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Acetate alters the process of lipid metabolism in rabbits

Published online by Cambridge University Press:  04 December 2017

C. Fu
Affiliation:
Shandong Provincial Key Laboratory of Animal Biotechnology and Disease Control and Prevention, Department of Animal Science and Technology, Shandong Agricultural University, Taian 271018, China Poultry Institute, Shandong Academy of Agricultural Sciences, Jinan 250023, China
L. Liu*
Affiliation:
Shandong Provincial Key Laboratory of Animal Biotechnology and Disease Control and Prevention, Department of Animal Science and Technology, Shandong Agricultural University, Taian 271018, China
F. Li*
Affiliation:
Shandong Provincial Key Laboratory of Animal Biotechnology and Disease Control and Prevention, Department of Animal Science and Technology, Shandong Agricultural University, Taian 271018, China
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Abstract

An experiment was conducted to investigate the effect of acetate treatment on lipid metabolism in rabbits. New Zealand Rabbits (30 days, n=80) randomly received a subcutaneous injection (2 ml/injection) of 0, 0.5, 1.0 or 2.0 g/kg per day body mass acetate (dissolved in saline) for 4 days. Our results showed that acetate induced a dose-dependent decrease in shoulder adipose (P<0.05). Although acetate injection did not alter the plasma leptin and glucose concentration (P>0.05), acetate treatment significantly decreased the plasma adiponectin, insulin and triglyceride concentrations (P<0.05). In adipose, acetate injection significantly up-regulated the gene expression of peroxisome proliferator-activated receptor gamma (PPARγ), CCAAT/enhancer-binding protein α (C/EBPα), differentiation-dependent factor 1 (ADD1), adipocyte protein 2 (aP2), carnitine palmitoyltransferase 1 (CPT1), CPT2, hormone-sensitive lipase (HSL), G protein-coupled receptor (GPR41), GPR43, adenosine monophosphate-activated protein kinase α1 (AMPKα1), adiponectin receptor (AdipoR1), AdipoR2 and leptin receptor. In addition, acetate treatment significantly increased the protein levels of phosphorylated AMPKα, extracellular signaling-regulated kinases 1 and 2 (ERK1/2), p38 mitogen-activated protein kinase (P38 MAPK) and c-jun amino-terminal kinase (JNK). In conclusion, acetate up-regulated the adipocyte-specific transcription factors (PPARγ, C/EBPα, aP2 and ADD1), which were associated with the activated GPR41/43 and MAPKs signaling. Meanwhile, acetate decreased fat content via the upregulation of the steatolysis-related factors (HSL, CPT1 and CPT2), and AMPK signaling may be involved in the process.

Type
Research Article
Copyright
© The Animal Consortium 2017 

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References

Armstrong, VL, Wiggam, MI, Ennis, CN, Sheridan, B, Traub, AI, Atkinson, AB and Bell, PM 2001. Insulin action and insulin secretion in polycystic ovary syndrome treated with ethinyl oestradiol/cyproterone acetate. QJM: An International Journal of Medicine 94, 3137.Google Scholar
Bost, F, Aouadi, M, Caron, L and Binétruy, B 2005. The role of MAPKs in adipocyte differentiation and obesity. Biochimie 87, 5156.Google Scholar
Chen, SC, Brooks, R, Houskeeper, J, Bremner, SK, Dunlop, J, Viollet, B, Logan, PJ, Salt, IP, Ahmed, SF and Yarwood, SJ 2017. Metformin suppresses adipogenesis through both AMP-activated protein kinase (AMPK)-dependent and AMPK-independent mechanisms. Molecular and Cellular Endocrinology 440, 5768.Google Scholar
Choi, SH, Chung, KY, Johnson, BJ, Go, GW, Kim, KH, Choi, CW and Smith, SB 2013. Co-culture of bovine muscle satellite cells with preadipocytes increases PPARγ and C/EBPα gene expression in differentiated myoblasts and increases GPR43 gene expression in adipocytes. The Journal of Nutritional Biochemistry 24, 539543.Google Scholar
den Besten, G, Bleeker, A, Gerding, A, van Eunen, K, Havinga, R, van Dijk, TH, Oosterveer, MH, Jonker, JW, Groen, AK, Reijngoud, DJ and Bakker, BM 2015. Short-chain fatty acids protect against high-fat diet-induced obesity via a PPARγ-dependent switch from lipogenesis to fat oxidation. Diabetes 64, 23982408.Google Scholar
de Blas JC and Mateos GG 1998. Feed formulation. In The nutrition of rabbit (ed. C de Blas and J Wiseman), pp. 241–253. CABI Publishing, New York, NY, USAGoogle Scholar
Dewulf, EM, Cani, PD, Neyrinck, AM, Possemiers, S, Van Holle, A, Muccioli, GG, Deldicque, L, Bindels, LB, Pachikian, BD, Sohet, FM, Mignolet, E, Francaux, M, Larondelle, Y and Delzenne, NM 2011. Inulin-type fructans with prebiotic properties counteract GPR43 overexpression and PPARγ-related adipogenesis in the white adipose tissue of high-fat diet-fed mice. The Journal of Nutritional Biochemistry 22, 712722.Google Scholar
Engelman, JA, Berg, AH, Lewis, RY, Lin, A, Lisanti, MP and Scherer, PE 1999. Constitutively active mitogen-activated protein kinase kinase 6 (MKK6) or salicylate induces spontaneous 3T3-L1 adipogenesis. Journal of Biological Chemistry 274, 3563035638.Google Scholar
Gregoire, FM 2001. Adipocyte differentiation: from fibroblast to endocrine cell. Experimental Biology and Medicine 226, 9971002.Google Scholar
Handy, JA, Saxena, NK, Fu, P, Lin, S, Mells, JE, Gupta, NA and Anania, FA 2010. Adiponectin activation of AMPK disrupts leptin-mediated hepatic fibrosis via suppressors of cytokine signaling (SOCS-3). Journal of Cellular Biochemistry 110, 11951207.Google Scholar
Hardie, DG, Ross, FA and Hawley, SA 2012. AMPK: a nutrient and energy sensor that maintains energy homeostasis. Nature Reviews Molecular Cell Biology 13, 251262.Google Scholar
Hata, K, Nishimura, R, Ikeda, F, Yamashita, K, Matsubara, T, Nokubi, T and Yoneda, T 2003. Differential roles of Smad1 and p38 kinase in regulation of peroxisome proliferator-activating receptor gamma during bone morphogenetic protein 2-induced adipogenesis. Molecular Biology of the Cell 14, 545555.Google Scholar
He, Q, Huang, C, Zhao, L, Feng, J, Shi, Q, Wang, D and Wang, S 2013. α-Naphthoflavone inhibits 3T3-L1 pre-adipocytes differentiation via modulating p38MAPK signaling. International Journal of Clinical and Experimental Pathology 6, 168178.Google Scholar
Hong, YH, Nishimura, Y, Hishikawa, D, Tsuzuki, H, Miyahara, H, Gotoh, C, Choi, KC, Feng, DD, Chen, C, Lee, HG, Katoh, K, Roh, SG and Sasaki, S 2005. Acetate and propionate short chain fatty acids stimulate adipogenesis via GPCR43. Endocrinology 146, 50925099.Google Scholar
Hu, J, Kyrou, I, Tan, BK, Dimitriadis, GK, Ramanjaneya, M, Tripathi, G, Patel, V, James, S, Kawan, M, Chen, J and Randeva, HS 2016. Short-chain fatty acid acetate stimulates adipogenesis and mitochondrial biogenesis via GPR43 in brown adipocytes. Endocrinology 157, 18811894.Google Scholar
Hwang, JT, Lee, MS, Kim, HJ, Sung, MJ, Kim, HY, Kim, MS and Kwon, DY 2008. Antiobesity effect of ginsenoside Rg3 involves the AMPK and PPAR-gamma signal pathways. Phytotherapy Research 23, 262266.Google Scholar
Jurie, C, Cassar-Malek, I, Bonnet, M, Leroux, C, Bauchart, D, Boulesteix, P, Pethick, DW and Hocquette, JF 2007. Adipocyte fatty acid-binding protein and mitochondrial enzyme activities in muscles as relevant indicators of marbling in cattle. Journal of Animal Science 85, 26602669.Google Scholar
Kimura, I, Ozawa, K, Inoue, D, Imamura, T, Kimura, K, Maeda, T, Terasawa, K, Kashihara, D, Hirano, K, Tani, T, Takahashi, T, Miyauchi, S, Shioi, G, Inoue, H and Tsujimoto, G 2013. The gut microbiota suppresses insulin-mediated fat accumulation via the short-chain fatty acid receptor GPR43. Nature Communications 4, 1829.Google Scholar
Kraemer, FB and Shen, WJ 2006. Hormone-sensitive lipase knockouts. Nutrition & Metabolism 3, 1.Google Scholar
Laemmli, UK 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680685.Google Scholar
Lee, H, Kang, R, Bae, S and Yoon, Y 2011. AICAR, an activator of AMPK, inhibits adipogenesis via the WNT/b-catenin pathway in 3T3-L1 adipocytes. International Journal of Molecular Medicine 28, 6571.Google Scholar
Li, G, Yao, W and Jiang, H 2014. Short-chain fatty acids enhance adipocyte differentiation in the stromal vascular fraction of porcine adipose tissue. The Journal of Nutrition 144, 18871895.Google Scholar
Livak, KJ and Schmittgen, TD 2001. Analysis of relative gene expression data using real-time quantitative PCR and the 2 (−∆∆C(T)) method. Methods 25, 402408.Google Scholar
Lee, S, Cho, HY, Bui, HT and Kang, D 2014. The osteogenic or adipogenic lineage commitment of human mesenchymal stem cells is determined by protein kinase C delta. BMC Cell Biology 15, 42.Google Scholar
Mora, S and Fullerton, R 2015. Effects of short chain fatty acids on glucose and lipid metabolism in adipocytes. The FASEB Journal 29, 672675.Google Scholar
National Research Council (NRC) 1977. Nutrient requirements of rabbits, 2nd revised edition. National Academy of Sciences, Washington, DC, USA.Google Scholar
Pal, M, Febbraio, MA and Lancaster, GI 2016. The roles of c-Jun NH2-terminal kinases (JNKs) in obesity and insulin resistance. The Journal of Physiology 594, 267279.Google Scholar
Pantovic, A, Krstic, A, Janjetovic, K, Koci, J, Harhaji-Trajkovic, L, Bugarski, D and Trajkovic, V 2013. Coordinated time-dependent modulation of AMPK/Akt/mTOR signaling and autophagy controls osteogenic differentiation of human mesenchymal stem cells. Bone 52, 524531.Google Scholar
Rorato, R, Borges, BC, Uchoa, ET, Antunes-Rodrigues, J, Elias, CF and Elias, LLK 2017. LPS-induced low-grade inflammation increases hypothalamic JNK expression and causes central insulin resistance irrespective of body weight changes. International Journal of Molecular Sciences 18, 1431.Google Scholar
Sakakibara, S, Yamauchi, T, Oshima, Y, Tsukamoto, Y and Kadowaki, T 2006. Acetic acid activates hepatic AMPK and reduces hyperglycemia in diabetic KK-A(y) mice. Biochemical and Biophysical Research Communications 344, 597604.Google Scholar
Sale, EM, Atkinson, PG and Sale, GJ 1995. Requirement of MAP kinase for differentiation of fibroblasts to adipocytes, for insulin activation of p90 S6 kinase and for insulin or serum stimulation of DNA synthesis. The EMBO Journal 14, 674.Google Scholar
Solinas, G, Vilcu, C, Neels, JG, Bandyopadhyay, GK, Luo, JL, Naugler, W, Grivennikov, S, Wynshaw-Boris, A, Scadeng, M, Olefsky, JM and Karin, M 2007. JNK1 in hematopoietically derived cells contributes to diet-induced inflammation and insulin resistance without affecting obesity. Cell Metabolism 6, 386397.Google Scholar
Uddin, S, Ah-Kang, J, Ulaszek, J, Mahmud, D and Wickrema, A 2004. Differentiation stage-specific activation of p38 mitogen-activated protein kinase isoforms in primary human erythroid cells. Proceedings of the National Academy of Sciences 101, 147152.Google Scholar
Woo, JH, Lim, JH, Kim, YH, Suh, SI, Min, DS, Chang, JS, Lee, YH, Park, JW and Kwon, TK 2004. Resveratrol inhibits phorbol myristate acetate-induced matrix metalloproteinase-9 expression by inhibiting JNK and PKC delta signal transduction. Oncogene 23, 18451853.Google Scholar
Zhang, H, Zhang, X, Wang, Z, Dong, X, Tan, C, Zou, H, Peng, Q, Xue, B, Wang, L and Dong, G 2015. Effects of dietary energy level on lipid metabolism-related gene expression in subcutaneous adipose tissue of Yellow breed×Simmental cattle. Animal Science Journal 86, 392400.Google Scholar
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