Identification of a natural soluble form of the vascular endothelial growth factor receptor, FLT-1, and its heterodimerization with KDR
RL Kendall, G Wang, KA Thomas - Biochemical and biophysical research …, 1996 - Elsevier
RL Kendall, G Wang, KA Thomas
Biochemical and biophysical research communications, 1996•ElsevierA soluble form of the vascular endothelial growth factor (VEGF) receptor FLT-1 was
identified in conditioned culture medium of human umbilical vein endothelial cells. The
endogenous soluble FLT-1 (sFLT-1) receptor is chromatographically and immunologically
similar to recombinant human sFLT-1 and binds [125I] VEGF with a comparable high affinity.
Human sFLT-1 is shown to form a VEGF-stabilized complex with the extracellular domain of
KDRin vitro, suggesting that not only full-length receptors are capable of forming ligand …
identified in conditioned culture medium of human umbilical vein endothelial cells. The
endogenous soluble FLT-1 (sFLT-1) receptor is chromatographically and immunologically
similar to recombinant human sFLT-1 and binds [125I] VEGF with a comparable high affinity.
Human sFLT-1 is shown to form a VEGF-stabilized complex with the extracellular domain of
KDRin vitro, suggesting that not only full-length receptors are capable of forming ligand …
A soluble form of the vascular endothelial growth factor (VEGF) receptor FLT-1 was identified in conditioned culture medium of human umbilical vein endothelial cells. The endogenous soluble FLT-1 (sFLT-1) receptor is chromatographically and immunologically similar to recombinant human sFLT-1 and binds [125I]VEGF with a comparable high affinity. Human sFLT-1 is shown to form a VEGF-stabilized complex with the extracellular domain of KDRin vitro,suggesting that not only full-length receptors are capable of forming ligand-induced heterodimeric complexes but also sFLT-1 can form a dominant negative complex with the mitogenically competent full-length KDR receptor.
Elsevier