%0 Journal Article %1 Wu.2009 %A Wu, F. T. %A Stefanini, M. O. %A Mac, Gabhann F. %A Popel, A. S. %D 2009 %J PLoS.One. %K A Binding Biological Biology Capillaries Dimerization Endothelial Factor Growth Human Humans Ligands Lymphatic Models Muscle Plasma Receptor-1 Research Skeletal States Systems Tyrosine United Vascular Vessels metabolism physiology protein therapy ultrastructure %N 4 %P e5108 %T A compartment model of VEGF distribution in humans in the presence of soluble VEGF receptor-1 acting as a ligand trap %U PM:19352513 %V 4 %X Vascular endothelial growth factor (VEGF), through its activation of cell surface receptor tyrosine kinases including VEGFR1 and VEGFR2, is a vital regulator of stimulatory and inhibitory processes that keep angiogenesis--new capillary growth from existing microvasculature--at a dynamic balance in normal physiology. Soluble VEGF receptor-1 (sVEGFR1)--a naturally-occurring truncated version of VEGFR1 lacking the transmembrane and intracellular signaling domains--has been postulated to exert inhibitory effects on angiogenic signaling via two mechanisms: direct sequestration of angiogenic ligands such as VEGF; or dominant-negative heterodimerization with surface VEGFRs. In pre-clinical studies, sVEGFR1 gene and protein therapy have demonstrated efficacy in inhibiting tumor angiogenesis; while in clinical studies, sVEGFR1 has shown utility as a diagnostic or prognostic marker in a widening array of angiogenesis-dependent diseases. Here we developed a novel computational multi-tissue model

@article{Wu.2009, abstract = {Vascular endothelial growth factor (VEGF), through its activation of cell surface receptor tyrosine kinases including VEGFR1 and VEGFR2, is a vital regulator of stimulatory and inhibitory processes that keep angiogenesis--new capillary growth from existing microvasculature--at a dynamic balance in normal physiology. Soluble VEGF receptor-1 (sVEGFR1)--a naturally-occurring truncated version of VEGFR1 lacking the transmembrane and intracellular signaling domains--has been postulated to exert inhibitory effects on angiogenic signaling via two mechanisms: direct sequestration of angiogenic ligands such as VEGF; or dominant-negative heterodimerization with surface VEGFRs. In pre-clinical studies, sVEGFR1 gene and protein therapy have demonstrated efficacy in inhibiting tumor angiogenesis; while in clinical studies, sVEGFR1 has shown utility as a diagnostic or prognostic marker in a widening array of angiogenesis-dependent diseases. Here we developed a novel computational multi-tissue model }, added-at = {2010-02-05T11:28:39.000+0100}, author = {Wu, F. T. and Stefanini, M. O. and Mac, Gabhann F. and Popel, A. S.}, biburl = {https://www.bibsonomy.org/bibtex/27cd562128bbe2ee505432fc38695f843/kanefendt}, interhash = {63a9bf148b1e41b806e899e1ce0918a9}, intrahash = {7cd562128bbe2ee505432fc38695f843}, journal = {PLoS.One.}, keywords = {A Binding Biological Biology Capillaries Dimerization Endothelial Factor Growth Human Humans Ligands Lymphatic Models Muscle Plasma Receptor-1 Research Skeletal States Systems Tyrosine United Vascular Vessels metabolism physiology protein therapy ultrastructure}, number = 4, pages = {e5108}, timestamp = {2010-02-05T11:28:53.000+0100}, title = {A compartment model of VEGF distribution in humans in the presence of soluble VEGF receptor-1 acting as a ligand trap}, url = {PM:19352513}, volume = 4, year = 2009 }