Utilization of Distinct Signaling Pathways by Receptors for Vascular Endothelial Cell Growth Factor and Other Mitogens in the Induction of Endothelial Cell Proliferation
Li Wha Wu,Lindsey D. Mayo,James D. Dunbar,Kelly M. Kessler,Melinda R. Baerwald,Eric A. Jaffe,Dongfang Wang,Robert S. Warren,David B. Donner +8 more
TLDR
Two-hybrid cloning and immunoprecipitation from human umbilical vein endothelial cells (HUVEC) showed that KDR binds to and promotes the tyrosine phosphorylation of phospholipase Cγ (PLCγ), indicating that K DR is uniquely important to PLCγ activation in HUVEC.About:
This article is published in Journal of Biological Chemistry.The article was published on 2000-02-18 and is currently open access. It has received 297 citations till now. The article focuses on the topics: Kinase insert domain receptor & Tyrosine phosphorylation.read more
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Vascular endothelial growth factor: basic science and clinical progress.
TL;DR: Vascular endothelial growth factor (VEGF) is an endothelial cell-specific mitogen in vitro and an angiogenic inducer in a variety of in vivo models and is implicated in intraocular neovascularization associated with diabetic retinopathy and age-related macular degeneration.
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FGF and VEGF function in angiogenesis: signalling pathways, biological responses and therapeutic inhibition.
TL;DR: The current knowledge of FGF- and VEGF-induced signal transduction that leads to specific biological responses will be summarized and the manner in which this knowledge is being exploited to regulate angiogenesis will be discussed.
Journal ArticleDOI
Protein kinase C and other diacylglycerol effectors in cancer
Erin Griner,Marcelo G. Kazanietz +1 more
TL;DR: The challenge is faced of dissecting the relative contribution of each DAG signal to cancer progression and identifying the main targets of phorbol-ester tumour promoters and small G-protein regulators.
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Vascular Endothelial Growth Factor Expression of Intercellular Adhesion Molecule 1 (ICAM-1), Vascular Cell Adhesion Molecule 1 (VCAM-1), and E-selectin through Nuclear Factor-κB Activation in Endothelial Cells
TL;DR: Vascular endothelial growth factor induces adhesion molecules on endothelial cells during inflammation through two signal transduction pathways that have opposite functions in the induction of adhesion molecule expression, and VEGF-stimulated expression was mainly through NF-κB activation with PI 3′-kinase-mediated suppression but was independent of nitric oxide and MEK.
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Oxidant Signaling in Vascular Cell Growth, Death, and Survival A Review of the Roles of Reactive Oxygen Species in Smooth Muscle and Endothelial Cell Mitogenic and Apoptotic Signaling
TL;DR: A fuller understanding of how ROS regulate mitogenesis and apoptosis in vascular smooth muscle and endothelial cells will permit the development of novel strategies to modify or prevent vascular diseases in which these phenotypes predominate.
References
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Journal Article
Flt-1 but not KDR/Flk-1 tyrosine kinase is a receptor for placenta growth factor, which is related to vascular endothelial growth factor
TL;DR: Reverse transcription-PCR showed that PIGF-2, a subtype of P IGF-1 that bears a basic amino acid-rich domain, is more abundant than PIGf-1 and thus is the major subtype in human placenta, suggesting that the weak biological activities of PigF are due to its use of only part of the available VEGF signaling.
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The phosphorylated 1169-tyrosine containing region of flt-1 kinase (VEGFR-1) is a major binding site for PLCgamma.
TL;DR: Results strongly suggest that Tyr-1169 on Flt-1 is a major binding site for PLCgamma and important for FlT-1 signal transduction within the cell.
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Identification of Vascular Endothelial Growth Factor Receptor-1 Tyrosine Phosphorylation Sites and Binding of SH2 Domain-containing Molecules
TL;DR: 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.
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Interaction of the Flt-1 Tyrosine Kinase Receptor with the p85 Subunit of Phosphatidylinositol 3-Kinase MAPPING OF A NOVEL SITE INVOLVED IN BINDING
TL;DR: The interactions of the p85 regulatory subunit of phosphatidylinositol 3-kinase with the endothelium-specific Flt-1 receptor tyrosine kinase is examined using the yeast two-hybrid system and it is found that both the amino- and carboxyl-terminal SH2 domains of p85 bind to FlT-1.
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Biological activity and phosphorylation sites of the bacterially expressed cytosolic domain of the KDR VEGF-receptor
TL;DR: Using peptide mapping and sequencing of peptides, four tyrosine residues that are phosphorylated corresponding to residues 951, 996, 1054, and 1059 of the KDR protein are identified and suggest they may be identical to the phosphorylation sites of KDR in mammalian cells.