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Vascular endothelial growth factor A (VEGF-A), vascular endothelial growth factor B (VEGF-B), and placenta growth factor (PlGF) are closely related, secreted proteins in the VEGF family, which exert their biological effects by binding and activating specific receptor tyrosine kinases (VEGFR-1 and VEGFR-2) and co-receptors (neuropilin-1 and -2) on endothelial and other cells[1][2][3][4][5]. VEGF-A is the principal factor for physiological and pathological angiogenesis, is essential for embryonic development, and tightly regulated by hypoxic and growth-signaling pathways[2][4]. VEGF-B is important for vessel survival but induces weaker angiogenic signaling; its role is less well-defined than VEGF-A[2][4]. PlGF is specific for VEGFR-1, participates in vascular development, inflammation, and pathological angiogenesis, especially in pregnancy and some disease states[3][4]. Therapeutic inhibition of these factors or their receptors is a major strategy in the treatment of cancer, retinopathies, and other diseases driven by excessive vessel growth or permeability[4][5].
Neutralization of ligand (blocking VEGF or PlGF from receptor binding); Inhibition of receptor tyrosine kinase activity; Competitive antagonism at VEGFR or NRP co-receptor
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