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chemerin receptor 1

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Immunopharmacology Ligand  Target has curated data in GtoImmuPdb

Target id: 79

Nomenclature: chemerin receptor 1

Abbreviated Name: Chemerin1

Family: Chemerin receptors

Contents:

Gene and Protein Information Click here for help
class A G protein-coupled receptor
Species TM AA Chromosomal Location Gene Symbol Gene Name Reference
Human 7 373 12q23.3 CMKLR1 chemerin chemokine-like receptor 1 20
Mouse 7 371 5 F Cmklr1 chemerin chemokine-like receptor 1 42
Rat 7 371 12q16 Cmklr1 chemerin chemokine-like receptor 1 44
Previous and Unofficial Names Click here for help
Chemerin1 [31] | chemokine receptor-like 1 | CMKLR1 | Gpcr27 | G-protein coupled receptor ChemR23 | G-protein coupled receptor DEZ | resolvin E1 receptor | RVER1 | tazarotene induced gene 2 receptor | TIG2 receptor
Database Links Click here for help
Specialist databases
GPCRdb cml1_human (Hs), cml1_mouse (Mm), cml1_rat (Rn)
Other databases
Alphafold Q99788 (Hs), P97468 (Mm), O35786 (Rn)
ChEMBL Target CHEMBL3540 (Hs), CHEMBL4523269 (Mm)
Ensembl Gene ENSG00000174600 (Hs), ENSMUSG00000042190 (Mm), ENSRNOG00000000704 (Rn)
Entrez Gene 1240 (Hs), 14747 (Mm), 60669 (Rn)
Human Protein Atlas ENSG00000174600 (Hs)
KEGG Gene hsa:1240 (Hs), mmu:14747 (Mm), rno:60669 (Rn)
OMIM 602351 (Hs)
Pharos Q99788 (Hs)
RefSeq Nucleotide NM_004072 (Hs), NM_008153 (Mm), NM_022218 (Rn)
RefSeq Protein NP_004063 (Hs), NP_032179 (Mm), NP_071554 (Rn)
UniProtKB Q99788 (Hs), P97468 (Mm), O35786 (Rn)
Wikipedia CMKLR1 (Hs)
Natural/Endogenous Ligands Click here for help
chemerin {Sp: Human}
resolvin E1
Potency order of endogenous ligands
resolvin E1 > chemerin C-terminal peptide > 18R-HEPE > EPA  [2]

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Agonists
Key to terms and symbols View all chemical structures Click column headers to sort
Ligand Sp. Action Value Parameter Reference
chemerin {Sp: Human} Peptide Click here for species-specific activity table Ligand is endogenous in the given species Hs Full agonist 8.3 pKd 4
⤷ pKd 8.3 (Kd 4.9x10-9 M) [4]
[3H]resolvin E1 Small molecule or natural product Ligand is labelled Ligand is radioactive Immunopharmacology Ligand Hs Agonist 7.9 pKd 2-3
⤷ pKd 7.9 (Kd 1.1x10-8 M) [2-3]
resolvin E1 Small molecule or natural product Ligand is endogenous in the given species Immunopharmacology Ligand Hs Full agonist 7.9 pKd 2-3,59
⤷ pKd 7.9 (Kd 1.13x10-8 M) [2-3,59]
chemerin C-terminal peptide Peptide Click here for species-specific activity table Hs Full agonist 7.6 – 8.1 pKd 4,62
⤷ pKd 7.6 – 8.1 (Kd 2.4x10-8 – 7.1x10-9 M) [4,62]
chemerin {Sp: Human} Peptide Click here for species-specific activity table Hs Full agonist 7.6 – 8.5 pEC50 4,24,55,61-62
⤷ pEC50 7.6 – 8.5 (EC50 4.5x10-9 – 3x10-9 M) [4,55,61-62]
pEC50 8.0 (EC50 9.7x10-9 M) [24]
Description: In a β-arrestin recruitment assay.
tethered chemerin 9 Peptide Immunopharmacology Ligand Hs Agonist ~8.3 pIC50 14,61
⤷ pIC50 ~8.3 (IC50 ~5.5x10-9 M) [14,61]
Description: Binding affinity in a radioligand displacement assay using membranes prepared from chemerinR-expressing CHO-K1 cells and 125I-YHSFFFPGQFAFS as tracer.
Agonist Comments
Nonapeptide (149)YFPGQFAFS(157) (chemerin C-terminal peptide/chemerin-9), corresponding to the C terminus of processed chemerin, retains most of the activity of the full-size protein, with regard to agonism towards the chemerin receptor. Alanine-scanning mutagenesis identified residues Tyr(149), Phe(150), Gly(152), Phe(154), and Phe(156) as the key positions for receptor activation [62]. Removal of a single amino acid from the C-terminal of chemerin resulted in a peptide able to activate the receptor but with a 6-fold drop of potency [62]. Chemerin15 (C15; A140-A154), inhibited macrophage (MΦ) activation to a similar extent as proteolyzed chemerin, but exhibited reduced activity as a MΦ chemoattractant [10].

Serum chemerin levels have been shown to oscillate in a diurnal-type rhythmn [45].
Antagonists
Key to terms and symbols View all chemical structures Click column headers to sort
Ligand Sp. Action Value Parameter Reference
compound 14f [PMID: 35063894] Small molecule or natural product Immunopharmacology Ligand Hs Antagonist 7.9 pIC50 27
⤷ pIC50 7.9 (IC50 1.2x10-8 M) [27]
S-26d [PMID: 37883692] Small molecule or natural product Immunopharmacology Ligand Hs Antagonist 7.4 pIC50 33
⤷ pIC50 7.4 (IC50 3.63x10-8 M) [33]
Description: Determined in hCMKLR1-transfected CHO cells, measuring antagonism of agonist-induced intracellular calcium mobilisation
α-NETA Small molecule or natural product Immunopharmacology Ligand Hs Antagonist 6.4 pIC50 24
⤷ pIC50 6.4 (IC50 3.75x10-7 M) [24]
Description: Antagonism of chemerin-stimulated β-arrestin 2 recruitment to CMKLR1 in a cellular assay.
LC52-0332 Small molecule or natural product Hs Antagonist 5.2 pIC50 33
⤷ pIC50 5.2 (IC50 5.7x10-6 M) [33]
Antagonist Comments
CCX832 (structure not disclosed) is a selective antagonist, pKi=9.2 [32].
Immunopharmacology Comments
Studies in CMKLR1 (chemerin receptor 1) knockout mice highlight the role of this receptor in inflammation and obesity. Chemerin receptor 1 is activated by the lipid-derived, anti-inflammatory autacoid ligand resolvin E1. As its name suggests, reslovin E1 is involved in resolving physiological inflammatory responses. The metabolically stable resolvin E1 analogue, RX-10045 (navamepent) has completed Phase 2 clinical trials in several occular inflammation indications. In relation to multiple sclerosis (MS), clinical EAE is significantly reduced in CMKLR1 KO mice. Taking this in to consideration with data that confirm CMKLR1 expression by the main effector cells in MS, this protein is judged to be a novel and tractable target for therapeutic intervention in MS. CMKLR1 antagonists are being pursued as anti-inflammatory agents. The selective CMKLR1 antagonist CCX832 was developed by ChemoCentryx and GlaxoSmithKline as a potential anti-psoriatic medication, but development appears to have halted at Phase 1. α-NETA is a CMKLR1 antagonist that has shown efficacious effects applicable to MS in vitro and in vivo [24].
Immuno Process Associations
Immuno Process:  Inflammation
Immuno Process:  Immune regulation
Immuno Process:  Cytokine production & signalling
Immuno Process:  Chemotaxis & migration
Immuno Process:  Cellular signalling
Primary Transduction Mechanisms Click here for help
Transducer Effector/Response
Gi/Go family Adenylyl cyclase inhibition
Comments:  Activation of the receptor results in intracellular calcium release, inhibition of cAMP accumulation, and phosphorylation of p42-p44 MAP kinases [61].
References:  61
Tissue Distribution Click here for help
CD41+ platelets
Species:  Human
Technique:  Immunocytochemistry
References:  19
Spleen, thymus, appendix, lymph node, bone marrow, and fetal liver
Species:  Human
Technique:  Northern blot
References:  20
Endothelium (macro- and microvessels)
Species:  Human
Technique:  RT-PCR, immunocytochemistry
References:  30
Preadipocytes (low); adipocytes (high)
Species:  Human
Technique:  RT-PCR
References:  50
Primary adipocytes, skeletal muscle
Species:  Human
Technique:  Western blot
References:  52
Cardiovascular system and peripheral blood leukocytes (monocytes, neutrophils, T lymphocytes), brain, kidney, gastrointestinal tissues, and myeloid tissues
Species:  Human
Technique:  Dot blots
References:  2
Plasmacytoid dendritic cells
Species:  Human
Technique:  Immunohistochemistry
References:  53-54
Circulating dendritic cells. Negative in monocytes, lymphocytes, neutrophils and eosinophils
Species:  Human
Technique:  Immunohistochemistry, novel monoclonal Ab
References:  67
Secondary lymphoid organs: CD123+ plasmacytoid DCs and CD1a+ DC-SIGN + DCs, luminal side of high endothelial venules; dermis (dendritic cells)
Species:  Human
Technique:  Immunohistochemistry
References:  60
Monocyte-derived dendritic cells, macrophages; low expression in CD4+ T lymphocytes
Species:  Human
Technique:  Northern blot, RT-PCR
References:  51
Synovial fibroblasts
Species:  Human
Technique:  Immunohistochemistry
References:  16
Primary human granulosa cells, human ovarian granulosa-like tumour cell line (KGN)
Species:  Human
Technique:  RT-PCR, Immunoblotting, immunohistochemistry
References:  48
Blood CD56lowCD16+ natural killer cells
Species:  Human
Technique:  Immunohistochemistry and immunocytochemistry
References:  46
Articular chondrocytes
Species:  Human
Technique:  RT-PCR, immunohistochemistry
References:  6
Osseous tissue, cartilage, parathyroid glands
Species:  Mouse
Technique:  In situ hybridisation
References:  36
Brain
Species:  Mouse
Technique:  RT-PCR
References:  36
White adipose tissue, liver, placenta (high); ovary (intermediate)
Species:  Mouse
Technique:  RT-PCR
References:  21
Adipocytes and stomal vascular cells of adipose tissue
Species:  Mouse
Technique:  RT-PCR
References:  8
Microglial cells, CNS-infiltrating myeloid dendritic cells
Species:  Mouse
Technique:  Immunocytochemistry
References:  23
Macrophage and monocyte-macrophage primary endothelial cells
Species:  Mouse
Technique:  Immunocytochemistry
References:  25
Spleen, pancreas (high); skeletal muscle, liver (medium); brain, adipose tissue (low)
Species:  Mouse
Technique:  RT-PCR
References:  5
Peritoneal macrophages, tumour infiltrating macrophages
Species:  Mouse
Technique:  Immunohistochemistry, immunohistochemistry
References:  47
Developing bone
Species:  Mouse
Technique:  In situ hybridisation
References:  2
Adipose tissue, adipocytes, low ubiquitous expression
Species:  Mouse
Technique:  RT-PCR
References:  50
Small intestine (low), heart, lung, colon, kidney, liver, uterus, brain
Species:  Rat
Technique:  RT-PCR
References:  44
Vascular distribution in liver and kidney
Species:  Rat
Technique:  In situ hybridisation
References:  44
Tissue Distribution Comments
In dendritic cell differentiation from bone marrow, murine CMKLR1 is upregulated early and then diminishes with time in culture [66].

CMKLR1 expression is upregulated in adipose tissue of mice fed a high fat diet. Troglitazone, a PPAR-γ2 agonist, treatment also significantly increases CMKLR1 expression [50]. The chemerin receptor is coexpressed with CXCR1 and CXCL8 receptors in blood CD56lowCD16+ natural killer cells [46]. CMKLR1 is expressed ubiquitously in tissues from P. obesus, and differentially from chemerin in mesenteric tissue. CMKLR1 was also downregulated in adipocyte differentiation [8].

CMKLR1+ cells in kidney from SLE patients with nephritis, mostly localized at tubulointerstitial level surrounding tubular epithelial cells, with a typical DC pattern. Moreover, CMKLR1+ cells frequently localized around the glomeruli and were also associated with renal vessels [12].

Cigarette smoke decreases preprochemerin and CMKLR1 mRNA expression in the lung [13]. Homocysteine, uric acid, high glucose, or oxidized low-density lipoprotein down-regulated the chemerin secretion and CMKLR1 expression in rat aortic endothelial cells [68]. Synovial fibroblasts expressed chemerin receptor and chemerin mRNA, in rheumatoid- and osteo-arthritis patients [16]. CMKLR1 was expressed in a 3T3-L1 adipocyte cell line and examined with RT-PCR [5], and a J744A.1 cell line using immunocytochemistry and immunohistochemistry [47].

CMKLR1 levels also increased during differentiation and decreased again with full differentiation of primary human adipocytes after 13 days [52]. CMKLR1 mRNA levels have been reported as approximately 5-fold lower in skeletal muscle and 36-fold lower in liver tissue relative to white adipose tissue (using RT-PCR) [18]. TNF-α and IL-1β both dose-dependently increase receptor expression in human endothelial cells [30]. Of interest to cardiovascular medicine, CMKLR1 has also been identified on vascular smooth muscle cells [59]. Upregulation of CMKLR1 on F4/80+ macrophages is favored by the tumor cells [47].

CMKLR1 has been expressed in a murine NH15-CA2 cell line and detected by Northern blot analysis [36]. Other murine cell lines used to express the receptor are neuroblastoma NB4 1A3 cells and microglia BV2 cells [40,42]. CMKLR1 has been expressed at at low level in the human 3T3-L1 cell line and analysed by RT-PCR [50], and has also been expressed in a murine 3T3-L1 adipocyte cell line, also analysed by RT-PCR [5].
Expression Datasets Click here for help

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Log average relative transcript abundance in mouse tissues measured by qPCR from Regard, J.B., Sato, I.T., and Coughlin, S.R. (2008). Anatomical profiling of G protein-coupled receptor expression. Cell, 135(3): 561-71. [PMID:18984166] [Raw data: website]

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Functional Assays Click here for help
CMKLR1 expression was found to be associated with the fibroblast-assisted maturation of J744A.1 monocyte/macrophage cells in the co-cultures established to model tumor microenvironment.
Species:  Human
Tissue:  Macrophages
Response measured:  The presence of tumor cells was able to upregulate CMKLR1 expression independent of macrophage maturation.
References:  47
Stimulating cells with chemerin results in phosphorylation of p44/p42 MAPKs (ERK 1/2) and Akt (Ser 473).
Species:  Human
Tissue:  Articular chondrocytes (cartilage)
Response measured:  Significantly enhanced levels of the pro-inflammatory cytokines IL-6, IL-8, TNF-α, IL-1β, and the matrix metalloproteases MMP-1, MMP-2, MMP-3, MMP-8 and MMP-13.
References:  6
Chemerin peptides promote phagocytosis in a ChemR23- and Syk-dependent manner
Species:  Mouse
Tissue:  Macrophages
Response measured:  Enhanced macrophage phagocytosis of microbial particles and apoptotic cells in vitro
References:  9
When recombinant P2Y12–expressing cells were transiently transfected with CMKLR1 (present on human platelets), addition of RvE1 blocked ADP signals in P2Y12–CMKLR1–expressing cells compared with mock transfections
Species:  Human
Tissue:  Platelets
Response measured:  RvE1’s regulatory actions, reducing ADP-stimulated P-selectin mobilization and actin polymerization, are human CMKLR1-dependent
References:  19
RvE1 stimulates the phosphorylation of ribosomal protein S6, and enhances phagocytosis of zymosan A by human macrophages
Species:  Human
Tissue:  Differentiated HL60 cells
Response measured:  Direct activation of CMKLR1 and signals receptor-dependent phosphorylation
References:  43
Iptakalim via opening KATP channels enhanced the endothelial chemerin/ChemR23 axis
Species:  Rat
Tissue:  Aortic endothelium
Response measured:  Improved NO secretion and endothelial function
References:  68
Tumour necrosis factor α and obesity increase concentrations of bioactive chemerin and receptor activation
Species:  Mouse
Tissue:  Adipocytes
Response measured:  Increased activation of CMKLR1 (Tango cell assay)
References:  37
Chemerin promotes calcium mobilization and chemotaxis of immature dendritic cells and macrophages in a CMKLR1-dependent manner
Species:  Human
Tissue:  Dendritic cells and macrophages
Response measured:  Chemotaxis
References:  61
RvE1-receptor interaction blocks splenic dendritic cell response to pathogen
Species:  Mouse
Tissue:  Spleen
Response measured:  Mobilisation of dendritic cells to T cell-enriched areas and production of IL-12
References:  2
Recombinant chemerin induced the transmigration of plasmacytoid and myeloid dendritic cells which express CMKLR1 across an endothelial cell monolayer
Species:  Human
Tissue:  Dendritic cells
Response measured:  Directed migration
References:  60
Macrophage receptor expression is regulated by cytokines
Species:  Human
Tissue:  Macrophages
Response measured:  Macrophage mCMKLR1 is suppressed by proinflammatory cytokines and TLR ligands, whereas treatment with TGF-β upregulates the receptor
References:  66
Treatment with human recombinant chemerin clearly stimulated ERK 1/2 phosphorylation in differentiated 3T3-L1 cells
Species:  Mouse
Tissue:  3T3-L1 cells
Response measured:  ERK1/2 phosphorylation
References:  50
CMKLR1/L1.2 cells showed little migration to proteins extracted from the skin of normal individuals, but migrated significantly to protein extracts from lesional skin of psoriasis patients
Species:  Human
Tissue:  Skin (L1.2 cells)
Response measured:  Increased migration in lesional skin
References:  54
Chemerin stimulates the adhesion of macrophages through the chemerin receptor
Species:  Mouse
Tissue:  Macrophages
Response measured:  Cells adhere to fibronectin and VCAM-1 in response to chemerin stimulation
References:  25
In vitro culturing of NK cells with IL-2 or IL-15 induces a delayed and time-dependent down-regulation of CMKLR1 that was associated with the inhibition of NK cell migration to chemerin
Species:  Human
Tissue:  Natural killer cells
Response measured:  Inhibited chemotaxis
References:  46
Physiological Functions Click here for help
The chemerin receptor is expressed in NK cells involved in resolvin E1-mediated resolution of allergic airway inflammation
Species:  Mouse
Tissue:  Lung
References:  26
CMKLR1-dependent recruitment of plasmacytoid dendritic cells contributes to adaptive immune responses and viral clearance, but also enhances the inflammatory response
Species:  Mouse
Tissue:  Lung
References:  7
Physiological Functions Comments
Potential roles have been postulated for the CMKLR1/chemerin signaling pathway as a modulator of bone mass (osteoblastgenesis), and angiogenesis [30,39].
Physiological Consequences of Altering Gene Expression Click here for help
Treatment of dendritic cells with small interference RNA specific for CMKLR1 sharply reduced RvE1 regulation of IL-12
Species:  Human
Tissue:  Dendritic cells
Technique:  RNA interference (RNAi)
References:  2
Forced expression of the adipogenic transcription factor peroxisome proliferator-activated receptor γ induced chemerin expression and partially rescued the loss of adipogenesis associated with chemerin or CMKLR1 knockdown in BMSCs
Species:  None
Tissue:  Bone marrow stromal cells
Technique:  RNA interference (RNAi)
References:  39
Receptor knockout mice display higher mortality/morbidity, alteration of lung function, delayed viral clearance and increased neutrophilic infiltration in murine viral pneumonia. Lower recruitment of plasmacytoid dendritic cells and a reduction in type I interferon production is seen. Increased morbidity/mortality is not due to defective plasmacytoid dendritic cells recruitment, but rather to the loss of an anti-inflammatory pathway involving CMKLR1 expressed by non-leukocytic cells.
Species:  Mouse
Tissue:  Lung
Technique:  Gene knock-outs
References:  7
Regardless of diet CMKLR1(-/-) mice had lower food consumption, total body mass, and percent body fat compared with wild-type controls. Knockout mice also exhibited decreased hepatic and white adipose tissue TNFα and IL-6 mRNA levels, and were glucose intolerant.
Species:  Mouse
Tissue:  Adipose tissue
Technique:  Gene knockouts
References:  17
Knockdown of chemerin or CMKLR1 expression arrested adipogenic clonal expansion of bone marrow mesenchymal stem cells by inducing a loss of G2/M cyclins (cyclin A2/B2), but not the G1/S cyclin D2
Species:  Rat
Tissue:  Mesenchymal stem cells
Technique:  Gene knock-outs
References:  38
Increased expression of insulin receptor and IL-6. Small hairpin RNA targeted knockdown of chemerin or CMKLR1 expression impairs differentiation of 3T3-L1 cells into adipocytes, reduces the expression of adipocyte genes involved in glucose and lipid homeostasis, and alters metabolic functions in mature adipocytes
Species:  Mouse
Tissue:  3T3-L1 cells/adipocytes
Technique:  RNA interference (RNAi)
References:  21
Chemerin promotes calcium mobilization and chemotaxis on DCs and macrophages and these functional responses were abrogated in receptor knockout mice
Species:  Mouse
Tissue:  Macrophages, dendritic cells
Technique:  Gene knockouts
References:  34
Anti-inflammatory properties, reduced neutrophil infiltration and inflammatory cytokine release are inhibited in a receptor knockout mouse model of acute lung inflammation. Knockout mice also displayed an increased neutrophil infiltrate following LPS challenge.
Species:  Mouse
Tissue:  Neutrophils
Technique:  Gene knockouts
References:  34
Knockdown of CMKLR1 expression using RNA interference abrogated adipocyte differentiation, clonal expansion, and basal proliferation of BMSCs. In contrast increased osteoblast marker gene expression and mineralization in response to osteoblastogenic stimuli was also observed with receptor knockdown.
Species:  Human
Tissue:  Primary bone marrow stromal cells
Technique:  RNA interference (RNAi)
References:  39
C15 was unable to ameliorate zymosan-induced peritonitis in CMKLR1−/− mice, demonstrating that C15's anti-inflammatory effects are entirely CMKLR1 dependent. Receptor gene knockout ablates the antiinflammatory and chemotactic effects of chemerin mediated via CMKLR1.
Species:  Mouse
Tissue:  Neutrophils and monocytes
Technique:  Gene knockouts
References:  10
Prophagocytic effects of chemerin are significantly impaired in receptor knockout macrophages, associated with increased actin polymerization and localization of F-actin to the phagocytic cup. Additionally, during peritoneal inflammation, chemerin administration normally enhances microbial particle clearance and apoptotic neutrophil ingestion by macrophages, however this is lost in CMKLR1-/- mice.
Species:  Mouse
Tissue:  Macrophage
Technique:  Gene knockouts
References:  9
Decreasing CMKLR1 expression by adenoviral-delivered small-hairpin RNA (shRNA) impaired the differentiation of C(2)C(12) myoblasts into mature myotubes and reduced the mRNA expression of myogenic regulatory factors myogenin and MyoD while increasing Myf5 and Mrf4.
Species:  Mouse
Tissue:  Myoblasts
Technique:  RNA interference (RNAi)
References:  28
CMKRL1 knockout mice appear developmentally delayed and displayed significantly lower wet weights. Adult male CMKLR1(-/-) mice had significantly reduced bone-free lean mass and weighed less than the controls.
Species:  Mouse
Tissue:  Myotubes
Technique:  Gene knock-outs
References:  28
The chemerin receptor is a positive regulator of adipocyte differentiation and metabolic function in the 3T3-L1 model of adipogenesis
Species:  Mouse
Tissue:  Adipocytes
Technique:  Adenoviral mediated shRNA gene knockdown
References:  22
Chemerin was unable to promote the adhesion of PECs from CMKLR1−/− mice to fibronectin. However, a significant number of PECs from CMKLR1−/− mice were still capable of adhering to VCAM-1
Species:  Mouse
Tissue:  Macrophages (primary endothelial cells)
Technique:  Gene knockouts
References:  25
CMKLR1-deficient mice develop less severe clinical and histologic experimental autoimmune encephalomyelitis than their wild-type counterparts. Knockout lymphocytes proliferate and produce proinflammatory cytokines in vitro, yet MOG35–55-reactive CMKLR1 knockout lymphocytes are deficient in their ability to induce EAE by adoptive transfer to wild-type or CMKLR1 knockout recipients. Moreover, CMKLR1 knockout recipients fail to fully support EAE induction by transferred MOG-reactive wildtype lymphocytes
Species:  Mouse
Tissue:  Lymphocytes
Technique:  Gene knockouts
References:  23
Physiological Consequences of Altering Gene Expression Comments
In ob/ob mice, CMKLR1 mRNA was 2.3-fold lower in white adipose tissue and 4.8-fold higher in skeletal muscle compared with congenic C57BL/6 controls. Similarly, CMKLR1 levels were significantly lower (2.7-fold) in white adipose tissue and higher (4.3-fold) in skeletal muscle of db/db mice compared with C57BL/6 mice [18]. The receptor is also upregulated in mice on a high-fat diet [5].
Phenotypes, Alleles and Disease Models Click here for help Mouse data from MGI

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Allele Composition & genetic background Accession Phenotype Id Phenotype Reference
Cmklr1tm1Dgen Cmklr1tm1Dgen/Cmklr1tm1Dgen
B6.Cg-Cmklr1		 MGI:109603  MP:0008245 abnormal alveolar macrophage morphology PMID: 19841182 
Cmklr1tm1Dgen Cmklr1tm1Dgen/Cmklr1tm1Dgen
B6.Cg-Cmklr1		 MGI:109603  MP:0002452 abnormal antigen presenting cell physiology PMID: 19841182 
Cmklr1tm1Dgen Cmklr1tm1Dgen/Cmklr1tm1Dgen
B6.Cg-Cmklr1		 MGI:109603  MP:0002376 abnormal dendritic cell physiology PMID: 19841182 
Cmklr1tm1Dgen Cmklr1tm1Dgen/Cmklr1tm1Dgen
B6.Cg-Cmklr1		 MGI:109603  MP:0002123 abnormal hematopoiesis PMID: 19841182 
Cmklr1tm1Dgen Cmklr1tm1Dgen/Cmklr1tm1Dgen
B6.Cg-Cmklr1		 MGI:109603  MP:0000685 abnormal immune system morphology PMID: 19841182 
Cmklr1tm1Dgen Cmklr1tm1Dgen/Cmklr1tm1Dgen
B6.Cg-Cmklr1		 MGI:109603  MP:0005495 abnormal macrophage recruitment PMID: 19841182 
Cmklr1tm1Drg Cmklr1tm1Drg/Cmklr1tm1Drg
Not Specified		 MGI:109603  MP:0003799 impaired macrophage migration PMID: 18391062 
Cmklr1tm1Drg Cmklr1tm1Drg/Cmklr1tm1Drg
Not Specified		 MGI:109603  MP:0005496 impaired macrophage recruitment PMID: 18391062 
Cmklr1tm1Drg Cmklr1tm1Drg/Cmklr1tm1Drg
Not Specified		 MGI:109603  MP:0008719 impaired neutrophil recruitment PMID: 18391062 
Cmklr1tm1Dgen Cmklr1tm1Dgen/Cmklr1tm1Dgen
B6.Cg-Cmklr1		 MGI:109603  MP:0000219 increased neutrophil cell number PMID: 19841182 
Cmklr1tm1Dgen Cmklr1tm1Dgen/Cmklr1tm1Dgen
B6.Cg-Cmklr1		 MGI:109603  MP:0008735 increased susceptibility to endotoxin shock PMID: 19841182 
Cmklr1tm1Dgen Cmklr1tm1Dgen/Cmklr1tm1Dgen
B6.Cg-Cmklr1		 MGI:109603  MP:0001861 lung inflammation PMID: 19841182 
Clinically-Relevant Mutations and Pathophysiology Click here for help
Disease:  Diabetes mellitus, noninsulin-dependent; NIDDM
Synonyms: Diabetes mellitus, Type II; T2D [OMIM: 125853]
Maturity onset diabetes
Type 2 diabetes mellitus [Disease Ontology: DOID:9352]
Disease Ontology: DOID:9352
OMIM: 125853
References:  8,15
Disease:  Human immunodeficiency virus type 1, susceptibility to
Synonyms: Human immunodeficiency virus infectious disease [Disease Ontology: DOID:526]
Disease Ontology: DOID:526
OMIM: 609423
Orphanet: ORPHA319269
References:  41
Disease:  Lupus erythematosus
Disease Ontology: DOID:8857
References:  12
Disease:  Osteoarthritis
Disease Ontology: DOID:8398
References:  16
Disease:  Rheumatoid arthritis
Disease Ontology: DOID:7148
OMIM: 180300
References:  16
Clinically-Relevant Mutations and Pathophysiology Comments
SNP rs1878022 is an intronic variant located within CMKLR1 on human chromosome 12, and was found to be higher in normal mucosa of patients with esophageal squamous dysplasia patients whose disease had progressed, although no link has been found between either the CMKLR1 gene, or its protein, and non-small cell lung cancer [63].
Gene Expression and Pathophysiology Click here for help
Chemerin receptor knockout mice display higher morbidity and mortality from viral pneumonia than wildtype mice.
Tissue or cell type:  Lung
Pathophysiology:  Viral pneumonia
Species:  Mouse
Technique:  Gene knockout
References:  7
CMKLR1 knockout mice developed less severe experimental autoimmune encephalomyelitis than their wildtype counterparts while wildtype mice with induced experimental autoimmune encephalomyelitis showed increased expression of CMKLR1 and natural ligand chemerin in the CNS
Tissue or cell type:  CNS
Pathophysiology:  Experimental autoimmune encephalomyelitis
Species:  Mouse
Technique:  Knockout mice
References:  23
Gene Expression and Pathophysiology Comments
CMKLR1 expression was determined on peritoneal and tumor-infiltrating macrophages, suggesting a role for the receptor in mediating inflammatory responses in the tumour microenvironment [47].

CMKLR1 expression has been shown to be increased in inflammatory pain by RT-PCR [49]. HIV isolates are able to activate the chemerin receptor, and in the presence of CD4, this receptor functions as a "minor co-receptor" promoting infection by these classes of viruses [49]. Lesions which progress in mild to moderate squamous dysplasia have higher expression of inflammatory genes such as CMKLR1 [29]. Chemerin-derived peptides may represent a novel therapeutic strategy for the treatment of inflammatory diseases through the chemerin receptor [10]. The receptor is transiently upregulated in Peg-interferon alfa-2b plus ribavirin in peripheral blood monocytes (PBMC) of hepatitis C patients during the first 10 weeks of treatment [58].

Prepsoriatic skin adjacent to active lesions and early lesions were characterized by a strong expression of chemerin in the dermis and by the presence of CD15(+) neutrophils and CD123(+)/BDCA-2(+)/ChemR23(+) pDC, supporting a role for the chemerin/chemerin receptor axis in the early phases of psoriasis development [1]. Lesional skin from psoriasis patients contains the active form of the chemerin receptor ligand chemerin [54].

Coronary and aortic atherosclerosis have been correlated with increased chemerin concentration, though it is not indicated whether any effects are mediated by the chemerin receptor [56].

CMKLR1+ cells in kidney from SLE patients with nephritis, mostly localized at tubulointerstitial level.
General Comments
It is believed that another orphan receptor, CCLR2, may concentrate bioactive chemerin for presentation to the chemerin receptor [64-65].

The mouse and the two human splicing variants are 70% identical, the human splicing variants a and b showing 99% amino acid sequence identity. The mouse and the rat orthologues (the latter located to chromosome 12, region 12q16) display 91% identity [42]. The promoter does not seem to be tissue specific but other elements or enhancers may be missing, and sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions [42,57]. The murine receptor utilizes alternative promoters for transcription and is regulated by all-trans retinoic acid [40].

The chemerin receptor is a cell surface receptor that can be used to target recombinant adenovirus vectors to dendritic cells for vaccination development [35]. HIV-1 subtype C lineages also had diverse alternative coreceptor patterns including the ability to use the chemerin receptor [11].

Chemerin and resolvin mediated divergent results suggesting the chemerin receptor is multifunctional [64].

References

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1. Albanesi C, Scarponi C, Pallotta S, Daniele R, Bosisio D, Madonna S, Fortugno P, Gonzalvo-Feo S, Franssen JD, Parmentier M et al.. (2009) Chemerin expression marks early psoriatic skin lesions and correlates with plasmacytoid dendritic cell recruitment. J Exp Med, 206 (1): 249-58. [PMID:19114666]

2. Arita M, Bianchini F, Aliberti J, Sher A, Chiang N, Hong S, Yang R, Petasis NA, Serhan CN. (2005) Stereochemical assignment, antiinflammatory properties, and receptor for the omega-3 lipid mediator resolvin E1. J Exp Med, 201 (5): 713-22. [PMID:15753205]

3. Arita M, Ohira T, Sun YP, Elangovan S, Chiang N, Serhan CN. (2007) Resolvin E1 selectively interacts with leukotriene B4 receptor BLT1 and ChemR23 to regulate inflammation. J Immunol, 178 (6): 3912-7. [PMID:17339491]

4. Barnea G, Strapps W, Herrada G, Berman Y, Ong J, Kloss B, Axel R, Lee KJ. (2008) The genetic design of signaling cascades to record receptor activation. Proc Natl Acad Sci USA, 105 (1): 64-9. [PMID:18165312]

5. Bauer S, Wanninger J, Schmidhofer S, Weigert J, Neumeier M, Dorn C, Hellerbrand C, Zimara N, Schäffler A, Aslanidis C et al.. (2011) Sterol regulatory element-binding protein 2 (SREBP2) activation after excess triglyceride storage induces chemerin in hypertrophic adipocytes. Endocrinology, 152 (1): 26-35. [PMID:21084441]

6. Berg V, Sveinbjörnsson B, Bendiksen S, Brox J, Meknas K, Figenschau Y. (2010) Human articular chondrocytes express ChemR23 and chemerin; ChemR23 promotes inflammatory signalling upon binding the ligand chemerin(21-157). Arthritis Res Ther, 12 (6): R228. [PMID:21192818]

7. Bondue B, Vosters O, de Nadai P, Glineur S, De Henau O, Luangsay S, Van Gool F, Communi D, De Vuyst P, Desmecht D et al.. (2011) ChemR23 dampens lung inflammation and enhances anti-viral immunity in a mouse model of acute viral pneumonia. PLoS Pathog, 7 (11): e1002358. [PMID:22072972]

8. Bozaoglu K, Bolton K, McMillan J, Zimmet P, Jowett J, Collier G, Walder K, Segal D. (2007) Chemerin is a novel adipokine associated with obesity and metabolic syndrome. Endocrinology, 148 (10): 4687-94. [PMID:17640997]

9. Cash JL, Christian AR, Greaves DR. (2010) Chemerin peptides promote phagocytosis in a ChemR23- and Syk-dependent manner. J Immunol, 184 (9): 5315-24. [PMID:20363975]

10. Cash JL, Hart R, Russ A, Dixon JP, Colledge WH, Doran J, Hendrick AG, Carlton MB, Greaves DR. (2008) Synthetic chemerin-derived peptides suppress inflammation through ChemR23. J Exp Med, 205 (4): 767-75. [PMID:18391062]

11. Coetzer M, Nedellec R, Cilliers T, Meyers T, Morris L, Mosier DE. (2011) Extreme genetic divergence is required for coreceptor switching in HIV-1 subtype C. J Acquir Immune Defic Syndr, 56 (1): 9-15. [PMID:20921899]

12. De Palma G, Castellano G, Del Prete A, Sozzani S, Fiore N, Loverre A, Parmentier M, Gesualdo L, Grandaliano G, Schena FP. (2011) The possible role of ChemR23/Chemerin axis in the recruitment of dendritic cells in lupus nephritis. Kidney Int, 79 (11): 1228-35. [PMID:21346723]

13. Demoor T, Bracke KR, Dupont LL, Plantinga M, Bondue B, Roy MO, Lannoy V, Lambrecht BN, Brusselle GG, Joos GF. (2011) The role of ChemR23 in the induction and resolution of cigarette smoke-induced inflammation. J Immunol, 186 (9): 5457-67. [PMID:21430224]

14. Doyle JR, Krishnaji ST, Zhu G, Xu ZZ, Heller D, Ji RR, Levy BD, Kumar K, Kopin AS. (2014) Development of a membrane-anchored chemerin receptor agonist as a novel modulator of allergic airway inflammation and neuropathic pain. J Biol Chem, 289 (19): 13385-96. [PMID:24659779]

15. Du XY, Leung LL. (2009) Proteolytic regulatory mechanism of chemerin bioactivity. Acta Biochim Biophys Sin (Shanghai), 41 (12): 973-9. [PMID:20011981]

16. Eisinger K, Bauer S, Schäffler A, Walter R, Neumann E, Buechler C, Müller-Ladner U, Frommer KW. (2012) Chemerin induces CCL2 and TLR4 in synovial fibroblasts of patients with rheumatoid arthritis and osteoarthritis. Exp Mol Pathol, 92 (1): 90-6. [PMID:22037282]

17. Ernst MC, Haidl ID, Zúñiga LA, Dranse HJ, Rourke JL, Zabel BA, Butcher EC, Sinal CJ. (2012) Disruption of the chemokine-like receptor-1 (CMKLR1) gene is associated with reduced adiposity and glucose intolerance. Endocrinology, 153 (2): 672-82. [PMID:22186410]

18. Ernst MC, Issa M, Goralski KB, Sinal CJ. (2010) Chemerin exacerbates glucose intolerance in mouse models of obesity and diabetes. Endocrinology, 151 (5): 1998-2007. [PMID:20228173]

19. Fredman G, Van Dyke TE, Serhan CN. (2010) Resolvin E1 regulates adenosine diphosphate activation of human platelets. Arterioscler Thromb Vasc Biol, 30 (10): 2005-13. [PMID:20702811]

20. Gantz I, Konda Y, Yang YK, Miller DE, Dierick HA, Yamada T. (1996) Molecular cloning of a novel receptor (CMKLR1) with homology to the chemotactic factor receptors. Cytogenet Cell Genet, 74 (4): 286-90. [PMID:8976386]

21. Goralski KB, McCarthy TC, Hanniman EA, Zabel BA, Butcher EC, Parlee SD, Muruganandan S, Sinal CJ. (2007) Chemerin, a novel adipokine that regulates adipogenesis and adipocyte metabolism. J Biol Chem, 282 (38): 28175-88. [PMID:17635925]

22. Goralski KB, Sinal CJ. (2009) Elucidation of chemerin and chemokine-like receptor-1 function in adipocytes by adenoviral-mediated shRNA knockdown of gene expression. Meth Enzymol, 460: 289-312. [PMID:19446731]

23. Graham KL, Zabel BA, Loghavi S, Zuniga LA, Ho PP, Sobel RA, Butcher EC. (2009) Chemokine-like receptor-1 expression by central nervous system-infiltrating leukocytes and involvement in a model of autoimmune demyelinating disease. J Immunol, 183 (10): 6717-23. [PMID:19864606]

24. Graham KL, Zhang JV, Lewén S, Burke TM, Dang T, Zoudilova M, Sobel RA, Butcher EC, Zabel BA. (2014) A novel CMKLR1 small molecule antagonist suppresses CNS autoimmune inflammatory disease. PLoS ONE, 9 (12): e112925. [PMID:25437209]

25. Hart R, Greaves DR. (2010) Chemerin contributes to inflammation by promoting macrophage adhesion to VCAM-1 and fibronectin through clustering of VLA-4 and VLA-5. J Immunol, 185 (6): 3728-39. [PMID:20720202]

26. Haworth O, Cernadas M, Levy BD. (2011) NK cells are effectors for resolvin E1 in the timely resolution of allergic airway inflammation. J Immunol, 186 (11): 6129-35. [PMID:21515793]

27. Imaizumi T, Otsubo S, Maemoto M, Kobayashi A, Komai M, Takada H, Sakaida Y, Otsubo N. (2022) Discovery and mechanistic study of thiazole-4-acylsulfonamide derivatives as potent and orally active ChemR23 inhibitors with a long-acting effect in cynomolgus monkeys. Bioorg Med Chem, 56: 116587. [PMID:35063894]

28. Issa ME, Muruganandan S, Ernst MC, Parlee SD, Zabel BA, Butcher EC, Sinal CJ, Goralski KB. (2012) Chemokine-like receptor 1 regulates skeletal muscle cell myogenesis. Am J Physiol, Cell Physiol, 302 (11): C1621-31. [PMID:22460713]

29. Joshi N, Johnson LL, Wei WQ, Abnet CC, Dong ZW, Taylor PR, Limburg PJ, Dawsey SM, Hawk ET, Qiao YL et al.. (2006) Gene expression differences in normal esophageal mucosa associated with regression and progression of mild and moderate squamous dysplasia in a high-risk Chinese population. Cancer Res, 66 (13): 6851-60. [PMID:16818663]

30. Kaur J, Adya R, Tan BK, Chen J, Randeva HS. (2010) Identification of chemerin receptor (ChemR23) in human endothelial cells: chemerin-induced endothelial angiogenesis. Biochem Biophys Res Commun, 391 (4): 1762-8. [PMID:20044979]

31. Kennedy AJ, Davenport AP. (2018) International Union of Basic and Clinical Pharmacology CIII: Chemerin Receptors CMKLR1 (Chemerin1) and GPR1 (Chemerin2) Nomenclature, Pharmacology, and Function. Pharmacol Rev, 70 (1): 174-196. [PMID:29279348]

32. Kennedy AJ, Yang P, Read C, Kuc RE, Yang L, Taylor EJ, Taylor CW, Maguire JJ, Davenport AP. (2016) Chemerin Elicits Potent Constrictor Actions via Chemokine-Like Receptor 1 (CMKLR1), not G-Protein-Coupled Receptor 1 (GPR1), in Human and Rat Vasculature. J Am Heart Assoc, 5 (10). [PMID:27742615]

33. Ko B, Jang Y, Kwak SH, You H, Kim JH, Lee JE, Park HD, Kim SK, Goddard 3rd WA, Han JH et al.. (2023) Discovery of 3-Phenyl Indazole-Based Novel Chemokine-like Receptor 1 Antagonists for the Treatment of Psoriasis. J Med Chem, 66 (21): 14564-14582. [PMID:37883692]

34. Luangsay S, Wittamer V, Bondue B, De Henau O, Rouger L, Brait M, Franssen JD, de Nadai P, Huaux F, Parmentier M. (2009) Mouse ChemR23 is expressed in dendritic cell subsets and macrophages, and mediates an anti-inflammatory activity of chemerin in a lung disease model. J Immunol, 183 (10): 6489-99. [PMID:19841182]

35. Maguire CA, Sapinoro R, Girgis N, Rodriguez-Colon SM, Ramirez SH, Williams J, Dewhurst S. (2006) Recombinant adenovirus type 5 vectors that target DC-SIGN, ChemR23 and alpha(v)beta3 integrin efficiently transduce human dendritic cells and enhance presentation of vectored antigens. Vaccine, 24 (5): 671-82. [PMID:16154247]

36. Methner A, Hermey G, Schinke B, Hermans-Borgmeyer I. (1997) A novel G protein-coupled receptor with homology to neuropeptide and chemoattractant receptors expressed during bone development. Biochem Biophys Res Commun, 233 (2): 336-42. [PMID:9144535]

37. Morehouse MG, Scheer BT, Deuel HJ. (1947) The effect of dietary fat level on the physical capacity of rats during undernutrition. Fed Proc, 6 (1): 415. [PMID:20343880]

38. Muruganandan S, Parlee SD, Rourke JL, Ernst MC, Goralski KB, Sinal CJ. (2011) Chemerin, a novel peroxisome proliferator-activated receptor gamma (PPARgamma) target gene that promotes mesenchymal stem cell adipogenesis. J Biol Chem, 286 (27): 23982-95. [PMID:21572083]

39. Muruganandan S, Roman AA, Sinal CJ. (2010) Role of chemerin/CMKLR1 signaling in adipogenesis and osteoblastogenesis of bone marrow stem cells. J Bone Miner Res, 25 (2): 222-34. [PMID:19929432]

40. Mårtensson UE, Bristulf J, Owman C, Olde B. (2005) The mouse chemerin receptor gene, mcmklr1, utilizes alternative promoters for transcription and is regulated by all-trans retinoic acid. Gene, 350 (1): 65-77. [PMID:15792532]

41. Mårtensson UE, Fenyö EM, Olde B, Owman C. (2006) Characterization of the human chemerin receptor--ChemR23/CMKLR1--as co-receptor for human and simian immunodeficiency virus infection, and identification of virus-binding receptor domains. Virology, 355 (1): 6-17. [PMID:16904155]

42. Mårtensson UE, Owman C, Olde B. (2004) Genomic organization and promoter analysis of the gene encoding the mouse chemoattractant-like receptor, CMKLR1. Gene, 328: 167-76. [PMID:15019996]

43. Ohira T, Arita M, Omori K, Recchiuti A, Van Dyke TE, Serhan CN. (2010) Resolvin E1 receptor activation signals phosphorylation and phagocytosis. J Biol Chem, 285 (5): 3451-61. [PMID:19906641]

44. Owman C, Lolait SJ, Santén S, Olde B. (1997) Molecular cloning and tissue distribution of cDNA encoding a novel chemoattractant-like receptor. Biochem Biophys Res Commun, 241 (2): 390-4. [PMID:9425281]

45. Parlee SD, Ernst MC, Muruganandan S, Sinal CJ, Goralski KB. (2010) Serum chemerin levels vary with time of day and are modified by obesity and tumor necrosis factor-{alpha}. Endocrinology, 151 (6): 2590-602. [PMID:20363880]

46. Parolini S, Santoro A, Marcenaro E, Luini W, Massardi L, Facchetti F, Communi D, Parmentier M, Majorana A, Sironi M, Tabellini G, Moretta A, Sozzani S. (2007) The role of chemerin in the colocalization of NK and dendritic cell subsets into inflamed tissues. Blood, 109 (9): 3625-32. [PMID:17202316]

47. Rama D, Esendagli G, Guc D. (2011) Expression of chemokine-like receptor 1 (CMKLR1) on J744A.1 macrophages co-cultured with fibroblast and/or tumor cells: modeling the influence of microenvironment. Cell Immunol, 271 (1): 134-40. [PMID:21752353]

48. Reverchon M, Cornuau M, Ramé C, Guerif F, Royère D, Dupont J. (2012) Chemerin inhibits IGF-1-induced progesterone and estradiol secretion in human granulosa cells. Hum Reprod, 27 (6): 1790-800. [PMID:22447628]

49. Rodriguez Parkitna J, Korostynski M, Kaminska-Chowaniec D, Obara I, Mika J, Przewlocka B, Przewlocki R. (2006) Comparison of gene expression profiles in neuropathic and inflammatory pain. J Physiol Pharmacol, 57 (3): 401-14. [PMID:17033093]

50. Roh SG, Song SH, Choi KC, Katoh K, Wittamer V, Parmentier M, Sasaki S. (2007) Chemerin--a new adipokine that modulates adipogenesis via its own receptor. Biochem Biophys Res Commun, 362 (4): 1013-8. [PMID:17767914]

51. Samson M, Edinger AL, Stordeur P, Rucker J, Verhasselt V, Sharron M, Govaerts C, Mollereau C, Vassart G, Doms RW, Parmentier M. (1998) ChemR23, a putative chemoattractant receptor, is expressed in monocyte-derived dendritic cells and macrophages and is a coreceptor for SIV and some primary HIV-1 strains. Eur J Immunol, 28 (5): 1689-700. [PMID:9603476]

52. Sell H, Laurencikiene J, Taube A, Eckardt K, Cramer A, Horrighs A, Arner P, Eckel J. (2009) Chemerin is a novel adipocyte-derived factor inducing insulin resistance in primary human skeletal muscle cells. Diabetes, 58 (12): 2731-40. [PMID:19720798]

53. Skrzeczyńska-Moncznik J, Stefańska A, Zabel BA, Kapińska-Mrowiecka M, Butcher EC, Cichy J. (2009) Chemerin and the recruitment of NK cells to diseased skin. Acta Biochim Pol, 56 (2): 355-60. [PMID:19543554]

54. Skrzeczyńska-Moncznik J, Wawro K, Stefańska A, Oleszycka E, Kulig P, Zabel BA, Sułkowski M, Kapińska-Mrowiecka M, Czubak-Macugowska M, Butcher EC, Cichy J. (2009) Potential role of chemerin in recruitment of plasmacytoid dendritic cells to diseased skin. Biochem Biophys Res Commun, 380 (2): 323-7. [PMID:19168032]

55. Southern C, Cook JM, Neetoo-Isseljee Z, Taylor DL, Kettleborough CA, Merritt A, Bassoni DL, Raab WJ, Quinn E, Wehrman TS et al.. (2013) Screening β-Arrestin Recruitment for the Identification of Natural Ligands for Orphan G-Protein-Coupled Receptors. J Biomol Screen, 18 (5): 599-609. [PMID:23396314]

56. Spiroglou SG, Kostopoulos CG, Varakis JN, Papadaki HH. (2010) Adipokines in periaortic and epicardial adipose tissue: differential expression and relation to atherosclerosis. J Atheroscler Thromb, 17 (2): 115-30. [PMID:20145358]

57. Suzuki Y, Yamashita R, Shirota M, Sakakibara Y, Chiba J, Mizushima-Sugano J, Nakai K, Sugano S. (2004) Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions. Genome Res, 14 (9): 1711-8. [PMID:15342556]

58. Taylor MW, Tsukahara T, McClintick JN, Edenberg HJ, Kwo P. (2008) Cyclic changes in gene expression induced by Peg-interferon alfa-2b plus ribavirin in peripheral blood monocytes (PBMC) of hepatitis C patients during the first 10 weeks of treatment. J Transl Med, 6: 66. [PMID:18986530]

59. Uddin M, Levy BD. (2011) Resolvins: natural agonists for resolution of pulmonary inflammation. Prog Lipid Res, 50 (1): 75-88. [PMID:20887750]

60. Vermi W, Riboldi E, Wittamer V, Gentili F, Luini W, Marrelli S, Vecchi A, Franssen JD, Communi D, Massardi L, Sironi M, Mantovani A, Parmentier M, Facchetti F, Sozzani S. (2005) Role of ChemR23 in directing the migration of myeloid and plasmacytoid dendritic cells to lymphoid organs and inflamed skin. J Exp Med, 201 (4): 509-15. [PMID:15728234]

61. Wittamer V, Franssen JD, Vulcano M, Mirjolet JF, Le Poul E, Migeotte I, Brézillon S, Tyldesley R, Blanpain C, Detheux M, Mantovani A, Sozzani S, Vassart G, Parmentier M, Communi D. (2003) Specific recruitment of antigen-presenting cells by chemerin, a novel processed ligand from human inflammatory fluids. J Exp Med, 198 (7): 977-85. [PMID:14530373]

62. Wittamer V, Grégoire F, Robberecht P, Vassart G, Communi D, Parmentier M. (2004) The C-terminal nonapeptide of mature chemerin activates the chemerin receptor with low nanomolar potency. J Biol Chem, 279 (11): 9956-62. [PMID:14701797]

63. Wu X, Ye Y, Rosell R, Amos CI, Stewart DJ, Hildebrandt MA, Roth JA, Minna JD, Gu J, Lin J et al.. (2011) Genome-wide association study of survival in non-small cell lung cancer patients receiving platinum-based chemotherapy. J Natl Cancer Inst, 103 (10): 817-25. [PMID:21483023]

64. Yoshimura T, Oppenheim JJ. (2008) Chemerin reveals its chimeric nature. J Exp Med, 205 (10): 2187-90. [PMID:18809717]

65. Zabel BA, Nakae S, Zúñiga L, Kim JY, Ohyama T, Alt C, Pan J, Suto H, Soler D, Allen SJ, Handel TM, Song CH, Galli SJ, Butcher EC. (2008) Mast cell-expressed orphan receptor CCRL2 binds chemerin and is required for optimal induction of IgE-mediated passive cutaneous anaphylaxis. J Exp Med, 205 (10): 2207-20. [PMID:18794339]

66. Zabel BA, Ohyama T, Zuniga L, Kim JY, Johnston B, Allen SJ, Guido DG, Handel TM, Butcher EC. (2006) Chemokine-like receptor 1 expression by macrophages in vivo: regulation by TGF-beta and TLR ligands. Exp Hematol, 34 (8): 1106-14. [PMID:16863918]

67. Zabel BA, Silverio AM, Butcher EC. (2005) Chemokine-like receptor 1 expression and chemerin-directed chemotaxis distinguish plasmacytoid from myeloid dendritic cells in human blood. J Immunol, 174 (1): 244-51. [PMID:15611246]

68. Zhao RJ, Wang H. (2011) Chemerin/ChemR23 signaling axis is involved in the endothelial protection by K(ATP) channel opener iptakalim. Acta Pharmacol Sin, 32 (5): 573-80. [PMID:21516134]

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