Radicicol, a protein tyrosine kinase inhibitor, suppresses the expression of mitogen-inducible cyclooxygenase in macrophages stimulated with lipopolysaccharide and in experimental glomerulonephritis

J Biol Chem. 1995 Mar 10;270(10):5418-26. doi: 10.1074/jbc.270.10.5418.

Abstract

Two isoforms of cyclooxygenase (COX) have been identified in eukaryotic cells: a constitutively expressed COX-1 and mitogen-inducible COX-2, which is selectively expressed in response to various inflammatory stimuli. Thus, COX-2 instead of COX-1 is implicated to produce prostanoids mediating inflammatory responses. Major efforts have been focused on identifying nonsteroidal anti-inflammatory drugs (NSAIDS) which can selectively inhibit the enzyme activity of COX-2. Such NSAIDS would be more desirable anti-inflammatory agents in comparison to NSAIDS which inhibit both COX-1 and COX-2. Other than glucocorticoids, pharmacological agents which can selectively suppress the expression of COX-2 without affecting that of COX-1 have not been identified. We report here that radicicol, a fungal antibiotic, is a potent protein tyrosine kinase inhibitor, and that it inhibits the expression of COX-2 without affecting COX-1 expression in lipopolysaccharide (LPS)-stimulated macrophages with the IC50 value of 27 nM. Radicicol inhibited tyrosine phosphorylation of p53/56lyn, a Src family tyrosine kinase and one of the major tyrosine-phosphorylated proteins in LPS-stimulated macrophages. Radicicol also inhibited COX-2 expression in vivo in glomeruli of rats with experimental glomerulonephritis induced by the anti-glomerular basement membrane antibodies, in which COX-2 expression is known to be enhanced. The enzyme activity of COX-1 or COX-2 was not affected by radicicol in macrophages. Radiciciol also suppressed the COX-2 expression induced by IL-1 beta in rat smooth muscle cells. Other protein tyrosine kinase inhibitors suppressed the LPS-induced COX-2 expression in macrophages but at much higher concentrations than needed for radicicol. Radicicol did not inhibit the COX-2 expression induced by phorbol 12-myristate 13-acetate in macrophages. These results suggest that the activation of tyrosine-specific protein kinases is the proximal obligatory step in the LPS-induced signal transduction pathway leading to the induction of COX-2 expression in macrophages. The magnitude of the inhibition of COX-2 protein synthesis by radicicol was much greater than that of the steady state levels of COX-2 mRNA. These results suggest that radicicol inhibits COX-2 expression mainly at post-transcriptional steps.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Anti-Inflammatory Agents, Non-Steroidal / pharmacology
  • Antibodies / toxicity
  • Antifungal Agents / pharmacology*
  • Basement Membrane / immunology
  • Blotting, Western
  • Gene Expression / drug effects*
  • Glomerulonephritis / enzymology*
  • Glyceraldehyde-3-Phosphate Dehydrogenases / biosynthesis
  • Inflammation
  • Isoenzymes / biosynthesis
  • Kidney Glomerulus / drug effects
  • Kidney Glomerulus / enzymology*
  • Kidney Glomerulus / immunology
  • Kinetics
  • Lactones / chemistry
  • Lactones / isolation & purification
  • Lactones / pharmacology*
  • Lipopolysaccharides / pharmacology*
  • Macrolides
  • Macrophages, Alveolar / drug effects
  • Macrophages, Alveolar / enzymology*
  • Mitogens / pharmacology
  • Molecular Structure
  • Prostaglandin-Endoperoxide Synthases / analysis
  • Prostaglandin-Endoperoxide Synthases / biosynthesis
  • Protein-Tyrosine Kinases / antagonists & inhibitors*
  • RNA, Messenger / analysis
  • RNA, Messenger / biosynthesis
  • Rats
  • Rats, Sprague-Dawley
  • Tetradecanoylphorbol Acetate / pharmacology
  • Time Factors

Substances

  • Anti-Inflammatory Agents, Non-Steroidal
  • Antibodies
  • Antifungal Agents
  • Isoenzymes
  • Lactones
  • Lipopolysaccharides
  • Macrolides
  • Mitogens
  • RNA, Messenger
  • Prostaglandin-Endoperoxide Synthases
  • Glyceraldehyde-3-Phosphate Dehydrogenases
  • Protein-Tyrosine Kinases
  • monorden
  • Tetradecanoylphorbol Acetate