p42/p44 mitogen-activated protein kinases activation is required for the insulin-like growth factor-I/insulin induced proliferation, but inhibits differentiation, in rat fetal brown adipocytes

Mol Endocrinol. 1998 Jun;12(6):825-34. doi: 10.1210/mend.12.6.0122.

Abstract

Insulin-like growth factor I (IGF-I)/insulin induced cytosolic p42/p44 mitogen-activated protein kinase (MAPK) activation in a time-dependent manner in fetal brown adipocytes, reaching a maximum at 5 min. Concurrently, nuclear p42/p44 MAPKs were also activated by IGF-I and insulin. This cytosolic and nuclear MAPK activation was totally prevented by pretreatment with the MAPK kinase (MEK1) inhibitor, PD98059. These results indicate that MEK mediates the IGF-I/insulin-induced p42/ p44 MAPK activation. IGF-I and insulin also increased the number of cells in the S + G2/M phases of the cell cycle, PCNA levels, and DNA synthesis at 24 h. This IGF-I/insulin-induced proliferation was completely blunted by the presence of MEK1 inhibitor. In contrast, inhibition of MEK1 potentiated the IGF-I-induced uncoupling protein (UCP-1) and the insulin-induced fatty acid synthase mRNAs expression after short and long-term treatments. Moreover, transient expression of a transfected active MEK construct (R4F) decreased IGF-I-induced UCP-1 and insulin-induced fatty acid synthase mRNA expression. These results demonstrate that p42/p44 MAPKs are essential intermediates for the IGF-I/insulin-induced mitogenesis, but may have a negative role in the regulation of adipocytic and thermogenic differentiation in brown adipocytes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adipose Tissue, Brown / cytology
  • Adipose Tissue, Brown / drug effects*
  • Adipose Tissue, Brown / embryology
  • Animals
  • Body Temperature Regulation / physiology
  • Calcium-Calmodulin-Dependent Protein Kinases / physiology*
  • Cell Cycle
  • Cell Differentiation / drug effects
  • Cell Division / drug effects
  • Cell Nucleus / metabolism
  • Cells, Cultured
  • Cytosol / metabolism
  • Enzyme Activation
  • Enzyme Induction
  • Fatty Acid Synthases / biosynthesis
  • Fatty Acid Synthases / genetics
  • Insulin / pharmacology*
  • Insulin-Like Growth Factor I / pharmacology*
  • MAP Kinase Kinase 1
  • Mitogen-Activated Protein Kinase 1 / physiology*
  • Mitogen-Activated Protein Kinase 3
  • Mitogen-Activated Protein Kinase Kinases*
  • Mitogen-Activated Protein Kinases*
  • Proliferating Cell Nuclear Antigen / analysis
  • Protein Serine-Threonine Kinases / physiology
  • Protein-Tyrosine Kinases / physiology
  • RNA, Messenger / biosynthesis
  • RNA, Messenger / genetics
  • Rats

Substances

  • Insulin
  • Proliferating Cell Nuclear Antigen
  • RNA, Messenger
  • Insulin-Like Growth Factor I
  • Fatty Acid Synthases
  • Protein-Tyrosine Kinases
  • Protein Serine-Threonine Kinases
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Mitogen-Activated Protein Kinase 1
  • Mitogen-Activated Protein Kinase 3
  • Mitogen-Activated Protein Kinases
  • MAP Kinase Kinase 1
  • Mitogen-Activated Protein Kinase Kinases