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Biochem Biophys Res Commun. 1996 Sep 13;226(2):324-8.

Identification of a natural soluble form of the vascular endothelial growth factor receptor, FLT-1, and its heterodimerization with KDR.

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Department of Pharmacology, Merck Research Laboratories, West Point, Pennsylvania 19486, USA.


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 KDR in 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.

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