Vasoactive intestinal peptide, pituitary adenylate cyclase-activating peptide, and noradrenaline induce the transcription factors CCAAT/enhancer binding protein (C/EBP)-beta and C/EBP delta in mouse cortical astrocytes: involvement in cAMP-regulated glycogen metabolism

J Neurosci. 1996 Feb 1;16(3):919-29. doi: 10.1523/JNEUROSCI.16-03-00919.1996.

Abstract

We have described previously a transcription-dependent induction of glycogen resynthesis by the vasoactive intestinal peptide (VIP) or noradrenaline (NA) in astrocytes, which is mediated by cAMP. Because it has been postulated that the cAMP-mediated regulation of energy balance in hepatocytes and adipocytes is channeled at least in part through the CCAAT/enhancer binding protein (C/EBP) family of transcription factors, we tested the hypothesis that C/EBP isoforms could be expressed in mouse cortical astrocytes and that their level of expression could be regulated by VIP, by the VIP-related neuropeptide pituitary adenylate cyclase-activating peptide (PACAP), or by NA. We report in this study that in these cells, C/EBP beta and C/EBP delta are induced by VIP, PACAP, or NA via the cAMP second-messenger pathway. Induction of C/EBP beta and -delta mRNA by VIP occurs in the presence of a protein synthesis inhibitor. Thus, c/ebp beta and c/ebp delta behave as cAMP-inducible immediate-early genes in astrocytes. Moreover, transfection of astrocytes with expression vectors selectively producing the transcriptionally active form of C/EBP beta, termed liver-enriched transcriptional activator protein, or C/EBP delta enhance the glycogen resynthesis elicited by NA, whereas an expression vector producing the transcriptionally inactive form of C/EBP beta, termed liver-enriched transcriptional inhibitory protein, reduces this resynthesis. These results support the idea that C/EBP beta and -delta regulate gene expression of energy metabolism-related enzymes in astrocytes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 8-Bromo Cyclic Adenosine Monophosphate / pharmacology
  • Animals
  • Anisomycin / pharmacology
  • Astrocytes / drug effects*
  • Astrocytes / physiology
  • CCAAT-Enhancer-Binding Protein-delta
  • CCAAT-Enhancer-Binding Proteins
  • Cells, Cultured
  • Cerebral Cortex / cytology
  • Colforsin / pharmacology
  • Cyclic AMP / physiology*
  • DNA-Binding Proteins / biosynthesis*
  • DNA-Binding Proteins / genetics
  • Energy Metabolism / genetics
  • Gene Expression Regulation / drug effects*
  • Genes, Immediate-Early
  • Glycogen / metabolism*
  • Leucine Zippers / genetics
  • Mice
  • Nerve Tissue Proteins / biosynthesis*
  • Nerve Tissue Proteins / genetics
  • Neuropeptides / pharmacology*
  • Norepinephrine / pharmacology*
  • Nuclear Proteins / biosynthesis*
  • Nuclear Proteins / genetics
  • Pituitary Adenylate Cyclase-Activating Polypeptide
  • Protein Synthesis Inhibitors / pharmacology
  • Second Messenger Systems / drug effects
  • Second Messenger Systems / physiology
  • Transcription Factors / biosynthesis*
  • Transcription Factors / genetics
  • Transcription, Genetic / drug effects*
  • Vasoactive Intestinal Peptide / pharmacology*

Substances

  • Adcyap1 protein, mouse
  • CCAAT-Enhancer-Binding Proteins
  • Cebpd protein, mouse
  • DNA-Binding Proteins
  • Nerve Tissue Proteins
  • Neuropeptides
  • Nuclear Proteins
  • Pituitary Adenylate Cyclase-Activating Polypeptide
  • Protein Synthesis Inhibitors
  • Transcription Factors
  • CCAAT-Enhancer-Binding Protein-delta
  • Colforsin
  • 8-Bromo Cyclic Adenosine Monophosphate
  • Vasoactive Intestinal Peptide
  • Anisomycin
  • Glycogen
  • Cyclic AMP
  • Norepinephrine