Abstract
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.
MeSH terms
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Amino Acid Sequence
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Biopolymers
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Cells, Cultured
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Humans
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Molecular Sequence Data
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Protein Binding
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Proto-Oncogene Proteins / chemistry*
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Proto-Oncogene Proteins / genetics
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Proto-Oncogene Proteins / metabolism
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Receptor Protein-Tyrosine Kinases / chemistry*
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Receptor Protein-Tyrosine Kinases / genetics
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Receptor Protein-Tyrosine Kinases / metabolism
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Receptors, Growth Factor / chemistry*
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Receptors, Growth Factor / genetics
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Receptors, Growth Factor / metabolism
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Receptors, Vascular Endothelial Growth Factor
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Vascular Endothelial Growth Factor Receptor-1
Substances
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Biopolymers
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Proto-Oncogene Proteins
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Receptors, Growth Factor
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Recombinant Proteins
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Receptor Protein-Tyrosine Kinases
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Receptors, Vascular Endothelial Growth Factor
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Vascular Endothelial Growth Factor Receptor-1