TAILIEUCHUNG - Báo cáo khoa học: Adipophilin protein expression in muscle – a possible protective role against insulin resistance

Adipophilin is a 50 kDa protein that belongs to the PAT family (perilipin, adipophilin, TIP47, S3-12 and OXPAT), which comprises proteins involved in the coating of lipid droplets. Little is known about the functional role of adipophilin in muscle. Using the C2C12 cell line as a model, we demon-strate that palmitic acid-treated cells highly express the adipophilin protein in a dose-dependent way. | Adipophilin protein expression in muscle - a possible protective role against insulin resistance Janneke de Wilde1 2 Egbert Smit1 2 Frank J. M. Snepvangers2 Nicole W. J. de Wit1 3 Ronny Mohren1 2 Martijn F. M. Hulshof1 2 and Edwin C. M. Mariman1 2 1 Nutrigenomics Consortium Top Institute Food and Nutrition Wageningen The Netherlands 2 Department of Human Biology NUTRIM Schoolfor Nutrition Toxicology and Metabolism Maastricht University MedicalCentre The Netherlands 3 Nutrition Metabolism and Genomics group Wageningen University The Netherlands Keywords 2D gel electrophoresis C2C12 cells insulin signaling intramuscular triglycerides lipid droplet Correspondence J. de Wilde Department of Human Biology Maastricht University PO Box 616 6200 MD Maastricht The Netherlands Fax 31 43 36 70976 Tel 31 43 38 81509 E-mail Received 4 November 2009 revised 27 November 2009 accepted 30 November 2009 doi Adipophilin is a 50 kDa protein that belongs to the PAT family perilipin adipophilin TIP47 S3-12 and OXPAT which comprises proteins involved in the coating of lipid droplets. Little is known about the functional role of adipophilin in muscle. Using the C2C12 cell line as a model we demonstrate that palmitic acid-treated cells highly express the adipophilin protein in a dose-dependent way. Next we show that oleic acid is a more potent inducer of adipophilin protein levels than palmitic acid. Cells treated with oleic acid have a higher adipophilin protein expression and higher triglyceride levels but less impairment of insulin signaling than cells treated with palmitic acid. Additionally we show that peroxisome proliferator-activated receptor PPAR a PPARp ỗ and PPARy agonists all increase the expression of the adipophilin protein in C2C12 cells. This effect was most pronounced for the PPARa agonist GW7647. Furthermore the expression of adipophilin as a 37 kDa N-terminally truncated protein is higher in the gastrocnemius than .

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