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B and Expression of ICAM-1
*
UNIGEN–Center for Molecular Biology,
Department of Physiology and Biomedical Engineering,
Institute of Chemistry,
§
Institute of Botany,
¶
Institute of Cancer Research and Molecular Biology, Norwegian University of Science and Technology, and
||
Department of Clinical Chemistry, Trondheim Regional Hospital, Trondheim, Norway; and
#
Department of Chemistry, University of Oslo, Oslo, Norway
TNF signaling mechanisms involved in activation of transcription
factor NF-
B were studied in the human keratinocyte cell line HaCaT.
We show that TNF-induced activation of NF-B was inhibited by the
well-known selective inhibitors of cytosolic phospholipase
A2 (cPLA2): the trifluoromethyl ketone analogue
of arachidonic acid (AACOCF3) and methyl arachidonyl fluorophosphate.
The trifluoromethyl ketone analogue of eicosapentaenoic acid (EPACOCF3)
also suppressed TNF-induced NF-B activation and inhibited in vitro
cPLA2 enzyme activity with a similar potency as AACOCF3.
The arachidonyl methyl ketone analogue (AACOCH3) and the
eicosapentanoyl analogue (EPACHOHCF3), which both failed to inhibit
cPLA2 enzyme activity in vitro, had no effect on
TNF-induced NF-B activation. TNF-induced NF-B activation was also
strongly reduced in cells stimulated in the presence of the secretory
PLA2 (sPLA2) inhibitors 12-epi-scalaradial and
LY311727. Addition of excess arachidonic acid suppressed the inhibitory
effect of 12-epi-scalaradial and LY311727. Moreover, both methyl
arachidonyl fluorophosphate and 12-epi-scalaradial blocked TNF-mediated
enhancement of expression of ICAM-1. Activation of NF-B by IL-1ß
was markedly less sensitive to both cPLA2 and
sPLA2 inhibitors. The results indicate that both
cPLA2 and sPLA2 may be involved in the TNF
signal transduction pathway leading to nuclear translocation of NF-B
and to NF-B-activated gene expression in HaCaT
cells.
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