%0 Journal Article %1 Roeckl.1998 %A Roeckl, W. %A Hecht, D. %A Sztajer, H. %A Waltenberger, J. %A Yayon, A. %A Weich, H. A. %D 1998 %J Exp.Cell Res. %K & A Agents Animals BALB Binding C Cell Cells Cloning Competitive Cross-Linking Dimerization Endothelial Expression Factor Factors Fibrinolytic Gene Growth Heparin Human Humans Inbred Kinase Kinases Ligands Lymphokines Mice Mitogens Molecular Plastics Proliferation Protein Protein-Tyrosine Proteins Proto-Oncogene Reagents Receptor Receptor-1 Receptors Research Solubility Tyrosine Vascular antagonists cells drug effects genetics inhibitors isolation metabolism pharmacology protein purification %N 1 %P 161-170 %T Differential binding characteristics and cellular inhibition by soluble VEGF receptors 1 and 2 %U PM:9633524 %V 241 %X The FLT-1 and KDR genes encode transmembrane tyrosine kinases which function as high-affinity receptors for vascular endothelial growth factor (VEGF). We have used the baculovirus system to express the extracellular parts of the FLT-1 receptor and KDR receptor in soluble form (sFLT-1 and sKDR), for in vitro binding and competition assays. Here, we show that the binding of VEGF165 to sKDR but not sFLT-1 is dependent on heparin, regardless of whether VEGF165 or sKDR is immobilized. Further, only sFLT-1 acts as a receptor antagonist in solution and sKDR can neither compete with the binding of VEGF165 to human endothelial cells carrying both receptors nor block VEGF165 induced mitogenicity. Soluble KDR only partially inhibits cell migration even at high concentrations, in contrast to sFLT which can almost completely block (82%) VEGF-induced cell proliferation and migration. Taken together these results show that the two soluble VEGF receptor proteins, sFLT-1 and sKDR, despite binding the s

@article{Roeckl.1998, abstract = {The FLT-1 and KDR genes encode transmembrane tyrosine kinases which function as high-affinity receptors for vascular endothelial growth factor (VEGF). We have used the baculovirus system to express the extracellular parts of the FLT-1 receptor and KDR receptor in soluble form (sFLT-1 and sKDR), for in vitro binding and competition assays. Here, we show that the binding of VEGF165 to sKDR but not sFLT-1 is dependent on heparin, regardless of whether VEGF165 or sKDR is immobilized. Further, only sFLT-1 acts as a receptor antagonist in solution and sKDR can neither compete with the binding of VEGF165 to human endothelial cells carrying both receptors nor block VEGF165 induced mitogenicity. Soluble KDR only partially inhibits cell migration even at high concentrations, in contrast to sFLT which can almost completely block (82%) VEGF-induced cell proliferation and migration. Taken together these results show that the two soluble VEGF receptor proteins, sFLT-1 and sKDR, despite binding the s}, added-at = {2010-02-05T11:28:39.000+0100}, author = {Roeckl, W. and Hecht, D. and Sztajer, H. and Waltenberger, J. and Yayon, A. and Weich, H. A.}, biburl = {https://www.bibsonomy.org/bibtex/211302e187b42bf0097d4086be4612438/kanefendt}, interhash = {b4acf1d774ac58fcba7660385b51a70a}, intrahash = {11302e187b42bf0097d4086be4612438}, journal = {Exp.Cell Res.}, keywords = {& A Agents Animals BALB Binding C Cell Cells Cloning Competitive Cross-Linking Dimerization Endothelial Expression Factor Factors Fibrinolytic Gene Growth Heparin Human Humans Inbred Kinase Kinases Ligands Lymphokines Mice Mitogens Molecular Plastics Proliferation Protein Protein-Tyrosine Proteins Proto-Oncogene Reagents Receptor Receptor-1 Receptors Research Solubility Tyrosine Vascular antagonists cells drug effects genetics inhibitors isolation metabolism pharmacology protein purification}, number = 1, pages = {161-170}, timestamp = {2010-02-05T11:28:46.000+0100}, title = {Differential binding characteristics and cellular inhibition by soluble VEGF receptors 1 and 2}, url = {PM:9633524}, volume = 241, year = 1998 }