Thiazolidinediones and fatty acids convert myogenic cells into adipose-like cells.
Fatty acids and thiazolidinediones act as potent activators of the adipose differentiation program in established preadipose cell lines. In this report, the effects of these agents on the differentiation pathway of myoblasts have been investigated. Exposure of C2C12N myoblasts (a subclone of the C2C12 cell line) to thiazolidinediones or fatty acids prevents the expression of myogenin, alpha-actin, and creatine kinase, thus abolishing the formation of multinucleated myotubes. These treatments lead in parallel to the expression of a typical adipose differentiation program including acquisition of adipocyte morphology and activation of adipose-related genes. A similar transition toward the adipose differentiation pathway also occurs in mouse muscle satellite cells maintained in primary culture. Thiazolidinediones exert their adipogenic effects only in non-terminally differentiated myoblasts; myotubes are insensitive to the compounds. Continuous exposure to inducers after growth arrest is not required to maintain the adipose phenotype, but proliferation of adipose-like C2C12N cells leads to a complete reversion toward undifferentiated cells able to undergo either myogenic or adipogenic differentiation depending on the composition of culture medium. These results indicate that adipogenic inducers, such as thiazolidinediones or fatty acids, specifically convert the differentiation pathway of myoblasts into that of adipoblasts.
D015117:5,8,11,14-Eicosatetraynoic Acid / Q000494:pharmacology; D000199:Actins / Q000096:biosynthesis; D000273:Adipose Tissue / Q000166:cytology*; D000818:Animals; D015415:Biomarkers; D002352:Carrier Proteins / Q000096:biosynthesis; D002454:Cell Differentiation / Q000187:drug effects*; D002455:Cell Division / Q000187:drug effects; D002839:Chromans / Q000494:pharmacology; D002999:Clone Cells; D003402:Creatine Kinase / Q000096:biosynthesis; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D005230:Fatty Acids, Nonesterified / Q000494:pharmacology*; D015870:Gene Expression / Q000187:drug effects*; D005993:Glycerolphosphate Dehydrogenase / Q000096:biosynthesis; D007004:Hypoglycemic Agents / Q000494:pharmacology*; D019787:Linoleic Acid; D008041:Linoleic Acids / Q000494:pharmacology; D051379:Mice; D009132:Muscles / Q000166:cytology* / Q000187:drug effects / Q000378:metabolism; D018996:Myelin P2 Protein / Q000096:biosynthesis; D018008:Myogenin / Q000096:biosynthesis; D009363:Neoplasm Proteins; D009419:Nerve Tissue Proteins; D019308:Palmitic Acid; D010169:Palmitic Acids / Q000494:pharmacology; D010641:Phenotype; D000077205:Pioglitazone; D000077154:Rosiglitazone; D013844:Thiazoles / Q000494:pharmacology*; D045162:Thiazolidinediones; D000077288:Troglitazone
D000199:Actins; D015415:Biomarkers; D002352:Carrier Proteins; D002839:Chromans; C082667:Fabp5 protein, mouse; C086936:Fabp7 protein, mouse; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D005230:Fatty Acids, Nonesterified; D007004:Hypoglycemic Agents; D008041:Linoleic Acids; D018996:Myelin P2 Protein; C503801:Myog protein, mouse; D018008:Myogenin; D009363:Neoplasm Proteins; D009419:Nerve Tissue Proteins; D010169:Palmitic Acids; D013844:Thiazoles; D045162:Thiazolidinediones; D000077154:Rosiglitazone; D015117:5,8,11,14-Eicosatetraynoic Acid; D019308:Palmitic Acid; D019787:Linoleic Acid; D005993:Glycerolphosphate Dehydrogenase; D003402:Creatine Kinase; D000077288:Troglitazone; D000077205:Pioglitazone