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Porcine peroxisome proliferator-activated receptor induces transdifferentiation of myocytes into adipocytes¹

Department of Animal Science and Technology, National Taiwan University, Taipei 106, Taiwan

³ Corresponding author: sding{at}ntu.edu.tw

Peroxisome proliferator-activated receptor 2 (PPAR) is a nuclear transcription factor that regulates adipocyte differentiation and lipogenic genes during adipogenesis. The activity of rodent PPAR is regulated by phosphorylation of serine 112. The current experiment was designed to study the ability of porcine PPAR to stimulate transdifferentiation of myoblasts to adipocytes by overexpressing wild-type PPAR or mutated PPAR (serine 112 was mutated to alanine) in mouse myoblast cells. The expression of adipogenic marker genes (adipocyte fatty acid binding protein, lipoprotein lipase, and glycerol-3 phosphate dehydrogenase) in cells stably expressing mutated porcine PPAR was greater than in cells with wild-type PPAR, indicating that the mutated PPAR has greater adipogenic capability than the wild-type PPAR. Under treatment with a ligand, both wild-type and mutant porcine PPAR-expressing C2C12 myoblasts differentiated into adipocytes in 10 d. The expression of myogenic marker genes (myogenin, myogenic regulatory factor-4) was suppressed in cells transfected with the mutated PPAR or wild-type PPAR. Moreover, wild-type and mutant PPAR were able to inhibit myogenesis without addition of a ligand. Our results suggest that porcine wild-type PPAR and mutated PPAR can both convert myoblast cells into adipocytes, and also that the ability to transdifferentiate was greater in cells containing the mutated PPAR than in cells containing the wild-type PPAR. Therefore, the existence of serine 112 in PPAR may have a role in regulating adipocyte differentiation.

Key Words: adipocyte differentiation • adipocyte gene • myoblast transdifferentiation • myocyte gene • peroxisome proliferator-activated receptor

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