Modulation of phospholipase A2 activity in human fibroblasts

Br J Pharmacol. 1989 Mar;96(3):656-60. doi: 10.1111/j.1476-5381.1989.tb11865.x.

Abstract

1. Human embryonic skin fibroblasts (HSF) incubated overnight with either human recombinant interleukin-1 alpha (rIL-1 alpha) or interleukin-1 beta (rIL-1 beta) released large amounts of prostaglandin E2 (PGE2). 2. rIL-1 beta, bradykinin (Bk) and arachidonic acid (AA) significantly stimulated PGE2 release from HSF incubated overnight in the presence of either interleukin. 3. Hydrocortisone inhibited the PGE2 release induced by rIL-1 beta and Bk, but not by AA. 4. The steroid inhibitory effect was reversed by actinomycin D as well as by an anti-lipocortin monoclonal antibody. 5. The results suggest that in HSF, rIL-1 beta is able to stimulate both cyclo-oxygenase and phospholipase A2 (PLA2) activity. 6. The stimulation of PLA2 activity by rIL-1 beta is inhibited by hydrocortisone, probably via induction of lipocortin-like proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antibodies, Monoclonal
  • Cells, Cultured
  • Dactinomycin / pharmacology
  • Dinoprostone / biosynthesis
  • Dinoprostone / metabolism
  • Fibroblasts / enzymology
  • Humans
  • Hydrocortisone / pharmacology
  • Interleukin-1 / pharmacology
  • Phospholipases / metabolism*
  • Phospholipases A / metabolism*
  • Phospholipases A2
  • Recombinant Proteins / pharmacology

Substances

  • Antibodies, Monoclonal
  • Interleukin-1
  • Recombinant Proteins
  • Dactinomycin
  • Phospholipases
  • Phospholipases A
  • Phospholipases A2
  • Dinoprostone
  • Hydrocortisone