Secretory and cytosolic phospholipase A(2)regulate the long-term cytokine-induced eicosanoid production in human keratinocytes

Cytokine. 2000 Aug;12(8):1189-94. doi: 10.1006/cyto.1999.0727.

Abstract

The involvement of cytosolic phospholipase A(2)(cPLA(2)) and secretory non-pancreatic PLA(2)(npPLA(2)) in release of arachidonic acid (AA) preceding eicosanoid formation in the human keratinocyte cell line HaCaT was examined. Interleukin 1beta (IL-1beta) and tumour necrosis factor-alpha (TNF), phorbol myristate acetate (PMA) and calcium ionophore A(23187)increased the extracellular AA release, and stimulated eicosanoid synthesis as determined by HPLC analysis. The main metabolites after stimulation with IL-1beta, PMA or A(23187)were PGE(2), an unidentified PG and LTB(4), while TNF stimulated HETE-production. Both cPLA(2)and npPLA(2)message and enzyme activity were detected in unstimulated HaCaT cells. IL-1beta, PMA and TNF increased both cPLA(2)enzyme activity and expression, but did not lead to any increase in npPLA(2)expression or activity. The selective npPLA(2)inhibitors LY311727 and 12-epi-scalaradial, or the cPLA(2)inhibitor arachidonyl trifluoro methyl ketone (AACOCF(3)) reduced IL-1beta-induced eicosanoid production in a concentration dependent manner. The results presented strongly suggest that both cPLA(2)and npPLA(2)contribute to the long-term generation of AA preceding eicosanoid production in differentiated, human keratinocytes. Inhibitors against npPLA2 or cPLA2 enzymes should be useful in treating inflammatory skin diseases, such as psoriasis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arachidonic Acid / metabolism
  • Arachidonic Acids / pharmacology
  • Cell Differentiation
  • Cells, Cultured
  • Cytokines / physiology*
  • Cytosol / enzymology
  • Eicosanoids / biosynthesis*
  • Enzyme Inhibitors / pharmacology
  • Humans
  • Interleukin-1 / physiology
  • Keratinocytes / metabolism*
  • Models, Biological
  • Phospholipases A / antagonists & inhibitors
  • Phospholipases A / genetics
  • Phospholipases A / metabolism
  • Phospholipases A / physiology*

Substances

  • Arachidonic Acids
  • Cytokines
  • Eicosanoids
  • Enzyme Inhibitors
  • Interleukin-1
  • arachidonyltrifluoromethane
  • Arachidonic Acid
  • Phospholipases A