INT247759

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Context Info
Confidence 0.26
First Reported 2008
Last Reported 2008
Negated 3
Speculated 0
Reported most in Body
Documents 1
Total Number 21
Disease Relevance 1.19
Pain Relevance 0.90

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) extracellular region (Rarres2) plasma membrane (Ccrl2)
signal transducer activity (Ccrl2)
Anatomy Link Frequency
mast cells 3
NK cells 1
Ccrl2 (Mus musculus)
Rarres2 (Mus musculus)
Pain Link Frequency Relevance Heat
Potency 42 99.92 Very High Very High Very High
Inflammation 168 98.60 Very High Very High Very High
chemokine 693 86.20 High High
cytokine 126 78.36 Quite High
Bioavailability 21 73.72 Quite High
agonist 21 53.44 Quite High
Inflammatory response 63 5.00 Very Low Very Low Very Low
ketamine 21 5.00 Very Low Very Low Very Low
anesthesia 21 5.00 Very Low Very Low Very Low
Multiple sclerosis 21 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
INFLAMMATION 231 98.60 Very High Very High Very High
Anaphylaxis 609 97.08 Very High Very High Very High
Edema 399 94.16 High High
Contact Dermatitis 147 82.20 Quite High
Hypersensitivity 42 60.40 Quite High
Disease 42 5.00 Very Low Very Low Very Low
Demyelinating Disease 21 5.00 Very Low Very Low Very Low
Overdose 21 5.00 Very Low Very Low Very Low
Lymphatic System Cancer 21 5.00 Very Low Very Low Very Low
Cancer 21 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
The identification of chemerin as a nonsignaling ligand for CCRL2 introduces a novel functionality for atypical receptors (i.e., concentration and presentation, as we have shown herein for CCRL2, as opposed to internalization/degradation).
CCRL2 Binding (ligand) of chemerin
1) Confidence 0.26 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0.17 Pain Relevance 0.17
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 chemerin in NK cells
2) Confidence 0.26 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0.18 Pain Relevance 0.07
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 chemerin
3) Confidence 0.26 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0 Pain Relevance 0.04
The binding affinity of chemerin for CCRL2 was similar to, if not slightly better than, chemerin binding to the first identified chemerin receptor, mCMKLR1 (EC50 = 3.1 nM; Fig. 6 B).
CCRL2 Binding (affinity) of chemerin
4) Confidence 0.22 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0 Pain Relevance 0
The evolutionary conservation of chemerin binding to CCRL2 despite divergence in overall sequence between mouse and human receptors strongly suggests that the interaction of chemerin with CCRL2 is physiologically important.
CCRL2 Binding (interaction) of chemerin
5) Confidence 0.22 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0 Pain Relevance 0.03
Chemerin binding to CCRL2 was not affected by a variety of other chemoattractants (Fig.
CCRL2 Binding (binding) of Chemerin
6) Confidence 0.22 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0 Pain Relevance 0
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 chemerin in Mast cell associated with anaphylaxis
7) Confidence 0.22 Published 2008 Journal The Journal of Experimental Medicine Section Title Doc Link PMC2556791 Disease Relevance 0.27 Pain Relevance 0.04
CCRL2 does not internalize chemerin
CCRL2 Neg (not) Binding (internalize) of chemerin
8) Confidence 0.20 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0 Pain Relevance 0.07
S8 shows the displacement of iodinated chemerin (residues 21–148) binding to CCRL2 and CMKLR1 by His8-chemerin and bioactive chemerin peptide (YFPGQFAFS).
CCRL2 Binding (binding) of chemerin
9) Confidence 0.19 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0.26 Pain Relevance 0.04
CCRL2 binds chemerin
CCRL2 Binding (binds) of chemerin
10) Confidence 0.19 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0.32 Pain Relevance 0.04
The carboxyl-terminal domain of chemerin that is critical for binding to CMKLR1 is relatively uninvolved and unencumbered when chemerin is bound to CCRL2.
CCRL2 Binding (bound) of chemerin
11) Confidence 0.19 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0 Pain Relevance 0.08
Finally, peritoneal mast cells from mCCRL2 KO mice did not bind to chemerin, further confirming the role of CCRL2 in the binding of chemerin to such mast cells (Fig. 6 E).


CCRL2 Neg (not) Binding (bind) of chemerin in mast cells
12) Confidence 0.19 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0 Pain Relevance 0.05
Despite high-affinity binding to mCCRL2, chemerin failed to trigger intracellular calcium mobilization in mCCRL2/L1.2 transfectants (Fig. 7 A).
mCCRL2 Binding (binding) of chemerin
13) Confidence 0.19 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0 Pain Relevance 0.03
The carboxyl-terminal domain of chemerin that is critical for binding to CMKLR1 is relatively uninvolved and unencumbered when chemerin is bound to CCRL2.
CCRL2 Binding (bound) of chemerin
14) Confidence 0.19 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0 Pain Relevance 0.07
The evolutionary conservation of chemerin binding to CCRL2 despite divergence in overall sequence between mouse and human receptors strongly suggests that the interaction of chemerin with CCRL2 is physiologically important.
CCRL2 Binding (binding) of chemerin
15) Confidence 0.19 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0 Pain Relevance 0.03
In radioligand binding studies, the His8 tag had little effect on the potency of chemerin binding to mCCRL2 (EC50 = 0.8 nM); however, His8-tagged chemerin bound with 10-fold less potency to mCMKLR1 (EC50 = 26.3 nM; Fig.
mCCRL2 Binding (binding) of chemerin associated with potency
16) Confidence 0.17 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0 Pain Relevance 0.10
Furthermore, despite being the most divergent mouse-to-man orthologues in the chemoattractant receptor subfamily, huCCRL2 also bound specifically to chemerin (EC50 = 0.2 nM; Fig. 6 B).
huCCRL2 Binding (bound) of chemerin
17) Confidence 0.17 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0 Pain Relevance 0
In saturation binding studies, chemerin bound to mCCRL2 at a single binding site with a calculated kD of 1.6 nM (Fig. 6 C).
mCCRL2 Binding (bound) of chemerin
18) Confidence 0.17 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0 Pain Relevance 0
In this assay, chemerin bound specifically to mCCRL2-HA (EC50 = 45 nM) and huCCRL2 (EC50 = 7 nM) L1.2 transfectants (Fig. 6 D).
mCCRL2-HA Binding (bound) of chemerin
19) Confidence 0.17 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0 Pain Relevance 0
Finally, peritoneal mast cells from mCCRL2 KO mice did not bind to chemerin, further confirming the role of CCRL2 in the binding of chemerin to such mast cells (Fig. 6 E).


mCCRL2 Neg (not) Binding (bind) of chemerin in mast cells
20) Confidence 0.17 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0 Pain Relevance 0.06

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