HCSGD entry for VEGFA
1. General information
Official gene symbol | VEGFA |
---|---|
Entrez ID | 7422 |
Gene full name | vascular endothelial growth factor A |
Other gene symbols | MVCD1 VEGF VPF |
Links to Entrez Gene | Links to Entrez Gene |
2. Neighbors in the network

3. Gene ontology annotation
GO ID | GO term | Evidence | Category |
---|---|---|---|
GO:0000122 | Negative regulation of transcription from RNA polymerase II promoter | IDA | biological_process |
GO:0001525 | Angiogenesis | IDA | biological_process |
GO:0001541 | Ovarian follicle development | IEA ISS | biological_process |
GO:0001569 | Patterning of blood vessels | IEA ISS | biological_process |
GO:0001570 | Vasculogenesis | TAS | biological_process |
GO:0001666 | Response to hypoxia | IDA IEA | biological_process |
GO:0001701 | In utero embryonic development | IEA ISS | biological_process |
GO:0001822 | Kidney development | IEA ISS | biological_process |
GO:0001934 | Positive regulation of protein phosphorylation | IDA | biological_process |
GO:0001938 | Positive regulation of endothelial cell proliferation | IDA ISS | biological_process |
GO:0001968 | Fibronectin binding | IDA | molecular_function |
GO:0001974 | Blood vessel remodeling | IEA | biological_process |
GO:0002042 | Cell migration involved in sprouting angiogenesis | IDA | biological_process |
GO:0002052 | Positive regulation of neuroblast proliferation | IEA ISS | biological_process |
GO:0002053 | Positive regulation of mesenchymal cell proliferation | IEA ISS | biological_process |
GO:0002092 | Positive regulation of receptor internalization | IDA | biological_process |
GO:0002575 | Basophil chemotaxis | IDA | biological_process |
GO:0002576 | Platelet degranulation | TAS | biological_process |
GO:0002687 | Positive regulation of leukocyte migration | TAS | biological_process |
GO:0003007 | Heart morphogenesis | ISS | biological_process |
GO:0003151 | Outflow tract morphogenesis | IEA ISS | biological_process |
GO:0003169 | Coronary vein morphogenesis | IEA ISS | biological_process |
GO:0005125 | Cytokine activity | IDA ISS | molecular_function |
GO:0005161 | Platelet-derived growth factor receptor binding | IPI | molecular_function |
GO:0005172 | Vascular endothelial growth factor receptor binding | IPI | molecular_function |
GO:0005515 | Protein binding | IPI | molecular_function |
GO:0005576 | Extracellular region | TAS | cellular_component |
GO:0005578 | Proteinaceous extracellular matrix | NAS | cellular_component |
GO:0005604 | Basement membrane | IEA | cellular_component |
GO:0005615 | Extracellular space | IDA IEA ISS | cellular_component |
GO:0005737 | Cytoplasm | IDA IEA | cellular_component |
GO:0006357 | Regulation of transcription from RNA polymerase II promoter | IMP | biological_process |
GO:0007399 | Nervous system development | TAS | biological_process |
GO:0007498 | Mesoderm development | IEA ISS | biological_process |
GO:0007595 | Lactation | IEA ISS | biological_process |
GO:0007596 | Blood coagulation | TAS | biological_process |
GO:0008083 | Growth factor activity | IDA IEA ISS | molecular_function |
GO:0008201 | Heparin binding | IDA IEA IMP | molecular_function |
GO:0008283 | Cell proliferation | IEA | biological_process |
GO:0008284 | Positive regulation of cell proliferation | IDA | biological_process |
GO:0008360 | Regulation of cell shape | IDA | biological_process |
GO:0009409 | Response to cold | IEA | biological_process |
GO:0009986 | Cell surface | IDA | cellular_component |
GO:0010469 | Regulation of receptor activity | IPI | biological_process |
GO:0010595 | Positive regulation of endothelial cell migration | IDA | biological_process |
GO:0010628 | Positive regulation of gene expression | IDA | biological_process |
GO:0016020 | Membrane | IEA | cellular_component |
GO:0030141 | Secretory granule | IDA | cellular_component |
GO:0030168 | Platelet activation | TAS | biological_process |
GO:0030212 | Hyaluronan metabolic process | IEA | biological_process |
GO:0030224 | Monocyte differentiation | IDA | biological_process |
GO:0030225 | Macrophage differentiation | IDA | biological_process |
GO:0030324 | Lung development | ISS | biological_process |
GO:0030335 | Positive regulation of cell migration | IDA | biological_process |
GO:0030855 | Epithelial cell differentiation | IEA ISS | biological_process |
GO:0030949 | Positive regulation of vascular endothelial growth factor receptor signaling pathway | IDA | biological_process |
GO:0031077 | Post-embryonic camera-type eye development | IEA ISS | biological_process |
GO:0031093 | Platelet alpha granule lumen | TAS | cellular_component |
GO:0031334 | Positive regulation of protein complex assembly | IDA | biological_process |
GO:0031954 | Positive regulation of protein autophosphorylation | IDA | biological_process |
GO:0031988 | Membrane-bounded vesicle | IEA | cellular_component |
GO:0032147 | Activation of protein kinase activity | IDA | biological_process |
GO:0032793 | Positive regulation of CREB transcription factor activity | IDA | biological_process |
GO:0033138 | Positive regulation of peptidyl-serine phosphorylation | IDA | biological_process |
GO:0035148 | Tube formation | IDA | biological_process |
GO:0035767 | Endothelial cell chemotaxis | IDA | biological_process |
GO:0035924 | Cellular response to vascular endothelial growth factor stimulus | IDA | biological_process |
GO:0036303 | Lymph vessel morphogenesis | IEA ISS | biological_process |
GO:0038033 | Positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway | IDA | biological_process |
GO:0038084 | Vascular endothelial growth factor signaling pathway | IEA | biological_process |
GO:0038091 | Positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway | IDA | biological_process |
GO:0038190 | VEGF-activated neuropilin signaling pathway | ISS | biological_process |
GO:0040007 | Growth | IEA ISS | biological_process |
GO:0042056 | Chemoattractant activity | IDA | molecular_function |
GO:0042088 | T-helper 1 type immune response | IEA | biological_process |
GO:0042462 | Eye photoreceptor cell development | IEA ISS | biological_process |
GO:0042802 | Identical protein binding | IPI | molecular_function |
GO:0042803 | Protein homodimerization activity | IEA ISS | molecular_function |
GO:0043066 | Negative regulation of apoptotic process | IMP | biological_process |
GO:0043117 | Positive regulation of vascular permeability | IDA IEA | biological_process |
GO:0043129 | Surfactant homeostasis | IEA ISS | biological_process |
GO:0043154 | Negative regulation of cysteine-type endopeptidase activity involved in apoptotic process | IDA | biological_process |
GO:0043183 | Vascular endothelial growth factor receptor 1 binding | IPI | molecular_function |
GO:0043184 | Vascular endothelial growth factor receptor 2 binding | IPI | molecular_function |
GO:0043406 | Positive regulation of MAP kinase activity | IDA | biological_process |
GO:0043524 | Negative regulation of neuron apoptotic process | IEA | biological_process |
GO:0043536 | Positive regulation of blood vessel endothelial cell migration | IDA | biological_process |
GO:0045766 | Positive regulation of angiogenesis | IDA IEA IMP | biological_process |
GO:0045779 | Negative regulation of bone resorption | IEA | biological_process |
GO:0045785 | Positive regulation of cell adhesion | IDA | biological_process |
GO:0045944 | Positive regulation of transcription from RNA polymerase II promoter | IDA IEA IMP | biological_process |
GO:0046982 | Protein heterodimerization activity | IDA | molecular_function |
GO:0048010 | Vascular endothelial growth factor receptor signaling pathway | IDA IEA TAS | biological_process |
GO:0048018 | Receptor agonist activity | IPI | molecular_function |
GO:0048255 | MRNA stabilization | IEA | biological_process |
GO:0048286 | Lung alveolus development | IEA | biological_process |
GO:0048469 | Cell maturation | IEA ISS | biological_process |
GO:0048593 | Camera-type eye morphogenesis | IEA ISS | biological_process |
GO:0048661 | Positive regulation of smooth muscle cell proliferation | IEA | biological_process |
GO:0048739 | Cardiac muscle fiber development | IEA ISS | biological_process |
GO:0048754 | Branching morphogenesis of an epithelial tube | ISS | biological_process |
GO:0048842 | Positive regulation of axon extension involved in axon guidance | IEA ISS | biological_process |
GO:0048844 | Artery morphogenesis | ISS | biological_process |
GO:0050679 | Positive regulation of epithelial cell proliferation | IEA ISS | biological_process |
GO:0050731 | Positive regulation of peptidyl-tyrosine phosphorylation | IDA | biological_process |
GO:0050840 | Extracellular matrix binding | IC | molecular_function |
GO:0050918 | Positive chemotaxis | IDA IEA | biological_process |
GO:0050927 | Positive regulation of positive chemotaxis | IDA | biological_process |
GO:0050930 | Induction of positive chemotaxis | IDA NAS | biological_process |
GO:0051272 | Positive regulation of cellular component movement | IDA | biological_process |
GO:0051781 | Positive regulation of cell division | IEA | biological_process |
GO:0051894 | Positive regulation of focal adhesion assembly | IDA | biological_process |
GO:0051897 | Positive regulation of protein kinase B signaling | IEA | biological_process |
GO:0060319 | Primitive erythrocyte differentiation | IEA ISS | biological_process |
GO:0060326 | Cell chemotaxis | IEA | biological_process |
GO:0060749 | Mammary gland alveolus development | IEA ISS | biological_process |
GO:0060754 | Positive regulation of mast cell chemotaxis | IDA | biological_process |
GO:0060948 | Cardiac vascular smooth muscle cell development | IEA ISS | biological_process |
GO:0060982 | Coronary artery morphogenesis | IEA ISS | biological_process |
GO:0061418 | Regulation of transcription from RNA polymerase II promoter in response to hypoxia | TAS | biological_process |
GO:0061419 | Positive regulation of transcription from RNA polymerase II promoter in response to hypoxia | IMP | biological_process |
GO:0070374 | Positive regulation of ERK1 and ERK2 cascade | IEA | biological_process |
GO:0071456 | Cellular response to hypoxia | IDA TAS | biological_process |
GO:0071542 | Dopaminergic neuron differentiation | IEA ISS | biological_process |
GO:0071679 | Commissural neuron axon guidance | IEA ISS | biological_process |
GO:0090037 | Positive regulation of protein kinase C signaling | IDA | biological_process |
GO:0090050 | Positive regulation of cell migration involved in sprouting angiogenesis | IDA | biological_process |
GO:0090190 | Positive regulation of branching involved in ureteric bud morphogenesis | IEA ISS | biological_process |
GO:0090259 | Regulation of retinal ganglion cell axon guidance | ISS | biological_process |
GO:1900086 | Positive regulation of peptidyl-tyrosine autophosphorylation | IDA | biological_process |
GO:1900745 | Positive regulation of p38MAPK cascade | IDA | biological_process |
GO:1901492 | Positive regulation of lymphangiogenesis | IEA | biological_process |
GO:1901727 | Positive regulation of histone deacetylase activity | IDA | biological_process |
GO:1902336 | Positive regulation of retinal ganglion cell axon guidance | IEA ISS | biological_process |
GO:1902533 | Positive regulation of intracellular signal transduction | IDA | biological_process |
GO:2000273 | Positive regulation of receptor activity | IPI | biological_process |
GO:2001237 | Negative regulation of extrinsic apoptotic signaling pathway | IEA | biological_process |
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4. Expression levels in datasets
- Meta-analysis result
p-value up | p-value down | FDR up | FDR down |
---|---|---|---|
0.0057335891 | 0.2935620265 | 0.1985117647 | 1.0000000000 |
- Individual experiment result
( "-" represent NA in the specific microarray platform )
( "-" represent NA in the specific microarray platform )
Data source | Up or down | Log fold change |
---|---|---|
GSE11954 | Down | -0.8309789501 |
GSE13712_SHEAR | Down | -0.4877322310 |
GSE13712_STATIC | Up | 0.1426021948 |
GSE19018 | Up | 0.2493757587 |
GSE19899_A1 | Up | 0.4527131272 |
GSE19899_A2 | Up | 1.8415313513 |
PubMed_21979375_A1 | Up | 1.8105154772 |
PubMed_21979375_A2 | Up | 0.7810819713 |
GSE35957 | Down | -1.2000703813 |
GSE36640 | Down | -1.4500966794 |
GSE54402 | Down | -0.1305501631 |
GSE9593 | Up | 0.4922266102 |
GSE43922 | Up | 1.1591433820 |
GSE24585 | Up | 0.0452844200 |
GSE37065 | Up | 0.1225939009 |
GSE28863_A1 | Up | 0.7354217700 |
GSE28863_A2 | Up | 1.1178683229 |
GSE28863_A3 | Up | 0.0268011753 |
GSE28863_A4 | Down | -0.3731714982 |
GSE48662 | Up | 0.6758711292 |
5. Regulation relationships with compounds/drugs/microRNAs
- Compounds
Compound | Target | Confidence score | Uniprot |
---|---|---|---|
CHEMBL265885 | CHEMBL1783 | 4 | P15692 |
CHEMBL382044 | CHEMBL1783 | 4 | P15692 |
CHEMBL198643 | CHEMBL1783 | 4 | P15692 |
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- Drugs
Name | Drug | Accession number |
---|---|---|
Bevacizumab | DB00112 | BTD00087 | BIOD00087 |
Minocycline | DB01017 | APRD00547 |
Gliclazide | DB01120 | APRD00460 |
Carvedilol | DB01136 | APRD00091 |
Ranibizumab | DB01270 | - |
Pyroglutamic Acid | DB03088 | EXPT00247 |
Tris | DB03754 | EXPT03072 |
ABT-510 | DB05434 | - |
VEGF-AS | DB05890 | - |
Aflibercept | DB08885 | - |
- MicroRNAs
- mirTarBase
MiRNA_name | mirBase ID | miRTarBase ID | Experiment | Support type | References (Pubmed ID) |
---|---|---|---|---|---|
hsa-miR-200b-3p | MIMAT0000318 | MIRT006440 | Luciferase reporter assay//Western blot | Functional MTI | 21544626 |
hsa-miR-373-3p | MIMAT0000726 | MIRT000721 | ELISA//Luciferase reporter assay | Functional MTI | 18320040 |
hsa-miR-302d-3p | MIMAT0000718 | MIRT000722 | ELISA//Luciferase reporter assay | Functional MTI | 18320040 |
hsa-miR-145-5p | MIMAT0000437 | MIRT006215 | Luciferase reporter assay//qRT-PCR//Western blot | Functional MTI | 22472569 |
hsa-miR-126-3p | MIMAT0000445 | MIRT003428 | Luciferase reporter assay//Reporter assay | Functional MTI | 19223090 |
hsa-miR-126-3p | MIMAT0000445 | MIRT003428 | Luciferase reporter assay//qRT-PCR//Western blot | Functional MTI | 22510476 |
hsa-miR-126-3p | MIMAT0000445 | MIRT003428 | Reporter assay;Western blot | Functional MTI | 21249429 |
hsa-miR-147a | MIMAT0000251 | MIRT003810 | ELISA//Luciferase reporter assay | Functional MTI | 18320040 |
hsa-miR-134-5p | MIMAT0000447 | MIRT003811 | ELISA//Luciferase reporter assay | Functional MTI | 18320040 |
hsa-miR-140-5p | MIMAT0000431 | MIRT003812 | ELISA//Luciferase reporter assay | Functional MTI | 18320040 |
hsa-miR-29b-3p | MIMAT0000100 | MIRT003813 | ELISA//Luciferase reporter assay | Non-Functional MTI | 18320040 |
hsa-miR-107 | MIMAT0000104 | MIRT003814 | ELISA//Luciferase reporter assay | Functional MTI | 18320040 |
hsa-miR-16-5p | MIMAT0000069 | MIRT003890 | Luciferase reporter assay//Reporter assay | Non-Functional MTI | 15131085 |
hsa-miR-16-5p | MIMAT0000069 | MIRT003890 | ELISA//Luciferase reporter assay | Functional MTI | 18320040 |
hsa-miR-16-5p | MIMAT0000069 | MIRT003890 | Luciferase reporter assay//Western blot | Functional MTI | 19144909 |
hsa-miR-16-5p | MIMAT0000069 | MIRT003890 | Luciferase reporter assay | Functional MTI | 23083510 |
hsa-miR-16-5p | MIMAT0000069 | MIRT003890 | Luciferase reporter assay//qRT-PCR//Western blot | Functional MTI | 23104180 |
hsa-miR-16-5p | MIMAT0000069 | MIRT003890 | Luciferase reporter assay | Functional MTI | 23233752 |
hsa-miR-93-5p | MIMAT0000093 | MIRT004055 | ELISA//Luciferase reporter assay | Functional MTI | 18320040 |
hsa-miR-17-5p | MIMAT0000070 | MIRT004271 | ELISA//Luciferase reporter assay | Functional MTI | 18320040 |
hsa-miR-150-5p | MIMAT0000451 | MIRT004272 | ELISA//Luciferase reporter assay | Functional MTI | 18320040 |
hsa-miR-195-5p | MIMAT0000461 | MIRT004273 | ELISA//Luciferase reporter assay | Functional MTI | 18320040 |
hsa-miR-15b-5p | MIMAT0000417 | MIRT004274 | ELISA//Luciferase reporter assay | Functional MTI | 18320040 |
hsa-miR-15a-5p | MIMAT0000068 | MIRT004275 | ELISA//Luciferase reporter assay | Functional MTI | 18320040 |
hsa-miR-15a-5p | MIMAT0000068 | MIRT004275 | Luciferase reporter assay//qRT-PCR//Western blot | Functional MTI | 23104180 |
hsa-miR-15a-5p | MIMAT0000068 | MIRT004275 | Luciferase reporter assay | Functional MTI | 23233752 |
hsa-miR-520g-3p | MIMAT0002858 | MIRT004276 | ELISA//Luciferase reporter assay | Functional MTI | 18320040 |
hsa-miR-378a-3p | MIMAT0000732 | MIRT004277 | ELISA//Luciferase reporter assay | Non-Functional MTI | 18320040 |
hsa-miR-330-3p | MIMAT0000751 | MIRT004278 | ELISA//Luciferase reporter assay | Non-Functional MTI | 18320040 |
hsa-miR-383-5p | MIMAT0000738 | MIRT004443 | ELISA//Luciferase reporter assay | Functional MTI | 18320040 |
hsa-miR-125a-5p | MIMAT0000443 | MIRT004445 | ELISA//Luciferase reporter assay | Non-Functional MTI | 18320040 |
hsa-miR-361-5p | MIMAT0000703 | MIRT004447 | ELISA//Luciferase reporter assay | Functional MTI | 18320040 |
hsa-miR-20a-5p | MIMAT0000075 | MIRT004450 | ELISA//Luciferase reporter assay | Functional MTI | 18320040 |
hsa-miR-20b-5p | MIMAT0001413 | MIRT004451 | ELISA//Luciferase reporter assay | Functional MTI | 18320040 |
hsa-miR-504-5p | MIMAT0002875 | MIRT004457 | ELISA//Luciferase reporter assay | Functional MTI | 18320040 |
hsa-miR-520h | MIMAT0002867 | MIRT004458 | ELISA//Luciferase reporter assay | Functional MTI | 18320040 |
hsa-miR-372-3p | MIMAT0000724 | MIRT004461 | ELISA//Luciferase reporter assay | Functional MTI | 18320040 |
hsa-miR-106a-5p | MIMAT0000103 | MIRT004465 | ELISA//Luciferase reporter assay | Functional MTI | 18320040 |
hsa-miR-106b-5p | MIMAT0000680 | MIRT004466 | ELISA//Luciferase reporter assay | Functional MTI | 18320040 |
hsa-miR-106b-5p | MIMAT0000680 | MIRT004466 | Microarray | Functional MTI (Weak) | 17242205 |
hsa-miR-34a-5p | MIMAT0000255 | MIRT004513 | ELISA//Luciferase reporter assay | Non-Functional MTI | 18320040 |
hsa-miR-205-5p | MIMAT0000266 | MIRT004518 | ELISA//Luciferase reporter assay | Non-Functional MTI | 18320040 |
hsa-miR-205-5p | MIMAT0000266 | MIRT004518 | Luciferase reporter assay//Reporter assay | Functional MTI | 19238171 |
hsa-miR-34b-3p | MIMAT0004676 | MIRT004519 | ELISA//Luciferase reporter assay | Non-Functional MTI | 18320040 |
hsa-miR-200c-3p | MIMAT0000617 | MIRT006771 | Luciferase reporter assay//Western blot | Functional MTI | 22569286 |
hsa-miR-503-5p | MIMAT0002874 | MIRT007224 | Luciferase reporter assay | Functional MTI | 23352645 |
hsa-miR-335-5p | MIMAT0000765 | MIRT016911 | Microarray | Functional MTI (Weak) | 18185580 |
hsa-miR-29c-3p | MIMAT0000681 | MIRT020389 | Sequencing | Functional MTI (Weak) | 20371350 |
hsa-miR-9-5p | MIMAT0000441 | MIRT021401 | qRT-PCR;Other | Non-Functional MTI (Weak) | 20173740 |
hsa-miR-133a-3p | MIMAT0000427 | MIRT021711 | Reporter assay | Non-Functional MTI | 21249429 |
hsa-miR-101-3p | MIMAT0000099 | MIRT027248 | Sequencing | Functional MTI (Weak) | 20371350 |
hsa-miR-21-5p | MIMAT0000076 | MIRT030717 | qRT-PCR | Functional MTI (Weak) | 19435867 |
hsa-miR-21-5p | MIMAT0000076 | MIRT030717 | Western blot;qRT-PCR | Functional MTI | 21544242 |
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- mirRecord
MicroRNA name | mirBase ID | Target site number | MiRNA mature ID | Test method inter | MiRNA regulation site | Reporter target site | Pubmed ID |
---|---|---|---|---|---|---|---|
hsa-miR-34a-5p | MIMAT0000255 | 1 | hsa-miR-34a | {ELISA} | {overexpression by siRNA transfection} | 18320040 | |
hsa-miR-140-5p | MIMAT0000431 | NA | hsa-miR-140-5p | {ELISA} | {overexpression by siRNA transfection} | 18320040 | |
hsa-miR-15a-5p | MIMAT0000068 | 1 | hsa-miR-15a | {ELISA} | {overexpression by siRNA transfection} | 18320040 | |
hsa-miR-16-5p | MIMAT0000069 | NA | hsa-miR-16 | {ELISA} | {overexpression by siRNA transfection} | 18320040 | |
hsa-miR-147a | MIMAT0000251 | NA | hsa-miR-147 | {ELISA} | {overexpression by siRNA transfection} | 18320040 | |
hsa-miR-520h | MIMAT0002867 | 1 | hsa-miR-520h | {ELISA} | {overexpression by siRNA transfection} | 18320040 | |
hsa-miR-205-5p | MIMAT0000266 | 1 | hsa-miR-205 | {ELISA} | {overexpression by siRNA transfection} | 18320040 | |
hsa-miR-126-3p | MIMAT0000445 | 1 | hsa-miR-126 | 19223090 | |||
hsa-miR-205-5p | MIMAT0000266 | 1 | hsa-miR-205 | 19238171 | |||
hsa-miR-126-3p | MIMAT0000445 | NA | hsa-miR-126 | {Western blot} | {endogenous} | 21249429 | |
hsa-miR-16-5p | MIMAT0000069 | 1 | hsa-miR-16 | {Western blot} | {overexpression by miRNA mimics tranfection} | 21885851 | |
hsa-miR-424-5p | MIMAT0001341 | NA | hsa-miR-424 | {Western blot} | {overexpression by miRNA mimics tranfection} | 21885851 |
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6. Text-mining results about the gene
Gene occurances in abstracts of cellular senescence-associated articles: 43 abstracts the gene occurs.
PubMed ID of the article | Sentenece the gene occurs |
---|---|
27917303 | Then, the effect of synthetic miR-146a mimetic on IL-6 and VEGF-A expression was analyzed in RPE cells treated with and without TNF-alpha |
27917303 | Overexpression of miR-146a by miRNA mimics inhibited VEGF-A and TNF-alpha-induced IL-6 expression |
27508009 | Furthermore, we confirmed that the expressions of endothelial nitric oxide synthase (eNOS), vascular endothelial growth factor (VEGF) and phosphoryl-Akt were augmented in SRT1720-treated senescent HUVECs |
27009837 | Bmi-1 knockdown by Ad-Bmi-1i downregulated VEGF via inhibiting AKT activity |
26654980 | Oxidative stress-induced premature senescence dysregulates VEGF and CFH expression in retinal pigment epithelial cells: Implications for Age-related Macular Degeneration |
26654980 | Most important, we show for the first time that senescent ARPE-19 cells upregulated vascular endothelial growth factor (VEGF) and simultaneously downregulated complement factor H (CFH) expression |
26433963 | In this report we show that senescent human peritoneal mesothelial cells (HPMCs) alter the secretory profile of ovarian cancer cells (A2780, OVCAR-3, SKOV-3) by increasing the release of four angiogenic agents: CXCL1, CXCL8, HGF, and VEGF |
26420897 | Selective coexpression of VEGF receptor 2 in EGFRvIII-positive glioblastoma cells prevents cellular senescence and contributes to their aggressive nature |
26105007 | Upon LPS treatment, SV cells also developed senescence-associated secretory phenotype (SASP), as demonstrated by the increased expression of TNFalpha, IL-1beta, IL-6, MCP-1, and VEGFalpha |
26005508 | Initial animal studies and phase I clinical trials with vascular endothelial growth factor (VEGF) or fibroblast growth factor (FGF) demonstrated promising results, inspiring scientists to progress forward |
25952632 | Under these conditions, the anti-senescence genes TERT, bFGF, VEGF, and ANG were increased, whereas the senescence-related genes ATM, p21, and p53 were decreased |
25797700 | We investigated whether vascular endothelial growth factor (VEGF) signaling via its receptor, VEGFR2, regulates senescence and proliferation of tumor cells in mice with colitis-associated cancer (CAC) |
25633211 | Pre-clinical studies and Phase I clinical trials using VEGF and fibroblast growth factor (FGF) demonstrated promising results; however, more rigorous Phase II and III clinical trials failed to demonstrate benefits for CLI patients |
25633211 | EXPERT OPINION: Compared with VEGF and FGF, HGF has a unique molecular effect on inflammation, fibrosis and cell senescence under pathological conditions |
25453983 | After 2 weeks, the cells were treated with either VEGF or its vehicle and their transepithelial electrical resistance (TEER) was measured |
25453983 | RESULTS: VEGF was significantly more effective in reducing the TEER of the high PDL ARPE-19 cell layers than the low PDL layers (25% decrease vs |
25453983 | CONCLUSIONS: The present results show that the ability of VEGF to reduce the barrier function of RPE cell layers is greater in high PDL layers, which display signs of senescence, than in low PDL layers |
25388834 | Our data showed that both eNOS and Akt phosphorylation, VEGF expression and nitric oxide production were significantly decreased, RMVECs ageing and apoptosis increased after ox-LDL induction for 24 hrs, all of which were effectively reversed by ciglitazone pre-treatment |
25192254 | The expression of VEGF and VEGFR2 was reduced in Sirt3KO-EPCs |
25192254 | In post-MI mice, BMC treatment increased number of Sca1+/c-kit+ cells; enhanced VEGF expression and angiogenesis whereas Sirt3KO-BMC treatment had little effects |
25158160 | Hepatocyte growth factor (HGF), vascular endothelial growth factor (VEGF), and fibroblast growth factor (FGF) are all potent angiogenic growth factors in animal models of ischemia, but their therapeutic effects are not the same in animal experiments and clinical trials |
25158160 | A multicenter, double-blind, placebo-controlled phase III clinical trial in Japan and a US phase II clinical trial of HGF gene therapy for critical limb ischemia (CLI) demonstrated a significant improvement in primary end points and an increase in transcutaneous partial pressure of oxygen even after one year compared with placebo, whereas effectiveness of VEGF and FGF treatment for CLI has not yet been shown |
25158160 | Moreover, our recent publication and another researcher demonstrated that HGF acts as an anti-inflammatory cytokine, while VEGF and FGF act as pro-inflammatory cytokine |
25108204 | That is, DHA supplement inhibited cellular proliferation, destroyed cell membrane integrity, enhanced cellular senescence, increased vascular endothelial growth factor (VEGF) release, and decreased phagocytic function |
24681605 | Expression of two senescence-associated cytokines (VEGFA and MCP1) was durably increased by adjuvant chemotherapy |
23770676 | Coupling quantitative proteomics with small-molecule screens, we identified multiple SASP components mediating paracrine senescence, including TGF-beta family ligands, VEGF, CCL2 and CCL20 |
23758730 | In addition, angiogenesis and VEGF expression in CT26 colon carcinoma was significantly inhibited by TLBZT treatment |
23583398 | 7-fold) and down-regulated expression of vascular endothelial growth factor-A (0 |
23503666 | The downregulation of vascular endothelial growth factor (VEGF) was observed in the irradiated HUVECs as the PN increased |
23174937 | Potentially functional polymorphisms were found in vascular endothelial growth factor (VEGF), ABCB1, FGFR2 and PHLPP2 |
23174937 | VEGF polymorphisms were the most common and detected at four loci |
22904099 | Compared with young EC, senescent cells displayed increased expression of senescence-associated beta-galactosidase, nitric oxide synthase (eNOS), and AKT kinase, and secreted increased amounts of growth factors (VEGF, TGF-beta), cytokines (IL-6, IL-8, MCP-1), adhesion molecules (sICAM-1), and matrix proteins (fibronectin) |
22797809 | Atm deficiency also lowered tumor angiogenesis and enhanced the antiangiogenic action of vascular endothelial growth factor (Vegf) blockade |
22470345 | Based on its senescence-dependent involvement in alternative splicing, we postulate that SRSF1 is a key marker of EC senescence, regulating the expression of alternative isoforms of target genes such as endoglin (ENG), vascular endothelial growth factor A (VEGFA), tissue factor (T3), or lamin A (LMNA) that integrate in a common molecular senescence program |
22340562 | Expression of OPN, hypoxia inducible factor-1 (HIF-1) and vascular endothelial growth factor (VEGF) proteins was analyzed by Western blotting analysis |
22340562 | RESULTS: HIF-1 and VEGF proteins in MDA-MB-343 cells were significantly downregulated upon the efficient knockdown of OPN expression under either hypoxia or normoxia environment |
21793037 | The level of plasma vascular endothelial growth factor (VEGF) was measured by ELISA |
21793037 | In addition, there were higher levels of plasma VEGF in CA patients compared with healthy control subjects |
21622994 | RESULTS: Uremic MSCs showed decreased expression of vascular endothelial growth factor (VEGF), VEGF receptor (VEGFR)1 and stromal cell-derived factor (SDF)-1alpha, increased cellular senescence, decreased proliferation, defects in migration in response to VEGF and SDF-1alpha and in vitro tube formation |
21622994 | Uremia decreased hypoxia-inducible factor-1alpha, VEGF and VEGFR1 expression under hypoxia and Akt phosphorylation in both basal and VEGF-stimulated states |
21618508 | Vascular endothelial growth factor (VEGF) inhibitors, such as bevacizumab, have improved outcomes in metastatic colorectal cancer (CRC) |
21618508 | Recent studies have suggested that VEGF can delay the onset of cellular senescence in human endothelial cells |
21618508 | As VEGF receptors are known to be upregulated in CRC, we hypothesized that VEGF inhibition may directly influence cellular senescence in this disease |
21618508 | To understand how VEGF inhibitors may regulate cellular senescence, we noted that among the two important regulators of senescent growth arrest of tumor cells, bevacizumab-associated increase in cellular senescence coincided with an upregulation of p16 but appeared to be independent of p53 |
21618508 | These findings demonstrate a novel antitumor activity of VEGF inhibitors in CRC, involving p16 |
21245959 | This study investigated the effects of short- and long-term in vitro inhibition of vascular endothelial growth factor (VEGF) Receptor-2 (VEGFR-2) signaling by SU5416 and other inhibitors of the VEGF signaling pathway in OECs |
21245959 | Migration in vitro to VEGF and stromal cell-derived factor 1 of OECs was assessed |
21245959 | Naturally senescent cells and cells rendered senescent by VEGFR-2 TKIs had reduced VEGFR-2 and CXCR-4 expression and demonstrated reduced migratory ability to VEGF |
20713685 | Exposure to VAT adipocytes caused more EC senescence-associated beta-galactosidase activity than SAT adipocytes, an effect reduced in the presence of vascular endothelial growth factor A (VEGFA) neutralizing antibodies |
20374652 | Expression of the master cell cycle regulators p53 and p21 and growth factors HGF and VEGF also declined significantly at 26 months |
19047582 | Although both hepatocyte growth factor (HGF) and vascular endothelial growth factor (VEGF) are potent angiogenic growth factors in animal models of ischemia, their characteristics are not the same in animal experiments and clinical trials |
19047582 | To elucidate the discrepancy between HGF and VEGF, we compared the effects of HGF and VEGF on endothelial progenitor cells under angiotensin II stimulation, which is a well-known risk factor for atherosclerosis |
19047582 | Here, we demonstrated that HGF, but not VEGF, attenuated angiotensin II-induced senescence of endothelial progenitor cells through a reduction of oxidative stress by inhibition of the phosphatidylinositol-3,4,5-triphosphate/rac1 pathway |
19047582 | Potent induction of neovascularization of endothelial progenitor cells by HGF, but not VEGF, under angiotensin II was also confirmed by in vivo experiments using several models, including HGF transgenic mice |
19011671 | EC exhibited higher expression levels of markers of oxidative stress (lipid peroxydation level and caveolin-1 mRNA), inflammation (angiopoietin-like 2 mRNA), hypoxia (vascular endothelial growth factor (VEGF)-A mRNA), and cell damage (p53 mRNA) |
18583712 | Vascular endothelial growth factor (VEGF) binds both VEGF receptor-1 (VEGFR-1) and VEGF receptor-2 (VEGFR-2) |
18583712 | Activation of VEGFR-2 is thought to play a major role in the regulation of endothelial function by VEGF |
18583712 | In this study, we showed that VEGFR-1 performs "fine tuning" of VEGF signaling to induce neovascularization |
18583712 | When VEGFR-1 expression was blocked, VEGF constitutively activated Akt signals and thus induced endothelial cell senescence via a p53-dependent pathway |
18583712 | These results suggest that VEGFR-1 plays a critical role in the maintenance of endothelial integrity by modulating the VEGF/Akt signaling pathway |
17402563 | VEGF has been recognized as a predominant factor to induce the ischemic retinal neovascularization |
17402563 | We found that retinal vascular cells have a characteristic pattern in VEGF receptor expression, which causes vascular pathology more frequently in the retina than in other organs |
17402563 | Finally, we found that erythropoietin is an ischemia-induced angiogenic factor that acts independently and as potently as VEGF in proliferative diabetic retinopathy (PDR) |
17402563 | Our study utilizing human vitreous samples demonstrates that the VEGF level is particularly high and strongly associated with angiogenic activity in PDR patients |
17402563 | The potential of VEGF inhibitors has recently been recognized in clinical applications |
16880208 | Accordingly, increased vascular endothelial growth factor (VEGF) expression was a frequent characteristic of senescent human and mouse fibroblasts in culture |
16880208 | Increased VEGF expression was specific to the senescent phenotype and increased whether senescence was induced by replicative exhaustion, overexpression of p16(Ink4a), or overexpression of oncogenic RAS |
16880208 | The senescence-dependent increase in VEGF production was accompanied by very little increase in hypoxic-inducible (transcription) factor 1 alpha protein levels, and hypoxia further induced VEGF in senescent cells |
16880208 | This result suggests the rise in VEGF expression at senescence is not a hypoxic response |
16827160 | In the immortalized HDFs, the transcriptional activity of HIF-1alpha was also evident by the accumulation of its main downstream gene targets, namely erythropoietin (EPO) and the vascular endothelial growth factor (VEGF) |
16755088 | Angiogenic growth factors secreted by EPCs, such as vascular endothelial growth factor (VEGF), basic fibroblast growth factor (b-FGF), hepatocyte growth factor (HGF), and macrophage chemoattractant protein (MCP-1) from the culture medium were also measured by enzyme-linked immunosorbent assay |
16755088 | There was no significant difference of angiogenic growth factors (VEGF, HGF, b-FGF, and MCP-1) secreted by EPCs between the two groups |
16093915 | In addition, EPCs released vascular endothelial growth factor (VEGF) protein--an effect that was significantly augmented by 17beta-estradiol |
16093915 | Finally, in a Matrigel assay, EPCs treated with both 17beta-estradiol and VEGF were shown to be more likely to integrate into the network formation than those treated with VEGF alone |
16010436 | HUV-ST cells are capable of organizing into tubule-like networks with branching morphology in response to appropriate stimuli and migrate upon exposure to VEGF |
12959928 | Senescent BMP4-treated cells had lower ERK activation, VEGF expression, and Bcl2 expression than wild-type cells, consistent with a less proliferative, less angiogenic phenotype with increased susceptibility to death by apoptosis |
12676798 | In this study, we examined the relationship between telomerase activity and endothelial cell proliferation as well as the regulation of this enzyme by fibroblast growth factor-2 (FGF-2) and vascular endothelial growth factor-A (VEGF) |
12676798 | Treatment of quiescent HUVECs with FGF-2 restored telomerase activity in a time- and dose-dependent manner, whereas VEGF had no such effect, although both factors induced comparable mitogenic responses |
12676798 | CONCLUSIONS: FGF-2, but not VEGF, restores telomerase activity and maintains the replicative capacity of endothelial cells |
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