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
%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
}