Protein kinase C eta mediates lipopolysaccharide-induced nitric-oxide synthase expression in primary astrocytes

J Biol Chem. 1998 Jul 31;273(31):19424-30. doi: 10.1074/jbc.273.31.19424.

Abstract

The signaling pathway involved in protein kinase C (PKC) activation and role of PKC isoforms in lipopolysaccharide (LPS)-induced nitric oxide (NO) release were studied in primary cerebellar astrocytes. LPS caused a dose- and time-dependent increase in NO release and inducible NO synthase (iNOS) expression. The tyrosine kinase inhibitor, genestein, the phosphatidylcholine-phospholipase C inhibitor, D609, and the phosphatidate phosphodrolase inhibitor, propranolol, attenuated the LPS effects, whereas the PI-PLC inhibitor, U73122, had no effect. The PKC inhibitors (staurosporine, Ro 31-8220, Go 6976, and calphostin C) also inhibited LPS-induced NO release and iNOS expression. However, long term (24 h) pretreatment of cells with 12-O-tetradecanoyl phorbol-13-acetate (TPA) did not affect the LPS response. Previous results have shown that TPA-induced translocation, but not down-regulation, of PKCeta occurs in astrocytes (Chen, C. C., and Chen, W. C. (1996) Glia 17, 63-71), suggesting possible involvement of PKCeta in LPS-mediated effects. Treatment with antisense oligonucleotides for PKCeta or delta, another isoform abundantly expressed in astrocytes, demonstrated the involvement of PKCeta, but not delta, in LPS-mediated effects. Stimulation of cells for 1 h with LPS caused activation of nuclear factor (NF)-kB in the nuclei as detected by the formation of a NF-kB-specific DNA-protein complex; this effect was inhibited by genestein, D609, propranolol, or Ro 31-8220 or by PKCeta antisense oligonucleotides, but not by long term TPA treatment. These data suggest that in astrocytes, LPS might activate phosphatidylcholine-phospholipase C and phosphatidylcholine-phospholipase D through an upstream protein tyrosine kinase to induce PKC activation. Of the PKC isoforms present in these cells, only activation of PKCeta by LPS resulted in the stimulation of NF-kB-specific DNA-protein binding and then initiated the iNOS expression and NO release. This is further evidence demonstrating that different members of the PKC family within a single cell are involved in specific physiological responses.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Astrocytes / enzymology*
  • Brain / enzymology
  • Enzyme Activation / physiology
  • Enzyme Inhibitors / pharmacology
  • Gene Expression Regulation, Enzymologic / drug effects*
  • Isoenzymes / physiology
  • Lipopolysaccharides / pharmacology*
  • Nitric Oxide Synthase / metabolism*
  • Nitric Oxide Synthase Type II
  • Oligonucleotides, Antisense / pharmacology
  • Phospholipase D / metabolism
  • Protein Kinase C / physiology*
  • Rats
  • Rats, Wistar
  • Signal Transduction / physiology
  • Tetradecanoylphorbol Acetate / pharmacology
  • Type C Phospholipases / metabolism

Substances

  • Enzyme Inhibitors
  • Isoenzymes
  • Lipopolysaccharides
  • Oligonucleotides, Antisense
  • Nitric Oxide Synthase
  • Nitric Oxide Synthase Type II
  • Nos2 protein, rat
  • Protein Kinase C
  • Type C Phospholipases
  • Phospholipase D
  • Tetradecanoylphorbol Acetate