Negative regulation of adipogenesis from human mesenchymal stem cells by Jun N-terminal kinase

Biochem Biophys Res Commun. 2005 Jan 14;326(2):499-504. doi: 10.1016/j.bbrc.2004.11.056.

Abstract

Human mesenchymal stem cells (hMSCs) are capable of differentiating into several cell types including adipocytes, osteoblasts, and chondrocytes, under appropriate culture conditions. We found that SP600125, an inhibitor of Jun N-terminal kinase (JNK), promoted adipogenesis whereas it repressed osteogenesis from hMSCs. SP600125 increased the expression of adipogenic transcription factors, CCAAT/enhancer-binding proteins alpha and beta as well as peroxisome proliferator-activated receptor gamma2, which suggested that the chemical acted on the early steps of transcriptional regulatory cascade in adipogenesis. A gene reporter assay showed that SP600125 and a dominant negative JNK promoted a transcriptional activity dependent on the cAMP-response element (CRE). Thus, JNK represses adipogenesis from hMSCs probably by, at least in part, inhibiting the transactivating function of CRE-binding protein. Another action of JNK, phosphorylation at Ser(307) of insulin receptor substrate-1, was also predicted to contribute to the repression of adipogenesis.

MeSH terms

  • Adipocytes / cytology*
  • Adipocytes / drug effects
  • Adipocytes / enzymology*
  • Adipocytes / metabolism
  • Anthracenes / pharmacology
  • Biomarkers / metabolism
  • Cell Differentiation
  • Cell Line
  • Enzyme Inhibitors / pharmacology
  • Humans
  • JNK Mitogen-Activated Protein Kinases / antagonists & inhibitors
  • JNK Mitogen-Activated Protein Kinases / metabolism*
  • Mesenchymal Stem Cells / cytology*
  • Mesenchymal Stem Cells / drug effects
  • Mesenchymal Stem Cells / enzymology*
  • Mesenchymal Stem Cells / metabolism
  • Osteogenesis / drug effects
  • Phosphoserine / metabolism
  • Transcriptional Activation / drug effects

Substances

  • Anthracenes
  • Biomarkers
  • Enzyme Inhibitors
  • Phosphoserine
  • pyrazolanthrone
  • JNK Mitogen-Activated Protein Kinases