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Vascular endothelial growth factor (VEGF) signal transduction through the cell surface receptors, VEGFR1 and VEGFR2, regulates angiogenesis–the growth of new capillaries from pre-existent microvasculature. Soluble VEGF receptor-1 (sVEGFR1), a non-signaling truncated variant of VEGFR1, has been postulated to inhibit angiogenic signaling via direct sequestration of VEGF ligands, or dominant-negative heterodimerization with surface VEGFRs. The relative contributions of these two mechanisms to sVEGFR1’s purported anti-angiogenic effects in vivo are currently unknown. We previously developed a computational model for predicting the compartmental distributions of VEGF and sVEGFR1 throughout the healthy human body, by simulating the molecular interaction networks of the VEGF ligand-receptor system, as well as intercompartmental macromolecular biotransport processes. In this study, we decipher …