Regulation of intrauterine prostaglandin biosynthesis: interactions between protein kinase C and interleukin 1 beta

Prostaglandins Leukot Essent Fatty Acids. 1994 Mar;50(3):137-40. doi: 10.1016/0952-3278(94)90096-5.

Abstract

Activation of protein kinase C with phorbol esters stimulates prostaglandin (PG) biosynthesis in many cell types whereas down-regulation of protein kinase C can suppress stimulatory responses. Interleukin-1 beta (IL-1 beta) can stimulate PG production by intrauterine tissues and may play a significant part in the mechanisms of preterm labor associated with intrauterine infection. Hence we have evaluated the effects of staurosporine and H7 (inhibitors of protein kinase C) on IL-1 beta stimulation of amnion, chorion and decidual prostaglandin E2 (PGE2) production. Staurosporine and H7 alone were without effect on PGE2 production by any cell type. However with minor exceptions both protein kinase C inhibitors enhanced the stimulatory actions of IL-1 beta on PGE2 production by all three cell types. Hence we believe that protein kinase C is closely linked to the regulation of intrauterine PG biosynthesis and that these links may have multiple layers of complexity.

MeSH terms

  • 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine
  • Alkaloids / pharmacology
  • Amnion / drug effects
  • Amnion / metabolism
  • Chorion / drug effects
  • Chorion / metabolism
  • Decidua / drug effects
  • Decidua / metabolism
  • Dinoprostone / biosynthesis*
  • Female
  • Humans
  • In Vitro Techniques
  • Interleukin-1 / pharmacology*
  • Isoquinolines / pharmacology
  • Obstetric Labor, Premature / etiology
  • Obstetric Labor, Premature / metabolism
  • Piperazines / pharmacology
  • Pregnancy
  • Protein Kinase C / antagonists & inhibitors
  • Protein Kinase C / metabolism*
  • Staurosporine
  • Uterus / metabolism*

Substances

  • Alkaloids
  • Interleukin-1
  • Isoquinolines
  • Piperazines
  • 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine
  • Protein Kinase C
  • Staurosporine
  • Dinoprostone