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Arachidonic acid induces c-jun gene expression in stromal cells stimulated
by interleukin-1 and tumor necrosis factor-alpha: evidence for a
tyrosine-kinase-dependent process
MT Rizzo, HS Boswell, L Mangoni, C Carlo-Stella and V Rizzoli
Division of Hematology and Bone Marrow Transplantation, Parma University
School of Medicine, Italy.
We have previously shown that granulocyte-macrophage colony-stimulating
factor (GM-CSF) gene expression induced by interleukin-1 (IL-1) and tumor
necrosis factor-alpha (TNF-alpha) in the murine stromal cell line +/+.1-LDA
11 involves activation of phospholipase A2 (PLA2). Furthermore, induction
of GM-CSF gene expression due to release of arachidonic acid as a result of
PLA2 activation was mediated by the transcriptional factor c-jun. In the
present study, we have investigated the potential mechanism involved in the
induction of c-jun gene expression by arachidonic acid. Arachidonic acid
induced transcription of c-jun mRNA. Downregulation of protein kinase C
(PKC) by chronic exposure of stromal cells to the phorbol ester 12-O-
tetradecanoyl-phorbol-13-acetate (TPA; 400 nmol/L) did not effect c-jun
expression induced by arachidonate. Moreover, pretreatment of cells with
the PKC inhibitor, calphostin C (1 mumol/L), caused a marked decrease of
c-jun expression induced by TPA, but had no influence on c- jun expression
induced by arachidonate. To explore the hypothesis that a tyrosine kinase
signalling pathway, independent of PKC activation, was involved in
arachidonate-induced c-jun expression, stromal cells were pretreated with
the protein tyrosine kinase inhibitor, genistein, before challenge with
arachidonic acid. Arachidonate 50 mumol/L)- induced c-jun expression was
inhibited, in a dose- and time-dependent manner, by genistein. Genistein
similarly inhibited c-jun expression in stromal cells exposed to IL-1 (500
U/mL) plus TNF-alpha (500 U/mL). The potential role of a tyrosine kinase
pathway in arachidonate-mediated c- jun expression was further investigated
by assaying the tyrosine kinase activity of cells challenged with
arachidonic acid, IL-1, and TNF- alpha. Exposure of stromal cells to
arachidonic acid induced a 2.1-fold increase in intracellular tyrosine
kinase activity determined by phosphorylation of the synthetic peptide,
raytide, in the presence of [gamma-32P]-ATP. Similarly, IL-1 and TNF-alpha
induced 1.7- and 2.4- fold increases in tyrosine protein kinase activity,
respectively. The effect of arachidonic acid on tyrosine kinase activity
was inhibited by genistein and was enhanced by sodium vanadate. The
increase of protein tyrosine kinase activity detected in
arachidonate-stimulated cells was associated, in a dose- and time-dependent
fashion, with tyrosine phosphorylation of 240-, 40-, and 29-kD substrates.
These results are consistent with the hypothesis that a tyrosine
phosphorylation process is triggered by arachidonate as an early event in
the signalling pathway that leads to increased expression of
c-jun.(ABSTRACT TRUNCATED AT 400 WORDS)
Volume 86,
Issue 8,
pp. 2967-2975,
10/15/1995
Copyright © 1995 by The American Society of Hematology
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