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The capability of platelet-activating factor (PAF) to induce
transcription factor activation was examined. In stably transfected
Chinese hamster ovary cells expressing the PAF receptor (CHO-PAFR), PAF
stimulation resulted in the nuclear expression of a DNA binding
activity with specificity to the
Volume 270,
Number 25,
Issue of June 23, pp. 14928-14934, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
B Activation through a G Protein-coupled Pathway
B sequence. The p50 and p65
proteins, constituents of the prototypic nuclear factor B
(NF-B), were identified as components of the DNAprotein
complexes by antipeptide antibodies in gel supershift as well as UV
cross-linking experiments. PAF induced an initial decrease and
subsequent increase of cytoplasmic I
B
levels, accompanied by
up-regulation of the IB messenger RNA, a feature of NF-B
activation. PAF-induced B binding activity was detected within 15
min after agonist stimulation, peaked at 30-40 min, and remained
detectable by 2.5 h. SR 27417, a PAF receptor antagonist, blocked
PAF-induced B binding activity but not that induced by tumor
necrosis factor- (TNF). Cholera toxin treatment markedly
reduced PAF-induced B binding activity, whereas pertussis toxin
had no significant inhibitory effect. Neither of the two toxins
affected the B binding activity induced by TNF in the same
cells. In addition to the CHO-PAFR cells, PAF stimulated B binding
activity in the murine P388D
macrophage and the human ASK.0
B cell lines that express endogenous PAF receptors. These results imply
a potential role of PAF in the regulation of gene expression through a
G protein-coupled transcription factor activation pathway.
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