INT200855

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Context Info
Confidence 0.45
First Reported 2006
Last Reported 2010
Negated 1
Speculated 0
Reported most in Body
Documents 14
Total Number 16
Disease Relevance 11.14
Pain Relevance 0.77

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

plasma membrane (Kdr) kinase activity (Kdr) cytoplasm (Kdr)
Anatomy Link Frequency
endothelial cells 5
heart 2
blood 1
tail 1
Kdr (Mus musculus)
Pain Link Frequency Relevance Heat
Inflammation 23 95.80 Very High Very High Very High
antagonist 13 94.68 High High
imagery 242 93.76 High High
cytokine 14 84.16 Quite High
Inflammatory mediators 1 70.48 Quite High
ischemia 14 67.32 Quite High
anesthesia 16 59.80 Quite High
cva 1 42.56 Quite Low
palliative 1 26.24 Quite Low
cINOD 4 18.24 Low Low
Disease Link Frequency Relevance Heat
Pathologic Neovascularization 13 99.60 Very High Very High Very High
Cancer 927 99.42 Very High Very High Very High
Targeted Disruption 71 99.20 Very High Very High Very High
Hypoxia 141 98.82 Very High Very High Very High
Injury 39 97.76 Very High Very High Very High
Pre-eclampsia 72 97.48 Very High Very High Very High
Increased Venous Pressure Under Development 15 97.12 Very High Very High Very High
INFLAMMATION 33 95.80 Very High Very High Very High
Wound Healing 10 94.12 High High
Hypertrophy 50 93.12 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
The growth of blood vessels (angiogenesis) is primarily initiated by activation of VEGFR-1 and VEGFR-2 by VEGF-A, whereas lymphangiogenesis is predominantly driven by VEGF-C, which activates VEGFR-2 and VEGFR-3 expressed in lymphatic endothelial cells.
Positive_regulation (activation) of VEGFR-2 in endothelial cells
1) Confidence 0.45 Published 2010 Journal BMC Med Section Body Doc Link PMC2989928 Disease Relevance 1.22 Pain Relevance 0
3-null endothelial cells have elevated VEGFR2 (Flk-1) levels [12], [27], [53], even after Rac1-depletion, indicates that elevated VEGFR2 levels alone are not sufficient to enhance angiogenesis.
Positive_regulation (elevated) of VEGFR2 in endothelial cells
2) Confidence 0.36 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2842301 Disease Relevance 0.24 Pain Relevance 0
3-null endothelial cells have elevated VEGFR2 (Flk-1) levels [12], [27], [53], even after Rac1-depletion, indicates that elevated VEGFR2 levels alone are not sufficient to enhance angiogenesis.
Positive_regulation (elevated) of Flk-1 in endothelial cells
3) Confidence 0.36 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2842301 Disease Relevance 0.26 Pain Relevance 0
3-null endothelial cells have elevated VEGFR2 (Flk-1) levels [12], [27], [53], even after Rac1-depletion, indicates that elevated VEGFR2 levels alone are not sufficient to enhance angiogenesis.
Positive_regulation (elevated) of VEGFR2 in endothelial cells
4) Confidence 0.36 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2842301 Disease Relevance 0.26 Pain Relevance 0
The growth of blood vessels (angiogenesis) is primarily initiated by activation of VEGFR-1 and VEGFR-2 by VEGF-A, whereas lymphangiogenesis is predominantly driven by VEGF-C, which activates VEGFR-2 and VEGFR-3 expressed in lymphatic endothelial cells.
Positive_regulation (activates) of VEGFR-2 in endothelial cells
5) Confidence 0.33 Published 2010 Journal BMC Med Section Body Doc Link PMC2989928 Disease Relevance 1.18 Pain Relevance 0
The increase in VEGFR2 gene activation reached a maximum after 7–10 days after the wound was inflicted [29].
Positive_regulation (increase) of VEGFR2 gene associated with injury
6) Confidence 0.31 Published 2010 Journal Angiogenesis Section Body Doc Link PMC2911541 Disease Relevance 0.85 Pain Relevance 0.14
3-integrin results in viable, fertile animals which display enhanced pathological angiogenesis due in part to the up-regulation of VEGFR2 [12], whereas in a transgenic model, where the cytoplasmic tail of ?
Positive_regulation (up-regulation) of VEGFR2 in tail associated with targeted disruption and pathologic neovascularization
7) Confidence 0.29 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2842301 Disease Relevance 0.73 Pain Relevance 0
On a related note, sVEGFR-3 can not only bind VEGFR-3 but also acts as a trap for VEGF-C, which blocks VEGFR-3 signaling [2,5].
Positive_regulation (acts) of sVEGFR-3
8) Confidence 0.27 Published 2010 Journal BMC Med Section Body Doc Link PMC2989928 Disease Relevance 1.12 Pain Relevance 0.05
These mediators are stimulated by VEGF-induced VEGFR2 signaling, which is blocked by sorafenib and sunitinib treatment.
Positive_regulation (induced) of VEGFR2
9) Confidence 0.21 Published 2010 Journal Journal of Oncology Section Body Doc Link PMC2902148 Disease Relevance 1.50 Pain Relevance 0
The cells were then trypsinized for 1 minute, centrifuged, washed with PBS, fixed in 4% paraformaldehyde for 0.5 hour at room temperature, washed and blocked in 2%FCS for 0.5 hour at room temperature with agitation. 1.5×105cells were then incubated with each of the following conjugated monoclonal antibodies: Tie-2, Flk-1, CD34, c-Kit, Thy-1, Sca-1 (PharMingen, San Diego, CA) for 90 mins at room temperature.
Positive_regulation (incubated) of Flk-1
10) Confidence 0.13 Published 2006 Journal PLoS ONE Section Body Doc Link PMC1762397 Disease Relevance 0.24 Pain Relevance 0.06
During angiogenesis, including tumor angiogenesis, both VEGF and VEGFR2 expression are locally upregulated [25–28].
Positive_regulation (upregulated) of VEGFR2 associated with cancer
11) Confidence 0.13 Published 2010 Journal Angiogenesis Section Body Doc Link PMC2911541 Disease Relevance 0.25 Pain Relevance 0.24
Differential expression of isoforms of the transcription factor HIF and the subsequent induction of target genes such as VEGFR-1 and VEGFR-2 appear responsible for the response to hypoxia in hypertrophied hearts.
Positive_regulation (induction) of VEGFR in hearts associated with hypoxia
12) Confidence 0.09 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2603310 Disease Relevance 1.10 Pain Relevance 0.03
Unlike the non-hypertrophied heart, hypoxia further increased VEGF-1 expression without a concomitant increase in the pro-angiogenic receptor, VEGFR-2.
Neg (without) Positive_regulation (increase) of VEGFR in heart associated with hypoxia
13) Confidence 0.06 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2603310 Disease Relevance 0.58 Pain Relevance 0
Like E-RoSH cells, plating of E-RoSHL1 cells on matrigel dramatically increased expression of endothelial markers such as Tie-2, Flk-1, c-kit, Sca1 and thy1 within 60 hours (fig. 5d) and they formed a network of vascular structures that covered the entire culture dish after one week (fig. 5e).


Positive_regulation (ly increa) of Flk-1
14) Confidence 0.05 Published 2006 Journal PLoS ONE Section Body Doc Link PMC1762397 Disease Relevance 0 Pain Relevance 0
Knowing that defective placentation due to increased antiangiogenic soluble receptor for vascular endothelial growth factor 1 (sFlt-1) can trigger PE in rodents and women [7], [8] and that inflammation has been implicated in the pathogenesis of PE [9], [10] led as to investigate if the CBA/J x DBA/2 mating model constitutes a model of PE.
Positive_regulation (increased) of antiangiogenic soluble receptor associated with inflammation and pre-eclampsia
15) Confidence 0.02 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2965104 Disease Relevance 1.03 Pain Relevance 0.05
Signals for endothelial cells are mediated through VEGFR-2 in blood vascular endothelial cells, and generally via VEGFR-3 in the lymphatic endothelial cells (29,41).
Positive_regulation (mediated) of VEGFR-2 in blood
16) Confidence 0.02 Published 2009 Journal Parasite Immunology Section Body Doc Link PMC2784903 Disease Relevance 0.58 Pain Relevance 0.20

General Comments

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