INT173082

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Context Info
Confidence 0.48
First Reported 2003
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 20
Total Number 20
Disease Relevance 11.16
Pain Relevance 0.79

This is a graph with borders and nodes. Maybe there is an Imagemap used so the nodes may be linking to some Pages.

extracellular space (VEGFA) growth (VEGFA) extracellular region (VEGFA)
proteinaceous extracellular matrix (VEGFA) cytoplasm (VEGFA)
Anatomy Link Frequency
blood 2
endothelial cells 2
B cells 2
Capan-1 2
VEGFA (Homo sapiens)
Pain Link Frequency Relevance Heat
cytokine 103 96.36 Very High Very High Very High
Inflammation 253 93.00 High High
agonist 63 90.88 High High
metalloproteinase 24 85.64 High High
Bioavailability 2 85.64 High High
alcohol 5 85.60 High High
Inflammatory marker 6 76.48 Quite High
antagonist 18 72.84 Quite High
Chronic pancreatitis 3 72.40 Quite High
cva 34 60.28 Quite High
Disease Link Frequency Relevance Heat
Hypoxia 149 100.00 Very High Very High Very High
Metastasis 85 100.00 Very High Very High Very High
Diabetes Mellitus 179 99.90 Very High Very High Very High
Cancer 657 99.00 Very High Very High Very High
Hyperglycemia 41 97.12 Very High Very High Very High
Chronic Lymphoid Leukemia 7 96.92 Very High Very High Very High
Pancreatic Cancer 83 94.68 High High
Age-related Macular Degeneration 298 94.20 High High
Retinal Neovascularization 6 94.16 High High
INFLAMMATION 291 93.00 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
As for the soluble species, total free VEGF in all compartments decreased with increasing VEGF-binding affinity of either VEGFR1 or VEGFR2 – presumably through enhanced internalization of complexed VEGF (Fig. 6B).
Positive_regulation (enhanced) of VEGF Binding (internalization) of
1) Confidence 0.48 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
Free sVEGFR1 concentrations, however, changed in opposite directions: lowered with increasing VEGF-VEGFR1 affinity but rose with increasing VEGF-VEGFR2 affinity.
Positive_regulation (increasing) of VEGF-VEGFR1 Binding (affinity) of
2) Confidence 0.48 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
Free sVEGFR1 concentrations, however, changed in opposite directions: lowered with increasing VEGF-VEGFR1 affinity but rose with increasing VEGF-VEGFR2 affinity.
Positive_regulation (increasing) of VEGF-VEGFR2 Binding (affinity) of
3) Confidence 0.48 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
As for the soluble species, total free VEGF in all compartments decreased with increasing VEGF-binding affinity of either VEGFR1 or VEGFR2 – presumably through enhanced internalization of complexed VEGF (Fig. 6B).
Positive_regulation (increasing) of VEGF Binding (internalization) of
4) Confidence 0.48 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
Vascular endothelial growth factor (VEGF) is composed of a family of five isoforms (VEGFA, VEGFB, VEGFC, VEGFD, and PLGF) which act as ligands for tyrosine kinase receptors (VEGF-Rs).203 Upon binding of VEGF to its receptors (primarily VEGFR2), intracellular signaling pathways, including MEK-ERK and PI3K-Akt, are activated that mediate angiogenic switches (Fig. 1).
Positive_regulation (activated) of VEGF Binding (ligands) of
5) Confidence 0.44 Published 2010 Journal Clinical Medicine Insights. Oncology Section Body Doc Link PMC2883240 Disease Relevance 0.68 Pain Relevance 0
Distribution changes were again more evident in the blood: the simultaneous elevations in free VEGF and sVEGFR1, due to increasing global kL (e.g., 10× from control), in turn synergistically increased sVEGFR1-VEGF complex formation (e.g., 88× from control), which elevated the complexed fractions of both VEGF (e.g., +13%) and sVEGFR1 (e.g., +8.7%).
Positive_regulation (increased) of sVEGFR1-VEGF Binding (formation) of in blood
6) Confidence 0.42 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0.09 Pain Relevance 0
Comparison of gene signatures from primary tumor, regional, and distant metastasis indicates that VEGF is only overexpressed in distant metastasis and is associated with poor survival.
Positive_regulation (overexpressed) of VEGF Binding (associated) of associated with cancer and metastasis
7) Confidence 0.41 Published 2010 Journal Clinical Medicine Insights. Oncology Section Body Doc Link PMC2883240 Disease Relevance 1.32 Pain Relevance 0
Functional receptor binding studies by this group confirmed high levels of VEGF-VEGFR interaction only in Capan-1 cells; VEGF dose-dependently enhanced proliferation, promoted MAPK phosphorylation, and induced c-fos activity only in these Capan-1 cells [82].
Positive_regulation (levels) of VEGF Binding (interaction) of in Capan-1
8) Confidence 0.40 Published 2003 Journal Mol Cancer Section Body Doc Link PMC150383 Disease Relevance 0.74 Pain Relevance 0.07
This complex can then bind a hypoxia response element, and induce VEGF transcription.22

VEGF function

Positive_regulation (induce) of VEGF Binding (function) of associated with hypoxia
9) Confidence 0.37 Published 2010 Journal Cancer management and research Section Body Doc Link PMC3004565 Disease Relevance 0.59 Pain Relevance 0
This complex can then bind a hypoxia response element, and induce VEGF transcription.22

VEGF function

Positive_regulation (induce) of VEGF Binding (bind) of associated with hypoxia
10) Confidence 0.37 Published 2010 Journal Cancer management and research Section Body Doc Link PMC3004565 Disease Relevance 0.60 Pain Relevance 0
Activated VEGF may bind to two
Positive_regulation (Activated) of VEGF Binding (bind) of
11) Confidence 0.29 Published 2008 Journal PPAR Research Section Body Doc Link PMC2490577 Disease Relevance 1.67 Pain Relevance 0.19
Bevacizumab binding to VEGF sterically hinders VEGF ligation to its receptors on vascular endothelial cells (Kim et al 1992).
Positive_regulation (hinders) of VEGF Binding (ligation) of in endothelial cells
12) Confidence 0.24 Published 2008 Journal Biologics : Targets & Therapy Section Body Doc Link PMC2721410 Disease Relevance 0.54 Pain Relevance 0.04
forms an active complex with the transcriptional coactivator p300 and activated Stat3 on the VEGF promoter, which likely explains the anomalous autocrine VEGF secretion from CLL B cells [273].
Positive_regulation (activated) of VEGF Binding (complex) of in B cells associated with chronic lymphoid leukemia
13) Confidence 0.20 Published 2010 Journal PPAR Research Section Body Doc Link PMC2829627 Disease Relevance 0.86 Pain Relevance 0.16
However, only the wild-type RNA was pulled-down with the ASF/SF2 protein, suggesting that the region we have mutated or deleted is required for ASF/SF2 binding to the VEGF pre-mRNA.


Positive_regulation (required) of VEGF Binding (binding) of
14) Confidence 0.18 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2820781 Disease Relevance 0.25 Pain Relevance 0
It also binds all isomers of VEGF (Ferrara et al 2004) but, unlike ranibizumab with a single VEGF binding site, it has two VEGF binding sites that increase its overall dissociation constant for VEGF to between 0.5 and 1.0 nM compared with 0.140 nM for ranibizumab (Chen et al 1999).
Positive_regulation (increase) of VEGF Binding (dissociation) of
15) Confidence 0.17 Published 2007 Journal Clinical ophthalmology (Auckland, N.Z.) Section Body Doc Link PMC2701127 Disease Relevance 0.08 Pain Relevance 0
Advanced glycation end products (AGE), senescent macroprotein derivatives form at an accelerated rate in diabetes and induce angiogenesis through overgeneration of autocrine vascular endothelial growth factor (VEGF).
Positive_regulation (induce) of VEGF Binding (overgeneration) of associated with diabetes mellitus
16) Confidence 0.14 Published 2007 Journal Immun Ageing Section Body Doc Link PMC1845171 Disease Relevance 1.19 Pain Relevance 0.15
Advanced glycation end products (AGE), senescent macroprotein derivatives form at an accelerated rate in diabetes and induce angiogenesis through overgeneration of autocrine vascular endothelial growth factor (VEGF).
Positive_regulation (induce) of vascular endothelial growth factor Binding (overgeneration) of associated with diabetes mellitus
17) Confidence 0.14 Published 2007 Journal Immun Ageing Section Body Doc Link PMC1845171 Disease Relevance 1.19 Pain Relevance 0.15
A supportive finding for this hypothesis is the fact that VEGF receptor 1 (FLT1) and PAI-1, both known Egr-1 responsive genes, are also increased in the presence of glucose and insulin.
Positive_regulation (increased) of VEGF Binding (receptor) of
18) Confidence 0.08 Published 2010 Journal Mediators of Inflammation Section Body Doc Link PMC2903979 Disease Relevance 1.00 Pain Relevance 0.03
Based on this information, excessive expression of VEGFR-1 could result in increased binding to VEGF ligand, resulting in competitive suppression of VEFGR-2 activation and the angiogenic response.
Positive_regulation (increased) of VEGF Binding (binding) of
19) Confidence 0.05 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2603310 Disease Relevance 0 Pain Relevance 0
Ranibizumab was generated after several rounds of molecular modification that significantly increased binding affinity for its target, VEGF-A.
Positive_regulation (increased) of VEGF Binding (binding) of
20) Confidence 0.04 Published 2007 Journal Core Evidence Section Body Doc Link PMC3012443 Disease Relevance 0.37 Pain Relevance 0

General Comments

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