Genomic organization and promoter analysis of the gene encoding the mouse chemoattractant-like receptor, CMKLR1

Mårtensson, Ulrika; Owman, Christer; Olde, Björn

doi:10.1016/j.gene.2003.12.004

Cited by 14 publications

(18 citation statements)

References 17 publications

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“…Similarly, two distinct start sites and several differentially spliced isoforms were reported for the mouse homolog of ChemR23 (DEZ) in mouse neuroblastoma and microglia cells (31,46). Such usage of alternative promoters has been previously described to enable differential transcriptional regulation in different cell types, developmental stages, or upon stimulation (47).…”

Section: Discussionmentioning

confidence: 61%

ChemR23, the Receptor for Chemerin and Resolvin E1, Is Expressed and Functional on M1 but Not on M2 Macrophages

Herová

Schmid

Gemperle

et al. 2015

The Journal of Immunology

141

100

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ChemR23 is a G protein–coupled receptor that is triggered by two ligands, the peptide chemerin and the eicosapentaenoic acid–derived lipid mediator resolvin E1 (RvE1). Chemerin acts as a chemoattractant for monocytes and macrophages, whereas RvE1 promotes resolution of inflammation-inducing macrophage phagocytosis of apoptotic neutrophils. Although ChemR23-mediated signaling plays a role in mononuclear cell migration to inflamed tissue, as well as in the resolution of inflammation, its regulation in different polarization states of macrophages is largely unknown. We analyzed the expression and function of ChemR23 in monocytes and differently activated human primary macrophages. Using 5′ RACE, we identified three transcription start sites and several splice variants of ChemR23 in both monocytes and macrophages. Although the promoters P1 and P3 are used equally in unpolarized macrophages, stimulation with LPS or IFN-γ leads to increased transcription from P3 in inflammatory M1 macrophages. Such ChemR23-expressing M1 macrophages are chemotactic to chemerin, whereas M2 macrophages not expressing ChemR23 surface receptor are not. Repolarization of ChemR23-expressing M1 macrophages with 10 nM RvE1 increases IL-10 transcription and phagocytosis of microbial particles, leading to a resolution-type macrophage distinct from the M2 phenotype. These results show that ChemR23 is tightly regulated in response to inflammatory and anti-inflammatory stimuli. The restricted expression of ChemR23 in naive and M1 macrophages supports the role of ChemR23 in the attraction of macrophages to inflamed tissue by chemerin and in the initiation of resolution of inflammation through RvE1-mediated repolarization of human M1 macrophages toward resolution-type macrophages.

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Section: Discussionmentioning

confidence: 61%

ChemR23, the Receptor for Chemerin and Resolvin E1, Is Expressed and Functional on M1 but Not on M2 Macrophages

Herová

Schmid

Gemperle

et al. 2015

The Journal of Immunology

141

100

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“…Transcription start site (TSS) was identified 254 bp upstream from intron1. The region from -1,269 to +54 (relative to TSS), which was similar to the human/mouse homologs without canonical TATA box or CAAT sequence (21), was found to contain two putative PPAR binding motifs and three KLF15 consensus binding motifs (CG/TCCCC) (22) (Fig. 4D).…”

Section: Tissue Distribution Of Chemerin Chemr23 and Gpr1 In Pigsmentioning

confidence: 90%

Cloning of porcine chemerin, ChemR23 and GPR1 and their involvement in regulation of lipogenesis

Huang¹,

Zhang²,

Lei³

et al. 2010

BMB Reports

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Chemerin is a novel adipokine which is abundant in adipose tissue to promote adipocyte differentiation and with significant relativity to BMI and insulin sensitivity. We report here the molecular characterization of porcine chemerin and its receptors ChemR23 and GPR1, as well as their transcriptional regulation during lipogenesis. Chemerin was mainly expressed in liver, intestine, kidney and adipose tissue, consistent with the expression pattern of GPR1, but not ChemR23, which was predominantly present in spleen and temperately in adipose tissue. We further investigated the lipogenesis-related transcriptional activation of PPARγ and KLF15 on chemerin and its receptors. The data showed that KLF15, but not PPARγ, can up-regulate the mRNA level of chemerin, ChemR23 and GPR1, which was consistent with the results of luciferase assay that confirmed the effect of KLF15 on ChemR23 promoter. Taken together, our data provide basic molecular information for the further investigation on the function of chemerin in lipogenesis. [BMB reports 2010; 43(7): 491-498]

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“…The mouse ChemR23 gene, also called mcmklr1 or Dez, is localized on chromosome 5. The cDNA was originally cloned from a brain library (32), and the genomic organization of the gene was previously reported (33,34). Prochemerin (Ensembl ID ENS-MUSG00000009281) and ChemR23 (Ensembl ID ENS-MUSG00000042190) amino acid sequences from vertebrate species were aligned with ClustalW and a dendrogram was constructed ( Fig.…”

Section: The Chemerin/chemr23 System Is Well Conserved In Vertebrate mentioning

confidence: 99%

Mouse ChemR23 Is Expressed in Dendritic Cell Subsets and Macrophages, and Mediates an Anti-Inflammatory Activity of Chemerin in a Lung Disease Model

Luangsay

Wittamer

Bondue

et al. 2009

The Journal of Immunology

223

241

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Chemerin is the ligand of the ChemR23 receptor and a chemoattractant factor for human immature dendritic cells (DCs), macrophages, and NK cells. In this study, we characterized the mouse chemerin/ChemR23 system in terms of pharmacology, structure-function, distribution, and in vivo biological properties. Mouse chemerin is synthesized as an inactive precursor (prochemerin) requiring, as in human, the precise processing of its C terminus for generating an agonist of ChemR23. Mouse ChemR23 is highly expressed in immature plasmacytoid DCs and at lower levels in myeloid DCs, macrophages, and NK cells. Mouse prochemerin is expressed in most epithelial cells acting as barriers for pathogens but not in leukocytes. Chemerin promotes calcium mobilization and chemotaxis on DCs and macrophages and these functional responses were abrogated in ChemR23 knockout mice. In a mouse model of acute lung inflammation induced by LPS, chemerin displayed potent anti-inflammatory properties, reducing neutrophil infiltration and inflammatory cytokine release in a ChemR23-dependent manner. ChemR23 knockout mice were unresponsive to chemerin and displayed an increased neutrophil infiltrate following LPS challenge. Altogether, the mouse chemerin/ChemR23 system is structurally and functionally conserved between human and mouse, and mouse can therefore be considered as a good model for studying the anti-inflammatory role of this system in the regulation of immune responses and inflammatory diseases.

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Genomic organization and promoter analysis of the gene encoding the mouse chemoattractant-like receptor, CMKLR1

Cited by 14 publications

References 17 publications

ChemR23, the Receptor for Chemerin and Resolvin E1, Is Expressed and Functional on M1 but Not on M2 Macrophages

ChemR23, the Receptor for Chemerin and Resolvin E1, Is Expressed and Functional on M1 but Not on M2 Macrophages

Cloning of porcine chemerin, ChemR23 and GPR1 and their involvement in regulation of lipogenesis

Mouse ChemR23 Is Expressed in Dendritic Cell Subsets and Macrophages, and Mediates an Anti-Inflammatory Activity of Chemerin in a Lung Disease Model

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