Identification of Vascular Endothelial Growth Factor Receptor-1 Tyrosine Phosphorylation Sites and Binding of SH2 Domain-containing Molecules
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TLDR
A spectrum of already known as well as novel phosphotyrosine-binding molecules are involved in signal transduction by Flt-1, and SHP-2, phospholipase C-γ, and Grb2 could also be shown to bind to the intact FlT-1 intracellular domain.About:
This article is published in Journal of Biological Chemistry.The article was published on 1998-09-04 and is currently open access. It has received 127 citations till now. The article focuses on the topics: Vascular endothelial growth factor B & Vascular endothelial growth factor A.read more
Citations
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VEGF receptor signalling - in control of vascular function.
TL;DR: Recent insights have shed light onto VEGFR signal transduction and the interplay between different V EGFRs and VEGF co-receptors in development, adult physiology and disease.
Journal ArticleDOI
Vascular Endothelial Growth Factor and Angiogenesis
Ann Hoeben,Bart Landuyt,Martin Highley,Hans Wildiers,Allan T. van Oosterom,Ernst A. de Bruijn +5 more
TL;DR: The role of V EGF in physiological and pathological processes is reviewed and how modulation of VEGF expression creates new therapeutic possibilities is discussed.
Journal ArticleDOI
Signal Transduction by Vascular Endothelial Growth Factor Receptors
Sina Koch,Lena Claesson-Welsh +1 more
TL;DR: This review outlines the current information on VEGF signal transduction in relation to blood and lymphatic vessel biology and develops treatments to halt blood vessel formation, angiogenesis in diseases that involve tissue growth and inflammation, such as cancer.
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Signal transduction by VEGF receptors in regulation of angiogenesis and lymphangiogenesis
TL;DR: The VEGF/VPF ligands and receptors are crucial regulators of vasculogenesis, angiogenesis, lymphangiogenesis and vascular permeability in vertebrates and mapping the signaling system of these important receptors may provide the knowledge necessary to suppress specific signaling pathways in major human diseases.
Journal ArticleDOI
Mechanisms and regulation of endothelial VEGF receptor signalling
TL;DR: A clear understanding of the tight and multi-level regulation of VEGFR2 signalling is key to successful therapeutic suppression or stimulation of vascular growth.
References
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Signal transduction by receptors with tyrosine kinase activity
Axel Ullrich,Joseph Schlessinger +1 more
TL;DR: Cet article synthese montre comment des recepteurs membranaires a activite tyrosine kinase peuvent etre impliques dans la transduction and notamment jouent le role de signal de the transduction.
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Vascular endothelial growth factor induced by hypoxia may mediate hypoxia-initiated angiogenesis.
TL;DR: It is shown that vascular endothelial growth factor (VEGF) probably functions as a hypoxia-inducible angiogenic factor and is specifically induced in a subset of glioblastoma cells distinguished by their immediate proximity to necrotic foci and the clustering of capillaries alongside VEGF-producing cells.
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Failure of blood-island formation and vasculogenesis in Flk-1-deficient mice.
Fouad Shalaby,Janet Rossant,Janet Rossant,Terry P. Yamaguchi,Terry P. Yamaguchi,Marina Gertsenstein,Xiang-Fu Wu,Xiang-Fu Wu,Martin L. Breitman,Martin L. Breitman,Andre C. Schuh +10 more
TL;DR: The generation of mice deficient in Flk-1 by disruption of the gene using homologous recombination in embryonic stem (ES) cells is reported, indicating that FlK-1 is essential for yolk-sac blood-island formation and vasculogenesis in the mouse embryo.
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Vascular Endothelial Growth Factor in Ocular Fluid of Patients with Diabetic Retinopathy and Other Retinal Disorders
Lloyd Paul Aiello,Robert L. Avery,Paul G. Arrigg,B A Keyt,Henry D. Jampel,Sweta Shah,Louis R. Pasquale,Hagen Thieme,Mami Iwamoto,John Edward Park +9 more
TL;DR: The data suggest that VEGF plays a major part in mediating active intraocular neovascularization in patients with ischemic retinal diseases, such as diabetic retinopathy and retinal-vein occlusion.
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SH2 domains recognize specific phosphopeptide sequences
Songyang Zhou,Songyang Zhou,Steven E. Shoelson,Manas Chaudhuri,Gerald D. Gish,Tony Pawson,Wayne G. Haser,Frederick J. King,Thomas M. Roberts,Sheldon Ratnofsky,Robert J. Lechleider,Benjamin G. Neel,Raymond B. Birge,J. Eduardo Fajardo,Margaret M. Chou,Hidesaburo Hanafusa,Brian Schaffhausen,Lewis C. Cantley +17 more
TL;DR: The variability in SH2 domain sequences at likely sites of contact provides a structural basis for the phosphopeptide selectivity of these families.