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http://dx.doi.org/10.5713/ajas.2012.12083

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

Suzuki, Y. (Laboratory of Animal Physiology, Graduate School of Agricultural Science, Tohoku University)
Hong, Y.H. (Laboratory of Animal Production, Faculty of Life and Environmental Science, Shimane University)
Song, S.H. (Laboratory of Animal Physiology, Graduate School of Agricultural Science, Tohoku University)
Ardiyanti, A. (Laboratory of Animal Physiology, Graduate School of Agricultural Science, Tohoku University)
Kato, D. (Laboratory of Animal Physiology, Graduate School of Agricultural Science, Tohoku University)
So, K.H. (Laboratory of Animal Physiology, Graduate School of Agricultural Science, Tohoku University)
Katoh, K. (Laboratory of Animal Physiology, Graduate School of Agricultural Science, Tohoku University)
Roh, Sang-Gun (Laboratory of Animal Physiology, Graduate School of Agricultural Science, Tohoku University)
Publication Information
Asian-Australasian Journal of Animal Sciences / v.25, no.9, 2012 , pp. 1316-1321 More about this Journal
Abstract
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.
Keywords
Bovine; Adipocyte; Chemerin; CMKLR1; TNF-${\alpha}$; Adiponectin;
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1 Suzuki, Y., S. H. Song, K. Sato, K. H. So, A. Ardiyanti, S. Kitayama, Y. H. Hong, S. D. Lee, K. C. Choi, A. Hagino, K. Katoh and S. G. Roh. 2012. Chemerin analog regulates energy metabolism in sheep. Anim. Sci. J. 83:263-267.   DOI   ScienceOn
2 White, U. A. and J. M. Stephens. 2010. Transcriptional factors that promote formation of white adipose tissue. Mol. Cell. Endocrinol. 318:10-14.   DOI   ScienceOn
3 Wittamer, V., J. D. Franssen, M. Vulcano, J. F. Mirjolet, E. Le Poul, I. Migeotte, S. Brezillon, R. Tyldesley, C. Blanpain, M. Detheux, A. Mantovani, S. Sozzani, G. Vassart, M. Parmentier and D. Communi. 2003. Specific recruitment of antigen-presenting cells by chemerin, a novel processed ligand from human inflammatory fluids. J. Exp. Med. 198:977-985.   DOI   ScienceOn
4 Yamauchi, T., J. Kamon, Y. Minokoshi, Y. Ito, H. Waki, S. Uchida, S. Yamashita, M. Noda, S. Kita, K. Ueki, K. Eto, Y. Akanuma, P. Froguel, F. Foufelle, P. Ferre, D. Carling, S. Kimura, R. Nagai, B. B. Kahn and T. Kadowaki. 2002. Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMP-activated protein kinase. Nat. Med. 8:1288-1295.   DOI   ScienceOn
5 Mussig, K., H. Staiger, F. Machicao, C. Thamer, J. Machann, F. Schick, C. D. Claussen, N. Stefan, A. Fritsche and H. U. Haring. 2009. RARRES2, encoding the novel adipokine chemerin, is a genetic determinant of disproportionate regional body fat distribution: a comparative magnetic resonance imaging study. Metab. Clin. Exp. 58:519-524.   DOI   ScienceOn
6 Ohtani, Y., T. Yonezawa, S. H. Song, T. Takahashi, A. Ardiyanti, K. Sato, A. Hagino, S. G. Roh and K. Katoh. 2011. Gene expression and hormonal regulation of adiponectin and its receptors in bovine mammary gland and mammary epithelial cells. Anim. Sci. J. 82:99-106.   DOI   ScienceOn
7 Roh, S. G., D. Hishikawa, Y.-H. Hong and S. Sasaki. 2006. Control of adipogenesis in ruminants. Anim. Sci. J. 77:472-477.   DOI   ScienceOn
8 Roh, S. G., S. H. Song, K. C. Choi, K. Katoh, V. Wittamer, M. Parmentier and S. Sasaki. 2007. Chemerin-a new adipokine that modulates adipogenesis via its own receptor. Biochem. Biophys. Res. Commun. 362:1013-1018.   DOI   ScienceOn
9 Sell, H., J. Laurencikiene, A. Taube, K. Eckardt, A. Cramer, A. Horrighs, P. Arner and J. Eckel. 2009. Chemerin is a novel adipocyte-derived factor inducing insulin resistance in primary human skeletal muscle cells. Diabetes 58:2731-2740.   DOI   ScienceOn
10 Shimamura, K., M. Matsuda, Y. Miyamoto, R. Yoshimoto, T. Seo and S. Tokita. 2009. Identification of a stable chemerin analog with potent activity toward ChemR23. Peptides 30:1529-1538.   DOI   ScienceOn
11 Song, S. H., K. Fukui, K. Nakajima, T. Kozakai, S. Sasaki, S. G. Roh and K. Katoh. 2010. Cloning, expression analysis, and regulatory mechanisms of bovine chemerin and chemerin receptor. Domest. Anim. Endocrinol. 39:97-105.   DOI   ScienceOn
12 Suganami, T. and Y. Ogawa. 2010. Adipose tissue macrophages: their role in adipose tissue remodeling. J. Leukoc. Biol. 88:33-39.   DOI   ScienceOn
13 Kralisch, S., S. Weise, G. Sommer, J. Lipfert, U. Lossner, M. Bluher, M. Stumvoll and M. Fasshauer. 2009. Interleukin- 1beta induces the novel adipokine chemerin in adipocytes in vitro. Regul. Pept. 154:102-106.   DOI   ScienceOn
14 Kukla, M., K. Zwirska-Korczala, M. Hartleb, M. Waluga, A. Chwist, M. Kajor, M. Ciupinska-Kajor, A. Berdowska, E. Wozniak-Grygiel and R. Buldak. 2010. Serum chemerin and vaspin in non-alcoholic fatty liver disease. Scand. J. Gastroenterol. 45:235-242.   DOI   ScienceOn
15 Laliotis, G. P., I. Bizelis and E. Rogdakis. 2010. Comparative approach of the de novo fatty acid synthesis (Lipogenesis) between ruminant and non ruminant mammalian species: From biochemical level to the main regulatory lipogenic genes. Curr. Genomics 11:168-183.   DOI   ScienceOn
16 Le Lay, S., P. Ferre and I. Dugail. 2004. Adipocyte cholesterol balance in obesity. Biochem. Soc. Trans. 32:103-106.   DOI
17 Lefterova, M. I. and M. A. Lazar. 2009. New developments in adipogenesis. Trends Endocrinol. Metab. 20:107-114.   DOI   ScienceOn
18 Lehrke, M., A. Becker, M. Greif, R. Stark, R. P. Laubender, F. von Ziegler, C. Lebherz, J. Tittus, M. Reiser, C. Becker, B. Goke, A. W. Leber, K. G. Parhofer and U. C. Broedl. 2009. Chemerin is associated with markers of inflammation and components of the metabolic syndrome but does not predict coronary atherosclerosis. Eur. J. Endocrinol. 161:339-344.   DOI   ScienceOn
19 Muruganandan, S., S. D. Parlee, J. L. Rourke, M. C. Ernst, K. B. Goralski and C. J. Sinal. 2011. Chemerin, a novel peroxisome proliferator-activated receptor $\gamma$(PPAR$\gamma$) target ene that promotes mesenchymal stem cell adipogenesis. J. Biol. Chem. 286:23982-23995.   DOI   ScienceOn
20 Muruganandan, S., A. A. Roman and C. J. Sinal. 2010. Role of chemerin/CMKLR1 signaling in adipogenesis and osteoblastogenesis of bone marrow stem cells. J. Bone Miner. Res. 25:222-234.   DOI
21 Bauer, S., J. Wanninger, S. Schmidhofer, J. Weigert, M. Neumeier, C. Dorn, C. Hellerbrand, N. Zimara, A. Schaffler, C. Aslanidis, and C. Buechler. 2011. Sterol regulatory element-binding protein 2 (SREBP2) activation after excess triglyceride storage induces chemerin in hypertrophic adipocytes. Endocrinology 152:26-35.   DOI   ScienceOn
22 Bionaz, M. and J. J. Loor. 2008. ACSL1, AGPAT6, FABP3, LPIN1, and SLC27A6 are the most abundant isoforms in bovine mammary tissue and their expression is affected by stage of lactation. J. Nutr. 138:1019-1024.
23 Bozaoglu, K., K. Bolton, J. McMillan, P. Zimmet, J. Jowett, G. Collier, K. Walder and D. Segal. 2007. Chemerin is a novel adipokine associated with obesity and metabolic syndrome. Endocrinology 148:4687-4694.   DOI   ScienceOn
24 Combs, T. P., U. B. Pajvani, A. H. Berg, Y. Lin, L. A. Jelicks, M. Laplante, A. R. Nawrocki, M. W. Rajala, A. F. Parlow, L. Cheeseboro, Y. Y. Ding, R. G. Russell, D. Lindemann, A. Hartley, G. R. Baker, S. Obici, Y. Deshaies, M. Ludgate, L. Rossetti and P. E. Scherer. 2004. A transgenic mouse with a deletion in the collagenous domain of adiponectin displays elevated circulating adiponectin and improved insulin sensitivity. Endocrinology 145:367-383.   DOI   ScienceOn
25 Fajas, L., J. C. Fruchart and J. Auwerx. 1998. Transcriptional control of adipogenesis. Curr. Opin. Cell Biol. 10:165-173.   DOI   ScienceOn
26 Friedman, M. I. and I. Ramirez. 1994. Food intake in diabetic rats: relationship to metabolic effects of insulin treatment. Physiol. Behav. 56:373-378.   DOI   ScienceOn
27 Goralski, K. B., T. C. McCarthy, E. A. Hanniman, B. A. Zabel, E. C. Butcher, S. D. Parlee, S. Muruganandan and C. J. Sinal. 2007. Chemerin, a novel adipokine that regulates adipogenesis and adipocyte metabolism. J. Biol. Chem. 282:28175-28188.   DOI   ScienceOn
28 Guilherme, A., J. V. Virbasius, V. Puri and M. P. Czech. 2008. Adipocyte dysfunctions linking obesity to insulin resistance and type 2 diabetes. Nat. Rev. Mol. Cell Biol. 9:367-377.   DOI   ScienceOn