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Vascular Endothelial Growth Factor Receptor

Vascular Endothelial Growth Factor Receptors (VEGFRs) are a family of receptor tyrosine kinases that mediate the biological effects of vascular endothelial growth factors (VEGFs).
These receptors play a cruitcal role in angiogenesis, lymphangiogenesis, and vascular permeability.
VEGFRs are expressed on the surface of endothelial cells and are activated upon binding to their respective VEGF ligands.
This activation triggers downstream signaling cascades that regulate essential cellular processes such as cell proliferation, survival, migration, and differentiation.
Understanding the complex biology of VEGFRs is crucial for developing targeted therapies for vascular diseases, cancer, and other disorders with aberrant angiogenesis.

Most cited protocols related to «Vascular Endothelial Growth Factor Receptor»

Most of the parameters for the anti-VEGF agent were taken from published data on bevacizumab. We assume a half-life of 21 days (4 (link)) for the anti-VEGF whether unbound or bound to VEGF121 or VEGF165, as bound and free bevacizumab exhibit the same pharmacokinetic profile (9 (link)). Kinetic parameters (kon, koff) for the binding and unbinding of the anti-VEGF to the vascular endothelial growth factor were taken to be 9.2 × 104 M-1·s-1 and 2.0 × 10-4 s-1 respectively, leading to a dissociation constant Kd of 2.2 nM (17 (link)).
Experiments have shown that bevacizumab may have multimeric binding to VEGF (9 (link), 18 (link)) and can bind to extracellular matrix-sequestered VEGF (19 (link)). For simplicity purposes, we limit our model to monomeric binding to VEGF and neglect binding to VEGF sequestered by the extracellular matrix; these can be included when quantification of binding sites and the kinetics become available. Bevacizumab has also been reported to alter the VEGF-dependent microvascular permeability to soluble molecules (20 (link)). As a first approximation, we assume that the geometry of each tissue and the capillary density remain constant in the course of our simulations, i.e., we do not include tissue remodeling after the injection of the anti-VEGF agent. Although it may be important, the inclusion of tissue remodeling would take the model beyond the scope of this study but could be of interest for further studies. This model does not include VEGF receptors on the luminal side of endothelial cells that have not been experimentally characterized, but we have recently shown how such expression would alter the VEGF distribution (21 (link)).
Note that the simulations are not aimed at representing a particular type or stage of cancer, recognizing that VEGF-neutralizing agents may be administered in cases of both metastatic and primary tumors. Thus, in the model the tumor compartment can represent either an aggregate volume of metastases or a primary tumor. Due to the wide range of possibilities that could be represented for different types and stages of cancer, we adopt the parameters for this compartment from our previous study (16 (link)) and conduct a sensitivity study to ascertain that our qualitative conclusions are not dependent on the choice of parameters.
For each simulation, the system was first equilibrated at a baseline for a cancer patient with tumor before the injection of the VEGF-neutralizing agent. At time zero, intravenous infusion of the anti-VEGF agent begins and delivery to the blood compartment continues as a slow infusion for 90 minutes. We considered two treatment regimens: a single-dose treatment of 10 mg/kg or 10 consecutive daily doses of 1 mg/kg (metronomic therapy).
The parameters and their assigned numerical values are summarized in Supplement 3. The equations governing the three-compartment VEGF transport system have been described in our previous papers (16 (link), 21 (link)) and can be found in Supplement 1. We have also added equations to describe the interactions and inter-compartmental transport of the anti-VEGF molecule (Equations (S.30) to (S.38)).
Publication 2010
Bevacizumab Binding Sites BLOOD Capillaries Dietary Supplements Endothelial Cells Extracellular Matrix Hypersensitivity Intravenous Infusion Kinetics Malignant Neoplasms Neoplasm Metastasis Neoplasms Obstetric Delivery Patients Permeability, Microvascular Phenobarbital Staging, Cancer Therapeutics Tissues Treatment Protocols vascular endothelial growth factor-165 Vascular Endothelial Growth Factor Receptor Vascular Endothelial Growth Factors VEGF protein, human

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Publication 2009
Alleles Base Pairing Blood Vessel Cells Chimera Deletion Mutation Embryo Endothelium Exons Mutagenesis Plasmids RNA, Messenger Transposase Vascular Endothelial Growth Factor Receptor Vertebral Column Zebrafish Zinc Finger Nucleases
The hemangiosarcoma cell lines Frog, Tucker, Dal-4, Joey, and DD-1 (Table 1) were cultured as described previously [23] (link). Veronica and Emma cell lines were developed as described [23] (link) from splenic and a metastatic brain hemangiosarcomas, respectively, both from Golden Retrievers. For VEGFR inhibition, cells were cultured in the presence of small molecules that selectively inhibit VEGFR kinase (VEGF Receptor Tyrosine Kinase Inhibitor II, N-(4-Chlorophenyl)-2-[(pyridin-4-ylmethyl)amino]benzamid, hereafter called “Drug 1”; VEGFR Tyrosine Kinase Inhibitor III, KRN633, N-(2-Chloro-4-((6,7-dimethoxy-4-quinazolinyl)oxy)phenyl)-N′-propylurea, hereafter called “Drug 2”; or VEGF Receptor Kinase Inhibitor IV, 3-(3-Thienyl)-6-(4-methoxyphenyl)pyrazolo[1,5-a]pyrimidine, hereafter called “Drug 3”). The half maximal inhibitory concentrations for VEGFR1 and VEGFR2 for Drugs 1, 2, and 3, respectively are 180 and 20, 170 and 160, and 1.9 and 19. Cells (10,000/well) were plated in duplicate in 96-well microtiter plates and allowed to attach for 16 hr prior to addition of inhibitors over a concentration range from 1 pM to 1 µM. Cells were then cultured for 72 hr, and the number of viable cells was determined using the MTS assay (Promega, Madison, WI). Absorption at 490 nm for each well was averaged, and data normalized to % viability where the mean of wells that received no treatment (0 nm) was considered = 1. The results show the means of two independent experiments for each cell line.
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Publication 2009
Biological Assay Brain Cardiac Arrest Cell Lines Cells Hemangiosarcoma inhibitors KRN 633 Pharmaceutical Preparations Phosphotransferases Promega propylurea Psychological Inhibition Pyrimidines Rana Spleen Vascular Endothelial Growth Factor Receptor Vascular Endothelial Growth Factor Receptor-1 Vascular Endothelial Growth Factor Receptor-2 Veronica
Frozen medullary tissue was isolated, and standard Western blotting protocols were performed by pulverizing and homogenizing it in chilled protein extraction buffer. The lysate was used for immunoblotting against swine specific antibodies for vascular endothelial growth factor (VEGF) (dilution 1∶200), VEGF receptor (FLK-1) (dilution 1∶200), hypoxia-inducible factor (HIF)-1α (dilution 1∶500), NAD(P)H-oxidase p47 (dilution 1∶200), matrix metalloproteinase (MMP)-2 (dilution 1∶500), IL-10 (dilution 1∶500), and tumor necrosis factor (TNF)-α (dilution 1∶200), to investigate mechanisms involved in renal neovascularization, tubular oxygen consumption, fibrogenesis and inflammation. GAPDH served as a loading control, except for MMP-2 expression, which was quantified by normalizing the active to pro-MMP.
Renal vascularization, fibrosis and inflammation mediators were also quantified in 5 µm slides stained for H&E, trichrome, CD68, CD163+ macrophages, Arginase (Arg)-1 (a marker of trophic M2 macrophages) and monocyte chemotactic protein (MCP)-1, and oxidative stress in 30 µm dihydroethidium (DHE) stained slides. Medullary capillaries, tubules and neutrophils were counted at 100× magnification in H&E stained slides using an ApoTome microscope (Carl ZEISS SMT, Oberkochen, Germany). Capillaries were identified by the presence of lumen, red blood cells and/or an endothelial cell lining, and the ratio of capillary number to tubules was calculated [25] (link). In addition, microvascular density was assessed by immunoreactivity of von Willebrand factor (vWF) in colorimetric stained slides. Tubular injury was scored on a 1–5 scale (1: <10%, 2∶10–25%, 3∶26–50%, 4∶51–75% and 5: >75% injury) using 40× H&E slides based on tubular dilation, atrophy, cast formation, sloughing tubular endothelial cells or thickening basement membrane [26] (link).
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Publication 2013
Antibodies arginase-1, human Atrophy Buffers Capillaries CD3EAP protein, human CD163 protein, human Colorimetry dihydroethidium Dilatation Endothelial Cells Endothelium Erythrocytes Factor VIII-Related Antigen Fibrosis Freezing GAPDH protein, human HIF1A protein, human IL10 protein, human Inflammation Inflammation Mediators Injuries Kidney Macrophage Matrix Metalloproteinase 2 Matrix Metalloproteinases Medulla Oblongata Membrane, Basement Microscopy Monocyte Chemoattractant Protein-1 NADPH Oxidase Neutrophil Oxidative Stress Oxygen Consumption Pathologic Neovascularization Pigs Proteins Technique, Dilution Tissues Tumor Necrosis Factor-alpha Vascular Endothelial Growth Factor Receptor vascular endothelial growth factor receptor-2, human Vascular Endothelial Growth Factors
The basis of this mouse model is the human model developed by Stefanini and co-workers that was used to explore the VEGF distributions in humans in health and disease [8] (link), [18] (link), [19] (link), [21] (link); the model is significantly expanded as explained below. The mouse is divided into the blood compartment and tissue compartment (Figure 1). As an approximation, the tissue compartment is represented by skeletal muscle that comprises the majority of its mass (43% of total body mass [22] (link)). To build the tissue compartment, the skeletal muscle is represented as cylindrical fibers (myocytes) aligned in parallel with cylindrical microvessels dispersed between the muscle fibers. The space between the muscle fibers and microvessels is designated as the interstitial space, which is itself composed of the basement membranes of the parenchymal cells/myocytes (PBM) and endothelial cells (EBM), in addition to the extracellular matrix (ECM). VEGF is secreted by the myocytes into the interstitial space where it can bind to VEGF receptors VEGFR-1, VEGFR-2, and NRP-1 on the abluminal surface of the endothelial cells, as well as to glycosaminoglycan chains (GAG) in the basement membranes and extracellular matrix. The binding of VEGF to NRP-1 on the surface of the myocytes is also included. VEGF can be transported to the blood via the lymphatics at a rate kL and can be exchanged between the blood and interstitium via microvascular permeability at a rate kp. VEGF in the blood can bind to receptors on the luminal surface of the endothelial cells and can be removed via plasma clearance at a rate cV. Receptors and VEGF/receptor complexes can be internalized at a rate kint.Figure 2 summarizes the molecular interactions of VEGF120 and VEGF164 with their receptors and with GAG chains in the PBM, EBM, and ECM.
In our model, we include an anti-VEGF agent that can bind to and form a complex with VEGF in both the blood and tissue. The unbound anti-VEGF agent and the complex are also subject to intercompartmental transport via permeability and lymphatic drainage, and can also be cleared from the blood. The molecular interactions between the two VEGF isoforms and the anti-VEGF agent are illustrated in Figure 2.
We incorporate pore theory in modeling the interstitial space to reflect the available volume for VEGF to diffuse. The VEGF molecules are free to diffuse in the available interstitial fluid volume, denoted KAV, which is defined as the available fluid volume (UAV) divided by the total tissue volume (U). Based on the geometry of the pores in the basement membranes and extracellular matrix, the partition coefficient and available fluid volume can be calculated as follows:




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Publication 2011
BLOOD Drainage Endothelial Cells Extracellular Matrix FLT1 protein, human Glycosaminoglycans Homo sapiens Human Body Interstitial Fluid Membrane, Basement Microvessels Mus Muscle Cells Muscle Tissue Permeability Permeability, Microvascular Phenobarbital Plasma Plasma Membrane Protein Isoforms Skeletal Muscles Tissues Vascular Endothelial Growth Factor Receptor Vascular Endothelial Growth Factor Receptor-1 Vascular Endothelial Growth Factor Receptor-2 Vascular Endothelial Growth Factors VEGF165 protein, human Vessel, Lymphatic Workers

Most recents protocols related to «Vascular Endothelial Growth Factor Receptor»

All animal experiments were approved by the Institutional Animal Care and Use Committee at Acceleron Pharma Inc., a subsidiary of Merck & Co., Inc., Rahway, NJ, USA and performed in accordance with the guidelines from the NIH Guide for the Care and Use of Laboratory Animals. Male C57BL/6 mice (10 weeks old, Jackson Laboratory) were used for TAC and MI models as described (18 (link), 22 (link)), and male Balb/c mice (10 weeks old, Jackson Laboratory) were used for the prolonged TAC model to establish PH. Male obese ZSF1 rats (8 and 23 weeks old) and their lean littermates (Charles River, Wilmington, MA, USA) were used for the PH-HFpEF study. PH was established by a single subcutaneous injection of a vascular endothelial growth factor receptor antagonist, Sugen 5416 (SU5416, 100 mg/kg; Cayman), suspended in CMC buffer (0.5% sodium carboxymethyl cellulose, 0.4% polysorbate 80, 0.9% sodium chloride, and 0.9% benzyl alcohol) (23 (link), 24 (link)). Animals were euthanized in all experiments by heart and lung removal en bloc according to AVMA guidelines.
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Publication 2023
Animals Animals, Laboratory Benzyl Alcohol Buffers Caimans Heart Institutional Animal Care and Use Committees Lung Males Mice, Inbred BALB C Mice, Inbred C57BL Obesity Polysorbate 80 Rattus norvegicus Rivers Sodium Carboxymethylcellulose Sodium Chloride SU 5416 Vascular Endothelial Growth Factor Receptor
The cells were harvested using trypsin-EDTA (0.25%) and centrifuged. Total RNA was extracted using the RNeasy Plus Mini Kit (Qiagen, Germany), following the manufacturer’s instructions. Next, cDNA was generated using a Veriti thermal cycler (Applied Biosystems). Real-time quantitative PCR was performed with cDNA supplemented with the appropriate TaqMan primers using a StepOnePlus PCR system (Applied Biosystems). mRNA expression level was calculated using the 2-ΔΔCT method. The primers used are as follows; VEGF (vascular endothelial growth factor) (Hs00900055_m1), VEGFR (VEGF receptor) (FLT1; Hs01052961_m1), IL-31 (Hs01098710_m1), IL-33 (Hs00369211_m1), TGF-β (Hs00998133_m1), TNF-α (Hs00174128_m1), IL-1β (Hs01555410_m1), and GAPDH (Hs02786624_g1).
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Publication 2023
Cells DNA, Complementary Edetic Acid FLT1 protein, human GAPDH protein, human IL31 protein, human IL33 protein, human Interleukin-1 beta Oligonucleotide Primers Real-Time Polymerase Chain Reaction RNA, Messenger Transforming Growth Factor beta Trypsin Tumor Necrosis Factor-alpha Vascular Endothelial Growth Factor Receptor Vascular Endothelial Growth Factors
All animal care and procedures were approved by French Animal Experimentation Ethics Committees and performed in accordance with the guidelines from the French National Research Council for the Care and Use of Laboratory Animals (permit numbers: Apafis #24107 and #11920). Experiments were performed in 10-week-old male wild-type Sprague–Dawley rats (Janvier Labs) rats. Male rats were used to minimize hormonal effects (e.g., estrogen). Rats received a single subcutaneous administration of the VEGF receptor antagonist SU5416 (20 mg/kg) and were then exposed to hypoxia (10% FiO2) for 3 weeks [12 (link),13 (link)]. Then, these rats returned to normoxia (21% FiO2) for 5 additional weeks before evaluation. Inhibition of sEH was achieved in SuHx rats using the oral administration of 1-trifluoromethoxyphenyl-3-(1-propionylpiperidin-4-yl) urea (TPPU; 5 mg/L in drinking water/PEG400, 99:1, v/v). TPPU treatment was started 5 weeks post-SU5416 injection and went on for 3 weeks. TPPU was provided by C.M. for the study. High in vivo exposure and sEH inhibitory potency, in particular at the cardiac level, of TPPU have already been shown at the dose of 5 mg/L of drinking water in adult male Sprague–Dawley rats [14 (link)]. Normoxic rats receiving vehicle or TPPU served as controls.
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Publication 2023
Administration, Oral Adult Animal Ethics Committees Animals Animals, Laboratory Estrogens Heart Hypoxia Males polyethylene glycol 400 Psychological Inhibition Rats, Sprague-Dawley Rattus norvegicus SU 5416 Urea Vascular Endothelial Growth Factor Receptor

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Publication 2023
alexa fluor 488 Antibodies Biopharmaceuticals Cell Nucleus Cornea endothelial PAS domain protein 1, human Equus asinus HIF1A protein, human Immunoglobulins Microscopy Mus Novus Paraffin Embedding Propidium Iodide Rabbits Thrombospondin 1 Tissues Vascular Endothelial Growth Factor Receptor Vascular Endothelial Growth Factors

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Publication 2023
beta-Actin Chemiluminescence endothelial PAS domain protein 1, human Gels Glycine HIF1A protein, human Immunoglobulins Methanol Phenobarbital polyvinylidene fluoride Proteins SDS-PAGE Thrombospondin 1 Tissue, Membrane Tromethamine Vascular Endothelial Growth Factor Receptor Vascular Endothelial Growth Factors

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More about "Vascular Endothelial Growth Factor Receptor"

Vascular Endothelial Growth Factor Receptors (VEGFRs) are a family of receptor tyrosine kinases that play a critical role in regulating angiogenesis, lymphangiogenesis, and vascular permeability.
These receptors, expressed on the surface of endothelial cells, bind to their respective Vascular Endothelial Growth Factor (VEGF) ligands, triggering downstream signaling cascades that control essential cellular processes such as proliferation, survival, migration, and differentiation.
Understanding the complex biology of VEGFRs is crucial for developing targeted therapies for a wide range of diseases, including vascular disorders, cancer, and other conditions associated with aberrant angiogenesis.
Researchers often utilize DMSO, ELISA kits, and FBS to study VEGFR-related signaling pathways and cellular responses.
Additionally, compounds like SU5416 and Axitinib have been extensively studied for their ability to inhibit VEGFR activity and suppress angiogenesis in preclinical models, including Sprague-Dawley rats.
Cutting-edge technologies, such as confocal microscopy and Whatman Nucleopore Track-Etch Membranes, have enabled scientists to visualize and analyze the localization, internalization, and trafficking of VEGFRs within endothelial cells.
By leveraging these advanced tools and techniques, researchers can gain deeper insights into the complex mechanisms underlying VEGFR function and uncover new therapeutic targets for a wide range of diseases.