INT143125

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Context Info
Confidence 0.40
First Reported 2003
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 48
Total Number 49
Disease Relevance 13.60
Pain Relevance 0.51

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

cell differentiation (FLT1) endosome (FLT1) Golgi apparatus (FLT1)
cytoplasm (FLT1) extracellular space (FLT1) extracellular region (FLT1)
Anatomy Link Frequency
endothelial cells 10
plasma 3
blood 2
placenta 2
body 2
FLT1 (Homo sapiens)
Pain Link Frequency Relevance Heat
antagonist 94 94.88 High High
cINOD 1 83.88 Quite High
Inflammation 74 78.72 Quite High
cytokine 82 78.24 Quite High
Clonidine 1 67.20 Quite High
cva 44 60.08 Quite High
metalloproteinase 92 49.12 Quite Low
addiction 87 44.96 Quite Low
ischemia 61 44.72 Quite Low
Restless leg syndrome 29 26.68 Quite Low
Disease Link Frequency Relevance Heat
Fibromyalgia 45 100.00 Very High Very High Very High
Eclampsia 92 99.60 Very High Very High Very High
Pre-eclampsia 183 99.36 Very High Very High Very High
Cancer 580 99.20 Very High Very High Very High
Genetic Predisposition To Disease 6 98.92 Very High Very High Very High
Pancreatic Cancer 166 98.18 Very High Very High Very High
Hyperglycemia 38 96.92 Very High Very High Very High
Disease 348 93.76 High High
Metastasis 85 92.88 High High
Solid Tumor 50 90.68 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
The much lower complexed fractions from experimental data may indicate that in vivo, other soluble receptors (e.g., sVEGFR2, sNRP1, plasma fibronectin) can strongly compete with sVEGFR1 as plasma reservoirs for VEGF, or significant quantities of other ligands (e.g., PlGF, VEGF-B) are present to compete with VEGF for sVEGFR1 binding.
sVEGFR1 Binding (binding) of in plasma
1) Confidence 0.40 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
We propose that the experimental quantification of all major in vivo binding partners for both VEGF and sVEGFR1 from peripheral blood samples to be essential in reconciling the apparent contradiction between predicted and measured VEGF-sVEGFR1 complexed fractions.
sVEGFR1 Binding (binding) of in blood
2) Confidence 0.40 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0.06 Pain Relevance 0
Hence we identified the need for a computational model that predicts the systemic distributions and molecular interactions of VEGF and sVEGFR1 across the human body, to serve as a platform for the mechanistic study of sVEGFR1's purported anti-angiogenic properties, as well as the pre-clinical study of sVEGFR1 as a disease marker and therapeutic agent.


sVEGFR1 Binding (interactions) of in body associated with disease
3) Confidence 0.40 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0.60 Pain Relevance 0
Based on genetic predisposition, this relationship may be strengthened by showing an association between polymorphisms of Flt-1 gene and an increased risk of developing preeclampsia.
Flt-1 gene Binding (association) of associated with genetic predisposition to disease and pre-eclampsia
4) Confidence 0.36 Published 2008 Journal BMC Med Genet Section Body Doc Link PMC2496902 Disease Relevance 0.61 Pain Relevance 0
Most of the Flt-1 produced in the mouse and human placenta during later stages of gestation is the soluble form (sFlt-1) generated by alternative splicing of Flt-1, leading to a premature termination after the sixth Ig-like domain [30]. sFlt-1 binds both VEGF and PlGF and acts as a soluble antagonist of their action.
Flt-1 Binding (splicing) of in placenta associated with antagonist
5) Confidence 0.36 Published 2008 Journal BMC Med Genet Section Body Doc Link PMC2496902 Disease Relevance 0.55 Pain Relevance 0.05
Among the major endothelial cell surface receptor targets for these VEGF isoforms are: the tyrosine kinases VEGFR1 (Flt-1; UniProt accession P17948-1) and VEGFR2 (mouse Flk-1; human KDR; UniProt accession P35968); as well as the co-receptor neuropilin-1 (NRP1; UniProt accession O14786), which couples directly with VEGFR1, and indirectly with VEGFR2 through non-overlapping binding sites on VEGF165 [7].


Flt-1 Binding (indirectly) of in endothelial cell
6) Confidence 0.35 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0.42 Pain Relevance 0.03
The overall drop in “anti-angiogenic potential”, as represented by ligated VEGFR1 complexes, can be explained by NRP1's high affinity for VEGFR1.
VEGFR1 Binding (ligated) of
7) Confidence 0.35 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
We have previously developed several computational models of the in vivo biochemical interactions between VEGF121, VEGF165, VEGFR1, VEGFR2, NRP1, and the interstitial matrix in skeletal muscle, including: a spatially-averaged single-tissue model of the human vastus lateralis muscle at rest [54]; and several 3D models for predicting spatial molecular gradients and intra-muscular pro-angiogenic treatment outcomes in resting and exercising rat extensor digitorum longus muscle [55]–[58].
VEGFR1 Binding (interactions) of in extensor digitorum longus
8) Confidence 0.35 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0.31 Pain Relevance 0
Among the major endothelial cell surface receptor targets for these VEGF isoforms are: the tyrosine kinases VEGFR1 (Flt-1; UniProt accession P17948-1) and VEGFR2 (mouse Flk-1; human KDR; UniProt accession P35968); as well as the co-receptor neuropilin-1 (NRP1; UniProt accession O14786), which couples directly with VEGFR1, and indirectly with VEGFR2 through non-overlapping binding sites on VEGF165 [7].


Flt-1 Binding (tyrosine) of in endothelial cell
9) Confidence 0.35 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0.41 Pain Relevance 0.03
Among the major endothelial cell surface receptor targets for these VEGF isoforms are: the tyrosine kinases VEGFR1 (Flt-1; UniProt accession P17948-1) and VEGFR2 (mouse Flk-1; human KDR; UniProt accession P35968); as well as the co-receptor neuropilin-1 (NRP1; UniProt accession O14786), which couples directly with VEGFR1, and indirectly with VEGFR2 through non-overlapping binding sites on VEGF165 [7].


VEGFR1 Binding (tyrosine) of in endothelial cell
10) Confidence 0.35 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0.41 Pain Relevance 0.03
The overall drop in “anti-angiogenic potential”, as represented by ligated VEGFR1 complexes, can be explained by NRP1's high affinity for VEGFR1.
VEGFR1 Binding (complexes) of
11) Confidence 0.35 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
Among the major endothelial cell surface receptor targets for these VEGF isoforms are: the tyrosine kinases VEGFR1 (Flt-1; UniProt accession P17948-1) and VEGFR2 (mouse Flk-1; human KDR; UniProt accession P35968); as well as the co-receptor neuropilin-1 (NRP1; UniProt accession O14786), which couples directly with VEGFR1, and indirectly with VEGFR2 through non-overlapping binding sites on VEGF165 [7].


VEGFR1 Binding (tyrosine) of in endothelial cell
12) Confidence 0.35 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0.42 Pain Relevance 0.03
Soluble Flt-1 binds to circulating free vascular endothelial growth factor and placenta growth factor and this is associated with endothelial dysfunction.
Flt-1 Binding (binds) of in placenta
13) Confidence 0.35 Published 2009 Journal Clin. Exp. Pharmacol. Physiol. Section Abstract Doc Link 19215236 Disease Relevance 0.34 Pain Relevance 0.07
In the interstitium, the fractional occupancies of VEGFR1 and VEGFR2 by VEGF decreased <0.5% within the 100-fold increase in kP tested.

6.2.

VEGFR1 Binding (occupancies) of
14) Confidence 0.34 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0.07 Pain Relevance 0
In this region, the greater abundance of VEGFR1 gave more prominence to NRP1's tendency to competitively shift the distribution of total VEGFR1 towards formation of unligated VEGFR1-NRP1 complexes, in the process freeing VEGF that had been bound to uncoupled VEGFR1, hence elevating free VEGF concentrations.
VEGFR1 Binding (bound) of
15) Confidence 0.34 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
However, the present study did not rule out the possibility that monomeric sVEGFR1, in its capacity to heterodimerize with surface VEGFR1 or VEGFR2 monomers, can significantly alter these distributions.


VEGFR1 Binding (heterodimerize) of
16) Confidence 0.34 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
The overall drop in “anti-angiogenic potential”, as represented by ligated VEGFR1 complexes, can be explained by NRP1's high affinity for VEGFR1.
VEGFR1 Binding (affinity) of
17) Confidence 0.34 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
At 105 NRP1/EC, almost all (97%) VEGFR1 became part of unligated VEGFR1-NRP1 complexes – a shift that dramatically reduced the availability of VEGFR1 for VEGF165-ligation (Fig. 5B).
VEGFR1 Binding (ligation) of
18) Confidence 0.34 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
Significant complexed fractions of VEGF and sVEGFR1 in plasma necessitate re-evaluation of assay specificity
sVEGFR1 Binding (fractions) of in plasma
19) Confidence 0.31 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
0.6% sVEGFR1-bound, 98.3%?
sVEGFR1 Binding (bound) of
20) Confidence 0.31 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0

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