Hepatocyte Growth Factor/Scatter Factor Binds with High Affinity to Dermatan Sulfate
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چکیده
منابع مشابه
Structure of a dermatan sulfate hexasaccharide that binds to heparin cofactor II with high affinity.
Dermatan sulfate increases the rate of inhibition of thrombin by heparin cofactor II (HCII) approximately 1000-fold by providing a catalytic template to which both the inhibitor and the protease bind. Dermatan sulfate is a linear polymer of D-glucuronic acid (GlcA) or L-iduronic acid (IdoA) alternating with N-acetyl-D-galactosamine (GalNAc) residues. Heterogeneity in dermatan sulfate results fr...
متن کاملHepatocyte growth factor interacts with both heparan and dermatan sulphates, in addition to its specific signalling
Hepatocyte growth factor/scatter factor (HGF/SF) is a 90 kDa paracrine factor synthesised by mesenchymal cells. In the extracellular milieu it is proteolytically clipped, yielding a disulphide-linked heterodimer (60 kDa α chain and 30 kDa β chain). The mature processed molecule is biologically active upon epithelial and endothelial cells, and also haemopoietic progenitor cells, and appears to h...
متن کاملHepatocyte growth factor/scatter factor and its interaction with heparan sulphate and dermatan sulphate.
Hepatocyte growth factor (HGF)/scatter factor (SF) is a unique growth factor, in that it binds both heparan sulphate (HS) and dermatan sulphate (DS). The sequences in HS and DS that specifically interact with and modulate HGF/SF activity have not yet been fully identified. Ascidian DS, which uniquely possesses O-sulphation at C-6 (and not C-4) of its N -acetylgalactosamine unit, was analysed fo...
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Select epidermal growth factor (EGF)-like (EGFL) repeats of human tenascin cytotactin (tenascin C) can stimulate EGF receptor (EGFR) signaling, but activation requires micromolar concentrations of soluble EGFL repeats in contrast to subnanomolar concentrations of classical growth factors such as EGF. Using in silico homology modeling techniques, we generated a structure for one such repeat, the...
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Thrombospondin-1 (TSP1) is a secreted trimeric glycoprotein of 450 kDa with demonstrated effects on cell growth, adhesion and migration. Its complex biological activity is attributed to its ability to bind to cell-surface receptors, growth factors and extracellular-matrix proteins. In this study, we used a (125)I solid-phase binding assay to demonstrate that TSP1 binds specifically to proteins ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1998
ISSN: 0021-9258
DOI: 10.1074/jbc.273.1.271