Effect of ciglitazone on adipogenic transdifferentiation of bovine skeletal muscle satellite cells
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Ciglitazone is a member of the thiazolidinedione family, and specifically binds to peroxisome proliferator-activated receptor-γ (PPARγ), thereby promoting adipocyte differentiation. We hypothesized that ciglitazone as a PPARγ ligand in the absence of an adipocyte differentiation cocktail would increase adiponectin and adipogenic gene expression in bovine satellite cells (BSC). Muscle-derived BSCs were isolated from six, 18-month-old Yanbian Yellow Cattle. The BSC were cultured for 96 h in differentiation medium containing 5 μM ciglitazone (CL), 10 μM ciglitazone (CM), or 20 μM ciglitazone (CH). Control (CON) BSC were cultured only in a differentiation medium (containing 2% horse serum). The presence of myogenin, desmin, and paired box 7 (Pax7) proteins was confirmed in the BSC by immunofluorescence staining. The CL, CM, and CH treatments produced higher concentrations of triacylglycerol and lipid droplet accumulation in myotubes than those of the CON treatment. Ciglitazone treatments significantly increased the relative expression of PPARγ, CCAAT/enhancer-binding protein alpha (C/EBPα), C/EBPβ, fatty acid synthase, stearoyl-CoA desaturase, and perilipin 2. Ciglitazone treatments increased gene expression of Pax3 and Pax7 and decreased expression of myogenic differentiation-1, myogenin, myogenic regulatory factor-5, and myogenin-4 (p < 0.01). Adiponectin concentration caused by ciglitazone treatments was significantly greater than CON (p < 0.01). RNA sequencing showed that 281 differentially expressed genes (DEGs) were found in the treatments of ciglitazone. DEGs gene ontology (GO) analysis showed that the top 10 GO enrichment significantly changed the biological processes such as protein trimerization, negative regulation of cell proliferation, adipocytes differentiation, and cellular response to external stimulus. Kyoto Encyclopedia of Genes and Genomes pathway analysis showed that DEGs were involved in the p53 signaling pathway, PPAR signaling pathway, biosynthesis of amino acids, tumor necrosis factor signaling pathway, non-alcoholic fatty liver disease, PI3K-Akt signaling pathway, and Wnt signaling pathway. These results indicate that ciglitazone acts as PPARγ agonist, effectively increases the adiponectin concentration and adipogenic gene expression, and stimulates the conversion of BSC to adipocyte-like cells in the absence of adipocyte differentiation cocktail.
Abstract
Ciglitazone is a member of the thiazolidinedione family, and specifically binds to peroxisome proliferator-activated receptor-γ (PPARγ), thereby promoting adipocyte differentiation. We hypothesized that ciglitazone as a PPARγ ligand in the absence of an adipocyte differentiation cocktail would increase adiponectin and adipogenic gene expression in bovine satellite cells (BSC). Muscle-derived BSCs were isolated from six, 18-month-old Yanbian Yellow Cattle. The BSC were cultured for 96 h in differentiation medium containing 5 μM ciglitazone (CL), 10 μM ciglitazone (CM), or 20 μM ciglitazone (CH). Control (CON) BSC were cultured only in a differentiation medium (containing 2% horse serum). The presence of myogenin, desmin, and paired box 7 (Pax7) proteins was confirmed in the BSC by immunofluorescence staining. The CL, CM, and CH treatments produced higher concentrations of triacylglycerol and lipid droplet accumulation in myotubes than those of the CON treatment. Ciglitazone treatments significantly increased the relative expression of PPARγ, CCAAT/enhancer-binding protein alpha (C/EBPα), C/EBPβ, fatty acid synthase, stearoyl-CoA desaturase, and perilipin 2. Ciglitazone treatments increased gene expression of Pax3 and Pax7 and decreased expression of myogenic differentiation-1, myogenin, myogenic regulatory factor-5, and myogenin-4 (p < 0.01). Adiponectin concentration caused by ciglitazone treatments was significantly greater than CON (p < 0.01). RNA sequencing showed that 281 differentially expressed genes (DEGs) were found in the treatments of ciglitazone. DEGs gene ontology (GO) analysis showed that the top 10 GO enrichment significantly changed the biological processes such as protein trimerization, negative regulation of cell proliferation, adipocytes differentiation, and cellular response to external stimulus. Kyoto Encyclopedia of Genes and Genomes pathway analysis showed that DEGs were involved in the p53 signaling pathway, PPAR signaling pathway, biosynthesis of amino acids, tumor necrosis factor signaling pathway, non-alcoholic fatty liver disease, PI3K-Akt signaling pathway, and Wnt signaling pathway. These results indicate that ciglitazone acts as PPARγ agonist, effectively increases the adiponectin concentration and adipogenic gene expression, and stimulates the conversion of BSC to adipocyte-like cells in the absence of adipocyte differentiation cocktail.
참고문헌 (35)
- Karen Yeow, "Inhibition of myogenesis enables adipogenic trans-differentiation in the C2C12 myogenic cell line", FEBS Letters, 506(2), pp.157~162 (2001), Wiley[DOI]
- N. K. Singh, "Transdifferentiation of porcine satellite cells to adipoblasts with ciglitizone1", Journal of Animal Science, 85(5), pp.1126~1135 (2007), Oxford University Press (OUP)[DOI]
- Xiang Z Li, "Oleic acid in the absence of a PPARγ agonist increases adipogenic gene expression in bovine muscle satellite cells1", Journal of Animal Science, 97(10), pp.4114~4123 (2019), Oxford University Press (OUP)[DOI]
- Lydia Teboul, "Thiazolidinediones and Fatty Acids Convert Myogenic Cells into Adipose-like Cells", Journal of Biological Chemistry, 270(47), pp.28183~28187 (1995), Elsevier BV[DOI]
- K.Y. Chung, "Lipid characteristics of subcutaneous adipose tissue and M. longissimus thoracis of Angus and Wagyu steers fed to US and Japanese endpoints", Meat Science, 73(3), pp.432~441 (2006), Elsevier BV[DOI]
- Manuel J. Deutsch, "Digital image analysis approach for lipid droplet size quantitation of Oil Red O-stained cultured cells", Analytical Biochemistry, 445, pp.87~89 (2014), Elsevier BV[DOI]
- S. H. Choi, "AMPKα, C", EBPβ, CPT1β, GPR43, PPARγ, and SCD Gene Expression in Single- and Co-cultured Bovine Satellite Cells and Intramuscular Preadipocytes Treated with Palmitic, Stearic, Oleic, and Linoleic Acid, 2015, pp.28(3), 411~419[DOI]
- E. Hu, "Transdifferentiation of myoblasts by the adipogenic transcription factors PPAR gamma and C", EBP alpha, 1995, pp.92(21), 9856~9860[DOI]
- C. Fux, "Dual-regulated expression of C", EBP- and BMP-2 enables differential differentiation of C2C12 cells into adipocytes and osteoblasts, 2004, pp.32(1), e1~[DOI]
- Wan-Chun Li, "The molecular basis of transdifferentiation", Journal of Cellular and Molecular Medicine, 9(3), pp.569~582 (2005), Wiley[DOI]
- Pallavi Cheguru, "Adipocyte differentiation-specific gene transcriptional response to C18 unsaturated fatty acids plus insulin", Pflügers Archiv - European Journal of Physiology, 463(3), pp.429~447 (2012), Springer Science and Business Media LLC[DOI]
- Márcio Y. Hassumi, "PPAR-γ agonist rosiglitazone prevents inflammatory periodontal bone loss by inhibiting osteoclastogenesis", International Immunopharmacology, 9(10), pp.1150~1158 (2009), Elsevier BV[DOI]
- Z. Yablonka-Reuveni, "Defining the transcriptional signature of skeletal muscle stem cells1,2", Journal of Animal Science, 86(suppl_14), pp.E207~E216 (2008), Oxford University Press (OUP)[DOI]
- Rehfeldt C, "Consequences of birth weight for postnatal growth performance and carcass quality in pigs as related to myogenesis", J Anim Sci, 84 (2006)[DOI]
- Dorothy Moseti, "Molecular Regulation of Adipogenesis and Potential Anti-Adipogenic Bioactive Molecules", International Journal of Molecular Sciences, 17(1), pp.124~ (2016), MDPI AG[DOI]
- Martina I. Lefterova, "New developments in adipogenesis", Trends in Endocrinology & Metabolism, 20(3), pp.107~114 (2009), Elsevier BV[DOI]
- J. B. Kim, "ADD1", SREBP1 activates PPARγ through the production of endogenous ligand, 1998, pp.95(8), 4333~4337[DOI]
- Haruaki Kageyama, "Lipoprotein lipase mRNA in white adipose tissue but not in skeletal muscle is increased by pioglitazone through PPAR-γ", Biochemical and Biophysical Research Communications, 305(1), pp.22~27 (2003), Elsevier BV[DOI]
- Lizcano Fernando, "Regulation of adipogenesis by nucelar receptor PPARγ is modulated by the histone demethylase JMJD2C", Genetics and Molecular Biology, 34(1), pp.19~24 (2011), FapUNIFESP (SciELO)[DOI]
- Anders Kristian Haakonsson, "Acute Genome-Wide Effects of Rosiglitazone on PPARγ Transcriptional Networks in Adipocytes", Molecular Endocrinology, 27(9), pp.1536~1549 (2013), The Endocrine Society[DOI]
- G. Cossu, "Wnt signaling and the activation of myogenesis in mammals", The EMBO Journal, 18(24), pp.6867~6872 (1999), Wiley[DOI]
- Stewart CEH, "Adaptive processes in skeletal muscle : molecular regulators and genetic influences", J Musculoskelet Neuronal Interact, 6, pp.73~86 (2006)
- D.D.W. Cornelison, "MyoD−", − Satellite Cells in Single-Fiber Culture Are Differentiation Defective and MRF4 Deficient, 2000, pp.224(2), 122~137[DOI]
- Chao Wang, "Loss of MyoD Promotes Fate Transdifferentiation of Myoblasts Into Brown Adipocytes", EBioMedicine, 16, pp.212~223 (2017), Elsevier BV[DOI]
- Ronnie Minnaard, "Adipocyte Differentiation-Related Protein and OXPAT in Rat and Human Skeletal Muscle: Involvement in Lipid Accumulation and Type 2 Diabetes Mellitus", The Journal of Clinical Endocrinology & Metabolism, 94(10), pp.4077~4085 (2009), The Endocrine Society[DOI]
- M.V. Dodson, "Cell Supermarket: Adipose Tissue as a Source of Stem Cells", Journal of Genomics, 1, pp.39~44 (2013), Ivyspring International Publisher[DOI]
- Xia Yi, "The whole transcriptional profiling of cellular metabolism during adipogenesis from hMSCs", Journal of Cellular Physiology, 235(1), pp.349~363 (2020), Wiley[DOI]
- Andreas Barthel, "Regulation of GLUT1 Gene Transcription by the Serine", Threonine Kinase Akt1, 1999, pp.274(29), 20281~20286[DOI]
- Sarah E. Ross, "Inhibition of Adipogenesis by Wnt Signaling", Science, 289(5481), pp.950~953 (2000), American Association for the Advancement of Science (AAAS)[DOI]
- Sona Kang, "Effects of Wnt Signaling on Brown Adipocyte Differentiation and Metabolism Mediated by PGC-1α", Molecular and Cellular Biology, 25(4), pp.1272~1282 (2005), American Society for Microbiology[DOI]
- Tyler C Prestwich, "Wnt", β-catenin signaling in adipogenesis and metabolism, 2007, pp.19(6), 612~617[DOI]
- Erine H. Budi, "Transforming Growth Factor-β Receptors and Smads: Regulatory Complexity and Functional Versatility", Trends in Cell Biology, 27(9), pp.658~672 (2017), Elsevier BV[DOI]
- Jong Seok Kang, "New regulatory mechanisms of TGF-β receptor function", Trends in Cell Biology, 19(8), pp.385~394 (2009), Elsevier BV[DOI]
- Antonio Fabregat, "The Reactome Pathway Knowledgebase", Nucleic Acids Research, 46(D1), pp.D649~D655 (2018), Oxford University Press (OUP)[DOI]
- Yiyang Yue, "Transforming growth factor beta (TGF-β) mediates cardiac fibrosis and induces diabetic cardiomyopathy", Diabetes Research and Clinical Practice, 133, pp.124~130 (2017), Elsevier BV[DOI]