INT173051

From wiki-pain
Jump to: navigation, search
Context Info
Confidence 0.44
First Reported 2003
Last Reported 2010
Negated 1
Speculated 0
Reported most in Body
Documents 16
Total Number 20
Disease Relevance 1.29
Pain Relevance 0.04

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

extracellular region (VEGFA, NRP1) cell differentiation (NRP1) cell-cell signaling (NRP1)
cytoplasm (VEGFA) cytosol (NRP1) signal transduction (NRP1)
Anatomy Link Frequency
endothelial cell 1
vascular endothelium 1
VEGFA (Homo sapiens)
NRP1 (Homo sapiens)
Pain Link Frequency Relevance Heat
Bioavailability 5 82.08 Quite High
addiction 39 43.12 Quite Low
cytokine 27 39.88 Quite Low
Inflammation 27 15.52 Low Low
metalloproteinase 41 5.00 Very Low Very Low Very Low
antagonist 39 5.00 Very Low Very Low Very Low
ischemia 26 5.00 Very Low Very Low Very Low
Central nervous system 15 5.00 Very Low Very Low Very Low
Restless leg syndrome 13 5.00 Very Low Very Low Very Low
tolerance 13 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Cancer 219 95.52 Very High Very High Very High
Pulmonary Disease 15 87.28 High High
Pancreatic Cancer 162 85.12 High High
Adult Respiratory Distress Syndrome 140 81.96 Quite High
Death 15 64.08 Quite High
Pressure And Volume Under Development 28 56.80 Quite High
Metastasis 50 53.84 Quite High
Hypoxia 123 50.00 Quite Low
Malignant Neoplastic Disease 18 48.88 Quite Low
Eye Disease 5 47.28 Quite Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
VEGFRs' affinities for VEGF affected free sVEGFR1 concentrations via NRP1 availability; NRP1's affinity for VEGF121 was inconsequential
VEGF121 Binding (affinity) of NRP1's
1) Confidence 0.44 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
Thus, as long as VEGF had a lower affinity to NRP1 than to VEGFRs, the system was largely insensitive to variations in the VEGF-binding affinities of NRP1.
VEGF Binding (affinity) of NRP1
2) Confidence 0.44 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
VEGF165b binds to VEGF-R2 with equal affinity to VEGF165, but it also phosphorylates VEGF-R2 but in a qualitatively unique way (15).
VEGF Binding (binds) of VEGF165b
3) Confidence 0.39 Published 2010 Journal American Journal of Physiology - Lung Cellular and Molecular Physiology Section Body Doc Link PMC2886605 Disease Relevance 0.06 Pain Relevance 0
This suggested that mechanistically, the significance of NRP1 as a co-receptor in the VEGF system could be largely attributed to NRP1's strength in coupling VEGFRs rather than its direct affinity for VEGF.

5.

VEGF Binding (affinity) of NRP1's
4) Confidence 0.34 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
This suggested that mechanistically, the significance of NRP1 as a co-receptor in the VEGF system could be largely attributed to NRP1's strength in coupling VEGFRs rather than its direct affinity for VEGF.

5.

VEGF Binding (affinity) of NRP1
5) Confidence 0.34 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
Higher NRP1 densities were generally associated with lower concentrations of all soluble species, since NRP1 was a vehicle for internalizing VEGF and sVEGFR1 via endothelial VEGF121-NRP1, VEGF165-NRP1, sVEGFR1-NRP1, VEGF121-VEGFR1-NRP1 complexes.
VEGF Binding (internalizing) of NRP1
6) Confidence 0.34 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
Higher NRP1 densities were generally associated with lower concentrations of all soluble species, since NRP1 was a vehicle for internalizing VEGF and sVEGFR1 via endothelial VEGF121-NRP1, VEGF165-NRP1, sVEGFR1-NRP1, VEGF121-VEGFR1-NRP1 complexes.
VEGF121 Binding (internalizing) of NRP1
7) Confidence 0.34 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
Sensitivity to VEGF-binding affinity of NRP1
VEGF-binding Binding (affinity) of NRP1
8) Confidence 0.34 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
In fact, against general consensus that VEGF121 does not bind NRP1, Pan et al. recently observed such binding at Kd?
VEGF121 Neg (not) Binding (bind) of NRP1
9) Confidence 0.34 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
Secondarily, declines in sVEGFR1-VEGF complex concentrations followed increases in NRP1 density (Fig. 5A), as NRP1 competed with sVEGFR1 for binding with free VEGF.
VEGF Binding (binding) of NRP1
10) Confidence 0.33 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
Curly brackets contain the terms referring to the direct binding interaction between VEGF121 and NRP1, which were turned off (kon?
VEGF121 Binding (interaction) of NRP1
11) Confidence 0.33 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
Our simulations also predicted inconsequential effects from incorporating the newly purported binding interaction between NRP1 and VEGF121.
VEGF121 Binding (interaction) of NRP1
12) Confidence 0.33 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
We thus tested both scenarios: adding a new interaction between VEGF121 and NRP1 at a dissociation constant 1.83 times higher than our control Kd for VEGF165 and NRP1 (to match the Kd ratio measured by Pan et al.); and setting NRP1 affinities for both VEGF isoforms to the exact values as Pan et al. reported.
VEGF121 Binding (interaction) of NRP1
13) Confidence 0.33 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
We thus tested both scenarios: adding a new interaction between VEGF121 and NRP1 at a dissociation constant 1.83 times higher than our control Kd for VEGF165 and NRP1 (to match the Kd ratio measured by Pan et al.); and setting NRP1 affinities for both VEGF isoforms to the exact values as Pan et al. reported.
VEGF121 Binding (interaction) of VEGF165
14) Confidence 0.33 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2663039 Disease Relevance 0 Pain Relevance 0
Interestingly, VEGF165b binds the generic VEGF receptors (VEGF-R1 and VEGF-R2) but not neuropilin-1 (NRP-1), the binding to which now appears to be exon 8a dependant (6).
VEGF Binding (binds) of VEGF165b
15) Confidence 0.30 Published 2010 Journal American Journal of Physiology - Lung Cellular and Molecular Physiology Section Body Doc Link PMC2886605 Disease Relevance 0 Pain Relevance 0
VEGF exerts its biological effect on vascular endothelium through specific receptors, VEGFR-1 and VEGFR-2, and coreceptors, neuropilin-1 and neuropilin-2 (10, 11, 19, 26, 27).
VEGF Binding (receptors) of neuropilin-1 in vascular endothelium
16) Confidence 0.30 Published 2010 Journal American Journal of Physiology - Lung Cellular and Molecular Physiology Section Body Doc Link PMC2886605 Disease Relevance 0.32 Pain Relevance 0.04
Interestingly, VEGF165b binds the generic VEGF receptors (VEGF-R1 and VEGF-R2) but not neuropilin-1 (NRP-1), the binding to which now appears to be exon 8a dependant (6).
VEGF-R1 Binding (binds) of VEGF165b
17) Confidence 0.30 Published 2010 Journal American Journal of Physiology - Lung Cellular and Molecular Physiology Section Body Doc Link PMC2886605 Disease Relevance 0 Pain Relevance 0
Interestingly, VEGF165b binds the generic VEGF receptors (VEGF-R1 and VEGF-R2) but not neuropilin-1 (NRP-1), the binding to which now appears to be exon 8a dependant (6).
VEGF Binding (binds) of VEGF165b
18) Confidence 0.30 Published 2010 Journal American Journal of Physiology - Lung Cellular and Molecular Physiology Section Body Doc Link PMC2886605 Disease Relevance 0 Pain Relevance 0
Existing evidence indicates that neuropilin-1 acts as a coreceptor which enhances the activity of VEGFR-2 upon binding to VEGF-A165, leading to increased endothelial cell migration [73].
VEGF-A165 Binding (binding) of neuropilin-1 in endothelial cell
19) Confidence 0.10 Published 2003 Journal Mol Cancer Section Body Doc Link PMC150383 Disease Relevance 0.35 Pain Relevance 0
Neuropilin-2 is also able to bind VEGF-A165, but unlike neuropilin-1, it also interacts with VEGF-A145 [70,72,73].
VEGF-A145 Binding (interacts) of neuropilin-1
20) Confidence 0.10 Published 2003 Journal Mol Cancer Section Body Doc Link PMC150383 Disease Relevance 0.56 Pain Relevance 0

General Comments

This test has worked.

Personal tools
Namespaces

Variants
Actions
Navigation
Toolbox