• Title, Summary, Keyword: Chemerin

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Serum Chemerin Levels are Associated with Visceral Adiposity, Independent of Waist Circumference, in Newly Diagnosed Type 2 Diabetic Subjects

  • Cheon, Dae Young;Kang, Jun Goo;Lee, Seong Jin;Ihm, Sung Hee;Lee, Eun Jig;Choi, Moon Gi;Yoo, Hyung Joon;Kim, Chul Sik
    • Yonsei Medical Journal
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    • v.58 no.2
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    • pp.319-325
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    • 2017
  • Purpose: Chemerin has been suggested to be linked to insulin resistance and type 2 diabetes mellitus (T2DM). However, the relationship between visceral adiposity and chemerin levels remains unclear in subjects with T2DM. In this study, we investigated the relationship between serum chemerin levels and visceral adiposity. Materials and Methods: This study included 102 subjects newly diagnosed with T2DM. The relationships between serum chemerin levels and clinical and biochemical parameters were examined. Multiple linear regression analysis was performed to determine the predictable factors of serum chemerin levels. Results: Serum chemerin levels showed significant positive correlations with body mass index (BMI), waist circumference (WC), visceral fat thickness (VFT), insulin levels, the homeostasis model assessment of insulin resistance, and levels of triglycerides (log-transformed) and high-sensitivity C-reactive protein, while showing significant negative correlations with high-density lipoprotein cholesterol. After adjusting for BMI and WC, VFT showed a significant relationship with serum chemerin levels (r=0.222, p=0.027). Moreover, VFT was an independent predictive factor of serum chemerin levels (${\beta}=0.242$, p=0.041). Conclusion: We demonstrated that chemerin is linked to metabolic syndrome components. Moreover, serum chemerin levels were associated significantly with obesity, especially visceral adipose tissue, in subjects with T2DM.

The Regulation of Chemerin and CMKLR1 Genes Expression by TNF-α, Adiponectin, and Chemerin Analog in Bovine Differentiated Adipocytes

  • Suzuki, Y.;Hong, Y.H.;Song, S.H.;Ardiyanti, A.;Kato, D.;So, K.H.;Katoh, K.;Roh, Sang-Gun
    • Asian-Australasian Journal of Animal Sciences
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    • v.25 no.9
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    • pp.1316-1321
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    • 2012
  • Adipokines, adipocyte-derived protein, have important roles in various kinds of physiology including energy homeostasis. Chemerin, one of adipocyte-derived adipokines, is highly expressed in differentiated adipocytes and is known to induce macrophage chemotaxis and glucose intolerance. The objective of the present study was to investigate the changes of chemerin and the chemokine-like-receptor 1 (CMKLR1) gene expression levels during differentiation of the bovine adipocyte and in differentiated adipocytes treated with tumor necrosis factor-${\alpha}$ (TNF-${\alpha}$), adiponectin, leptin, and chemerin (peptide analog). The expression levels of the chemerin gene increased at d 6 and 12 of the differentiation period accompanied by increased cytoplasm lipid droplets. From d 6 onward, peroxisome proliferator-activated receptor-${\gamma}2$ (PPAR-${\gamma}2$) gene expression levels were significantly higher than that of d 0 and 3. In contrast, CMKLR1 expression levels decreased at the end of the differentiation period. In fully differentiated adipocytes (i.e. at d 12), the treatment of TNF-${\alpha}$ and adiponectin upregulated both chemerin and CMKLR1 gene expression levels, although leptin did not show such effects. Moreover, chemerin analog treatment was shown to upregulate chemerin gene expression levels regardless of doses. These results suggest that the expression of chemerin in bovine adipocyte might be regulated by chemerin itself and other adipokines, which indicates its possible role in modulating the adipokine secretions in adipose tissues.

Homology Modelling of Chemerin like Receptor-1 (CMKLR1): Potential Target for Treating Type II Diabetes

  • B, Sathya.
    • Journal of the Chosun Natural Science
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    • v.10 no.1
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    • pp.20-26
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    • 2017
  • Chemerin receptor, which predominantly expressed in immune cells as well as adipose tissue, was found to stimulate chemotaxis of dendritic cells and macrophages to the site of inflammation. Chemerin is a widely distributed multifunctional secreted protein implicated in immune cell migration, adipogenesis, osteoblastogenesis, angiogenesis, myogenesis, and glucose homeostasis. Recent studies suggest chemerin may play an important role in the pathogenesis of obesity and insulin resistance and it becomes a potential therapeutic target for treating type II diabetes. The crystal structure of chemerin receptor has not yet been resolved. Therefore, in the present study, homology modelling of CMKLR1 was done utilizing the crystal structure of human angiotension receptor in complex with inverse agonist olmesartan as the template. Since the template has low sequence identity, we have incorporated both threading and comparative modelling approach to generate the three dimensional structure. 3D models were generated and validated. The reported models can be used to characterize the critical amino acid residues in the binding site of CMKLR1.

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

  • Huang, Jianfeng;Zhang, Jian;Lei, Ting;Chen, Xiaodong;Zhang, Yan;Zhou, Lulu;Yu, An;Chen, Zhilong;Zhou, Ronghua;Yang, Zaiqing
    • BMB Reports
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    • v.43 no.7
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    • pp.491-498
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    • 2010
  • 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 $PPAR{\gamma}$ and KLF15 on chemerin and its receptors. The data showed that KLF15, but not $PPAR{\gamma}$, 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.

Single Nucleotide Polymorphism in the Coding Region of Bovine Chemerin Gene and Their Associations with Carcass Traits in Japanese Black Cattle

Endophilin A2: A Potential Link to Adiposity and Beyond

  • Alfadda, Assim A.;Sallam, Reem M.;Gul, Rukhsana;Hwang, Injae;Ka, Sojeong
    • Molecules and Cells
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    • v.40 no.11
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    • pp.855-863
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    • 2017
  • Adipose tissue plays a central role in regulating dynamic cross-talk between tissues and organs. A detailed description of molecules that are differentially expressed upon changes in adipose tissue mass is expected to increase our understanding of the molecular mechanisms that underlie obesity and related metabolic co-morbidities. Our previous studies suggest a possible link between endophilins (SH3Grb2 proteins) and changes in body weight. To explore this further, we sought to assess the distribution of endophilin A2 (EA2) in human adipose tissue and experimental animals. Human paired adipose tissue samples (subcutaneous and visceral) were collected from subjects undergoing elective abdominal surgery and abdominal liposuction. We observed elevated EA2 gene expression in the subcutaneous compared to that in the visceral human adipose tissue. EA2 gene expression negatively correlated with adiponectin and chemerin in visceral adipose tissue, and positively correlated with $TNF-{\alpha}$ in subcutaneous adipose tissue. EA2 gene expression was significantly downregulated during differentiation of preadipocytes in vitro. In conclusion, this study provides a description of EA2 distribution and emphasizes a need to study the roles of this protein during the progression of obesity.