IL-1-induced receptor activator of NF-kappa B ligand in human periodontal ligament cells involves ERK-dependent PGE2 production

Bone. 2005 Feb;36(2):267-75. doi: 10.1016/j.bone.2004.09.011.

Abstract

Periodontitis, an inflammatory disorder of the supporting tissue of teeth, is one of the most common infectious diseases in humans. Periodontal pathogens promote inflammatory cytokines such as interleukin-1 (IL-1) and prostaglandin E2 (PGE2), resulting in alveolar bone destruction. In the present study, we examined the cellular and molecular mechanisms of IL-1-induced osteoclastogenesis using a coculture system of human periodontal ligament (PDL) cells and mouse spleen cells. IL-1alpha induced tartrate-resistant acid phosphatase positive (TRAP+) cell formation in a dose-dependent manner. IL-1alpha up-regulated receptor activator of NF-kappaB ligand (RANKL) and down-regulated osteoprotegerin (OPG) mRNA expression in PDL cells. The addition of cell-permeable PKI, an inhibitor of the cAMP/PKA signaling pathway, to the cocultures 8 h after the IL-1alpha stimulation inhibited IL-1alpha-induced TRAP+ cell formation. IL-1alpha-induced TRAP+ cell formation was completely blocked by either NS398, a selective inhibitor of cyclooxygenase (COX)-2, or PD98059, a specific inhibitor of extracellular signal-regulated kinase (ERK). Pretreatment with NS398 and PD98059 also inhibited both the up-regulation of RANKL and the down-regulation of OPG expression by IL-1alpha in PDL cells. IL-1alpha activated ERK phosphorylation and PD98059 greatly inhibited both COX-2 mRNA expression and PGE(2) production induced by IL-1alpha in PDL cells. In contrast, NEMO binding domain (NBD) peptide, a specific inhibitor of NF-kappaB signaling, did not affect COX2, RANKL, or OPG mRNA expression induced by IL-1alpha. These results suggest that IL-1alpha stimulates osteoclast formation by increasing the expression level of RANKL versus OPG via ERK-dependent PGE2 production in PDL cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carrier Proteins / biosynthesis*
  • Carrier Proteins / metabolism
  • Cells, Cultured
  • Coculture Techniques
  • Dinoprostone / biosynthesis*
  • Dinoprostone / genetics
  • Extracellular Signal-Regulated MAP Kinases / antagonists & inhibitors
  • Extracellular Signal-Regulated MAP Kinases / genetics
  • Extracellular Signal-Regulated MAP Kinases / physiology*
  • Flavonoids / pharmacology
  • Glycoproteins / metabolism*
  • Humans
  • Interleukin-1 / pharmacology*
  • Membrane Glycoproteins / biosynthesis*
  • Membrane Glycoproteins / metabolism
  • Mice
  • NF-kappa B / biosynthesis*
  • NF-kappa B / genetics
  • Osteoprotegerin
  • Periodontal Ligament / cytology
  • Periodontal Ligament / drug effects*
  • Periodontal Ligament / metabolism*
  • Periodontium / cytology
  • Periodontium / drug effects
  • Periodontium / metabolism
  • RANK Ligand
  • Receptor Activator of Nuclear Factor-kappa B
  • Receptors, Cytoplasmic and Nuclear / metabolism*
  • Receptors, Tumor Necrosis Factor / metabolism*

Substances

  • Carrier Proteins
  • Flavonoids
  • Glycoproteins
  • Interleukin-1
  • Membrane Glycoproteins
  • NF-kappa B
  • Osteoprotegerin
  • RANK Ligand
  • Receptor Activator of Nuclear Factor-kappa B
  • Receptors, Cytoplasmic and Nuclear
  • Receptors, Tumor Necrosis Factor
  • TNFRSF11A protein, human
  • TNFRSF11B protein, human
  • TNFSF11 protein, human
  • Tnfrsf11a protein, mouse
  • Tnfrsf11b protein, mouse
  • Tnfsf11 protein, mouse
  • Extracellular Signal-Regulated MAP Kinases
  • Dinoprostone
  • 2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one