in the pathogenesis of inflammatory , infectious , and neoplastic diseases in many organs including the lung. This enzyme is also secreted by lymphocytes and stromal cells upon stimulation by inflammatory cytokines , or upon delivery of bi-directional activation signals following integrin-mediated cell-cell or cell-extracellular matrix (ECM) contacts. Since the integrity of the tissue architecture is closely dependent on the delicate balance between MMPs and their inhibitors , excessive production of MMP-9 is linked to tissue damage and degenerative inflammatory disorders. As a consequence , regulation of gene transcription and tissue-specific expression of MMP-9 in normal and diseased states are being actively investigated to pave the way for new therapeutic targets. Besides , the dramatic overexpression of MMP-9 in cancer and various inflammatory conditions points to the molecular mechanisms controlling its expression as a potential target for eventual rational therapeutic intervention.
Matrix metallopeptidase 9 (MMP-9) is an enzyme encoded by the MMP9 gene. This protein, which is produced by normal alveolar macrophages and granulocytes, can be activated by 4-aminophenylmercuric acetate and phorbol ester and up-regulated by ARHGEF4, SPATA13 and APC via the JNK signaling pathway in colorectal tumor cells. MMP-9 is involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, angiogenesis, bone development, wound healing, cell migration, learning and memory, as well as in pathological processes, such as arthritis, intracerebral hemorrhage, and metastasis.
Matrix metalloproteinases (MMPs) are neutral proteinases that are involved in the breakdown and remodeling of the extracellular matrix (ECM) under a variety of physiological and pathological conditions, such as morphogenesis, differentiation, angiogenesis and tissue remodeling, as well as pathological processes including inflammation, arthritis, cardiovascular diseases, pulmonary diseases and tumor invasion. MMP9, also known as 92-kDa gelatinase B/type IV collagenase, is secreted from neutrophils, macrophages, and a number of transformed cells, and is the most complex family member in terms of domain structure and regulation of its activity. It plays an important role in tissue remodelling in normal and pathological inflammatory processes. MMP-9 is a major secretion product of macrophages and a component of cytoplasmic granules of neutrophils, and is particularly important in the pathogenesis of inflammatory, infectious, and neoplastic diseases in many organs including the lung. This enzyme is also secreted by lymphocytes and stromal cells upon stimulation by inflammatory cytokines, or upon delivery of bi-directional activation signals following integrin-mediated cell-cell or cell-extracellular matrix (ECM) contacts. The dramatic overexpression of MMP-9 in cancer and various inflammatory conditions clearly points to the molecular mechanisms controlling its expression as a potential target for eventual rational therapeutic intervention.
MOB Kinase Activator 1A (MOB1A) belongs to the MOB1/phocein family, which acts as an activator of LATS1/2 in the Hippo signaling pathway, plays a key role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. MOBKL1B stimulates the kinase activity of STK38 and STK38L. MOBKL1B binds to and regulate downstream targets such as the NDR-family protein kinases and LATS1 kinase.
MOB-Like Protein Phocein is a member of the MOB1/Phocein Family. MOB-Like Protein Phocein is associated with membranes and the Golgi stacks. It is present in the cytosol, where it behaves as a protein complex. It has been shown that MOB-Like Protein Phocein interacts with DNM1, EPS15 and Nucleoside Diphosphate Kinase. MOB-Like Protein Phocein is the major partner of Striatin Family members and may play a important role in membrane trafficking, specifically in membrane budding reactions.
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