INT247731

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Context Info
Confidence 0.35
First Reported 2008
Last Reported 2008
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 13
Disease Relevance 1.38
Pain Relevance 0.87

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

signal transduction (Ccrl2) plasma membrane (Ccrl2) signal transducer activity (Ccrl2)
Anatomy Link Frequency
Mast cell 2
NK cells 1
Ccrl2 (Mus musculus)
Pain Link Frequency Relevance Heat
chemokine 429 96.68 Very High Very High Very High
Inflammation 104 94.84 High High
Potency 26 88.20 High High
anesthesia 13 79.28 Quite High
ketamine 13 78.32 Quite High
Bioavailability 13 73.72 Quite High
cytokine 78 62.32 Quite High
agonist 13 21.80 Low Low
Inflammatory response 39 5.00 Very Low Very Low Very Low
Multiple sclerosis 13 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Anaphylaxis 377 96.72 Very High Very High Very High
INFLAMMATION 143 94.84 High High
Edema 247 94.16 High High
Overdose 13 80.24 Quite High
Lymphatic System Cancer 13 69.04 Quite High
Hypersensitivity 26 59.44 Quite High
Cancer 13 47.96 Quite Low
Increased Venous Pressure Under Development 13 33.60 Quite Low
Contact Dermatitis 91 5.00 Very Low Very Low Very Low
Disease 26 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Transfectant-expressed CCRL2 has been reported to bind CCL2 and CCL5, although this result is controversial (9).
CCRL2 Binding (bind) of
1) Confidence 0.35 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0 Pain Relevance 0.12
To ask whether CCRL2 might have interceptor activity, we assessed the internalization of CCRL2, and of CMKLR1 for comparison, in response to ligand binding. mCMKLR1-HA internalized rapidly (within 15 min) in response to 100 nM chemerin, and this internalization was inhibited by incubation on ice and in the presence of sodium azide (Fig. 8 A), confirming that the effect is an active process (not caused by chemerin-mediated displacement of the anti-HA mAb).
CCRL2 Binding (internalization) of
2) Confidence 0.27 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0 Pain Relevance 0.09
CCRL2 binds chemerin
CCRL2 Binding (binds) of
3) Confidence 0.27 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0.32 Pain Relevance 0.04
Mast cell–expressed orphan receptor CCRL2 binds chemerin and is required for optimal induction of IgE-mediated passive cutaneous anaphylaxis

Mast cells contribute importantly to both protective and pathological IgE-dependent immune responses.

CCRL2 Binding (binds) of in Mast cell associated with anaphylaxis
4) Confidence 0.26 Published 2008 Journal The Journal of Experimental Medicine Section Title Doc Link PMC2556791 Disease Relevance 0.27 Pain Relevance 0.04
Thus, it appears that CCRL2 binds and indeed concentrates chemerin on the cell surface.
CCRL2 Binding (binds) of
5) Confidence 0.26 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0 Pain Relevance 0
Rather, CCRL2 is able to bind the chemoattractant and increase local concentrations of bioactive chemerin, thus providing a link between CCRL2 expression and inflammation via the cell-signaling chemerin receptor CMKLR1.



CCRL2 Binding (bind) of associated with inflammation
6) Confidence 0.26 Published 2008 Journal The Journal of Experimental Medicine Section Abstract Doc Link PMC2556791 Disease Relevance 0.34 Pain Relevance 0.10
Thus, we hypothesize that CCRL2 (e.g. expressed by mast cells and activated macrophages) binds to chemerin in vivo and presents the cell-signaling carboxyl-terminal domain of the chemoattractant to CMKLR1+ cells such as macrophages, pDC, and NK cells (Fig. 9).
CCRL2 Binding (binds) of in NK cells
7) Confidence 0.26 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0.18 Pain Relevance 0.07
In addition, using either the binding conditions published in this paper for chemerin or those published by Biber et al. (9) for CCL2, we were unable to confirm the binding of biotinylated CCL2 to CCRL2/L1.2 transfectants (unpublished data).
CCRL2 Binding (binding) of
8) Confidence 0.26 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0 Pain Relevance 0.08
Furthermore, CCRL2 binds to chemerin in an orientation that permits antibody access to the short C-terminal His8 tag, suggesting that the critical cell-signaling carboxyl terminus of chemerin would also be exposed in the untagged form of the protein.
CCRL2 Binding (binds) of
9) Confidence 0.26 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0 Pain Relevance 0.04
In CCRL2 binding, however, the bioactive chemerin peptide was an inefficient competitor (EC50 could not be determined, Fig.
CCRL2 Binding (binding) of
10) Confidence 0.26 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0 Pain Relevance 0.09
Hybridomas producing anti-mCCRL2 mAbs were subcloned, and specificity was confirmed by reactivity with mCCRL2 but not other L1.2 receptor transfectants.
mCCRL2 Binding (reactivity) of
11) Confidence 0.23 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0.14 Pain Relevance 0.12
Wistar Furth rats were immunized with the mCCRL2 peptide/KLH conjugate, first emulsified in CFA and then, subsequently, in IFA.
mCCRL2 Binding (immunized) of
12) Confidence 0.23 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0.13 Pain Relevance 0.10
Although we failed to identify evidence of signaling effects of any of the tested chemoattractants, we were able to identify a high-affinity ligand for the receptor: in independent studies in which we were using our anti-CCRL2 mAbs as controls for staining, we serendipitously discovered that chemerin, a protein ligand for signaling receptor CMKLR1 (for review see reference 28), inhibited the binding of mCCRL2-specific mAbs to mouse peritoneal mast cells.
mCCRL2-specific Binding (binding) of in mast cells
13) Confidence 0.23 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0 Pain Relevance 0

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