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- W80930611 abstract "SummaryHepatocyte Growth Factor and Scatter Factor are indistinguishable factors (HGF/SF) secreted by mesodermal cells and acting on epithelial cells. HGF/SF stimulates mitogenesis, cell motility and dissociation of epithelial sheets, it promotes matrix invasion and is considered a major mediator of liver regeneration in vivo. HGF/SF is a potent angiogenic factor in vivo and in vitro induces endothelial cells to proliferate and migrate. HGF/SF is secreted as a single-chain biologically inactive precursor (pro-HGF/SF) and maturation into the active aβ heterodimer results from a proteolytic cleavage by urokinase which acts as a pro-HGF/SF convertase. HGF/SF is the ligand for p190 MET , the receptor tyrosine kinase encoded by the MET proto-oncogene. This is sustained by following evidence: (1) it binds to immunopurified p190 MET , (2)the chemical cross-linking of the radiolabelled ligand, (3) HGF/SF-induced tyrosine phosphorylation of p190 MET and (4) the reconstitution of high-affinity binding sites for HGF/SF into insect ceUs infected with a recombinant baculovirus carrying the human MET cDNA, The structure of p190 MET consists of a heterodimer of two (α, β) disulfide-linked protein subunits. The α subunit is solely extracellular, while the β subunit contains an extracellular portion involved in ligand binding, a transmembrane domain, and a cytoplasmic tyrosine kinase domain bearing phosphorylation sites which regulate its activity. The mature p190 MET results from glycosylation and proteolytic cleavage of the precursor of 170 kDa. Alternative post-transcriptional processing originates two truncated Met proteins, endowed with ligand binding activity and lacking the cytoplasmic kinase domain of the β subunit. Only one form is soluble and released from the cells. The interaction of HGF/SF with p190 MET in intact cells stimulates tyrosine autophosphorylation of the receptor β subunit. The autophosphorylation of the receptor upregulates its kinase activity. The tyrosine kinase activity of the receptor is downmodulated by PKC activity and also the rise of intracellular Ca2+. The signal transduction pathways of the target cells are also stimulated by the autophosphorylation of the HGF/SF receptor β subunit. The phosphorylated receptor associates rasGAP, phospholipase C-γ, and src-related tyrosine kinase in vitro. Phosphosphatidylinositol 3-kinase associates autophosphorylated p190 MET in vitro and in vivo, indicating that the generation of the D-3 phosphorylated inositol lipids is involved in effecting the motility and/or the growth response to HGF/SF." @default.
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- W80930611 date "1993-01-01" @default.
- W80930611 modified "2023-09-27" @default.
- W80930611 title "Structure, Biosynthesis and Biochemical Properties of the HGF/SF Receptor" @default.
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- W80930611 doi "https://doi.org/10.1007/978-3-0348-5663-8_6" @default.
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