RISS 검색 - 국내학술지논문 상세보기

다국어 초록 (Multilingual Abstract)

Objective: It is commonly accepted that adiponectin binds to its two receptors to regulate fatty acid metabolism in adipocytes. To better understand their functions in the regulation of intramuscular adipogenesis in goats, we cloned the three genes (adiponectin [AdipoQ], adiponectin receptor 1 [AdipoR1], and AdipoR2) encoding these proteins and detected their mRNA distribution in different tissues. We also determined the role of AdipoQ in the adipogenic differentiation of goat skeletal muscle satellite cells (SMSCs). Methods: SMSCs were isolated using 1 mg/mL Pronase E from the longissimus dorsi muscles of 3-day-old female Nanjiang brown goats. Adipogenic differentiation was induced in satellite cells by transferring the cells to Dulbecco's modified Eagle's medium supplemented with an isobutylmethylxanthine, dexamethasone and insulin cocktail. The pEGFP-N1-AD plasmid was transfected into SMSCs using Lipofectamine 2000. Expression of adiponectin in tissues and SMSCs was detected by quantitative polymerase chain reaction and immunocytochemical staining. Results: The three genes were predominantly expressed in adipose and skeletal muscle tissues. According to fluorescence and immunocytochemical analyses, adiponectin protein expression was only observed in the cytoplasm, suggesting that adiponectin is localized to the cytoplasm of goat SMSCs. In SMSCs overexpressing the AdipoQ gene, adiponectin promoted SMSC differentiation into adipocytes and significantly (p<0.05) up-regulated expression of AdipoR2, acetyl-CoA carboxylase, fatty-acid synthase, and sterol regulatory element-binding protein-1, though expression of CCAAT/enhancer-binding $protein-{\alpha}$, peroxisome proliferator-activated receptor ${\gamma}$, and AdipoR1 did not change significantly. Conclusion: Adiponectin induced SMSC differentiation into adipocytes, indicating that adiponectin may promote intramuscular adipogenesis in goat SMSC.

참고문헌 (Reference)

1 White UA, "Transcriptional factors that promote formation of white adipose tissue" 318 : 10-14, 2010

2 Shams M, "The relationship between serum adiponectin levels with the presence and severity of coronary artery disease" 15 : 611-616, 2012

3 Shapiro L, "The crystal structure of a complement-1q family protein suggests an evolutionary link to tumor necrosis factor" 8 : 335-340, 1998

4 Yamauchi T, "Targeted disruption of AdipoR1 and AdipoR2 causes abrogation of adiponectin binding and metabolic actions" 13 : 332-339, 2007

5 Katsiougiannis S, "Salivary gland epithelial cells: a new source of the immunoregulatory hormone adiponectin" 54 : 2295-2299, 2006

6 Fruebis J, "Proteolytic cleavage product of 30-kDa adipocyte complement-related protein increases fatty acid oxidation in muscle and causes weight loss in mice" 98 : 2005-2010, 2001

7 Lefterova MI, "PPARgamma and C/EBP factors orchestrate adipocyte biology via adjacent binding on a genome-wide scale" 22 : 2941-2952, 2008

8 Narasimhan ML, "Osmotin is a homolog of mammalian adiponectin and controls apoptosis in yeast through a homolog of mammalian adiponectin receptor" 17 : 171-180, 2005

9 Johnson PF, "Molecular stop signs: regulation of cell-cycle arrest by C/EBP transcription factors" 118 : 2545-2555, 2005

10 Ramachandran R, "Molecular cloning and tissue expression of chicken AdipoR1 and AdipoR2 complementary deoxyribonucleic acids" 33 : 19-31, 2007