VEGFR-1-mediated cell adhesion was divalent cation-dependent, and inhibited by antibodies directed against the α5β1 integrin. In adhesion assays, VEGFR-1 extracellular region specifically promoted endothelial cell attachment. In this study, we report that the secreted VEGFR-1 is present within the extracellular matrix deposited by endothelial cells in culture, suggesting a possible involvement in endothelial cell adhesion and migration. ![]() The role of this variant has not yet been completely defined. ![]() Endothelial cells express a membrane-spanning form of VEGFR-1 and secrete a soluble variant of the receptor comprising only the extracellular region. Vascular endothelial growth factor receptor-1 (VEGFR-1) is a tyrosine kinase receptor for several growth factors of the VEGF family.
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