Chemerin Is a Novel Adipokine Associated with Obesity and Metabolic Syndrome

Metabolic Research Unit, School of Exercise and Nutrition Sciences, Deakin University, Pigdons Road, Waurn Ponds, Geelong, Victoria 3217, Australia.
Endocrinology (Impact Factor: 4.5). 11/2007; 148(10):4687-94. DOI: 10.1210/en.2007-0175
Source: PubMed


Soluble protein hormones are key regulators of a number of metabolic processes, including food intake and insulin sensitivity. We have used a signal sequence trap to identify genes that encode secreted or membrane-bound proteins in Psammomys obesus, an animal model of obesity and type 2 diabetes (T2D). Using this signal sequence trap, we identified the chemokine chemerin as being a novel adipokine. Gene expression of chemerin and its receptor, chemokine-like receptor 1 (CMKLR1), was significantly higher in adipose tissue of obese and type 2 diabetic P. obesus compared with lean, normoglycemic P. obesus. Fractionation of P. obesus adipose tissue confirmed that chemerin was predominantly expressed in adipocytes, whereas CMKLR1 was expressed in both adipocytes and stromal-vascular cells of adipose tissue. In 3T3-L1 adipocytes, chemerin was markedly induced during differentiation, whereas CMKLR1 was down-regulated during differentiation. Serum chemerin levels were measured by ELISA in human plasma samples from 114 subjects with T2D and 142 normal glucose tolerant controls. Plasma chemerin levels were not significantly different between subjects with T2D and normal controls. However, in normal glucose tolerant subjects, plasma chemerin levels were significantly associated with body mass index, circulating triglycerides, and blood pressure. Here we report, for the first time, that chemerin is an adipokine, and circulating levels of chemerin are associated with several key aspects of metabolic syndrome.

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    • "An in vitro experiment showed that Chemerin and CMKLR1 were necessary for adipogenesis (Goralski et al., 2007; Roh et al., 2007). Knockdown of Chemerin in 3T3-L1 pre-adipocytes (Bozaoglu et al., 2007) and human multi-potent bone marrow-derived stromal cells (Muruganandan et al., 2010) abrogates adipogenesis, suggesting that Chemerin is necessary for adipocyte differentiation. Chemerin mainly impacts the mitotic clonal expansion phase in the first days of differentiation and has no effect on adipogenesis when knocked down in later phases of differentiation. "
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    ABSTRACT: Chemerin is an adipocyte-secreted adipokine that regulates the differentiation and metabolism of adipose through auto-/paracrine signaling. Its function in the differentiation of multipotent myoblast cells has thus far received little attention. In this study, C2C12 myoblast cells were cultured in the medium with Chemerin, and the differentiation potential of C2C12 myoblasts was analyzed. The results showed that Chemerin increased ROS levels and TG content of C2C12 cells. At the same time, the mRNA expressions and protein concentrations of the adipogenic factors PPARγ, C/EBPα and UCP1 were up-regulated, while the muscle specific transcription factors MyoD, Myogenin and MyHC were decreased in cultured C2C12 cells. In conclusion, the adipokine Chemerin promoted the adipogenic differentiation potential and altered the fate of myoblast cells from myogenesis to adipogenesis, which contributed in part to the up-regulated adipocyte genes. Our study reveals the importance of functional Chemerin signaling in adipogenesis and in directing the differentiation of multipotent myoblast cells. Copyright © 2015. Published by Elsevier Ireland Ltd.
    Molecular and Cellular Endocrinology 07/2015; 414. DOI:10.1016/j.mce.2015.07.006 · 4.41 Impact Factor
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    • ", Fatima et al. [21], Bozaoglu et al. [9], Bozaoglu et al. [10] Androgen sensitivity High expression in visceral adipose tissue in men and women with PCOS "
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    ABSTRACT: The discovery of several adipokines with diverse activities and their involvement in regulation of various pathophysiological functions of human body has challenged the researchers. In the family of adipokine, chemerin is a novel and unique addition. Ever since the first report on chemerin as a chemo- attractant protein, there are numerous studies showing a multitasking capacity of chemerin in the maintenance of homeostasis, for the activation of natural killer cells, macrophages and dendritic cells in both innate and adaptive immunity. Its diversity ranges from generalized inflammatory cascades to being explicitly involved in the manifestation of arthritis psoriasis, and peritonitis. Its association with certain cancerous tissue may render it as a potential tumor marker. In present review, we aim to consolidate recent data of investigations on chemerin in context to functional characteristics with a special reference to its role as a metabolic signal in inflammation and non-metabolic syndromes.
    Peptides 09/2014; 62. DOI:10.1016/j.peptides.2014.09.019 · 2.62 Impact Factor
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    • "However, chemerin levels higher in hepatic vein blood samples than in systemic circulation indicate that it is synthesized and secreted by the liver [16]. In humans, chemerin mRNA was found to be highly expressed not only in white adipose tissue, but also in liver and lungs [7]. Chemerin exerts its functions by binding the G proteincoupled receptor, chemokine receptor-like 1 (CMKLR1) (also known as chemerin receptor 23 (ChemR23)) [2, 17]. "
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    ABSTRACT: Introduction. Chemerin seems to be involved in pathogenesis of chronic hepatitis C (CHC). Hepatic expressions of chemerin and its receptor, chemokine receptor-like 1 (CMKLR1), in CHC have not been studied so far. Aim. To evaluate chemerin and CMKLR1 hepatic expression together with serum chemerin concentration in CHC patients and to assess their relationship with metabolic and histopathological abnormalities. Methods. The study included 63 nonobese CHC patients. Transcription of chemerin and CMKLR1 was assessed by quantitative real-time PCR, while serum chemerin was assessed by enzyme-linked immunosorbent assay. Results. Expression of chemerin and CMKLR1 was present in the liver of all CHC patients regardless of sex or age. This expression was not associated with necroinflammatory activity and steatosis grade, fibrosis stage, and metabolic abnormalities. There was a negative association between serum chemerin and chemerin hepatic expression (r = (-0.41), P = 0.006). Conclusion. The study for the first time confirmed a marked expression of chemerin and CMKLR1 in the liver of CHC patients. The study was performed using the homogenates of human liver tissue, so it is not possible to define whether hepatocytes or other cell types which are abundantly represented in the liver constitute the main source of chemerin and CMKLR1 mRNA.
    BioMed Research International 07/2014; 2014(47-48):517820. DOI:10.1155/2014/517820 · 1.58 Impact Factor
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