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J. Biol. Chem., Vol. 269, Issue 42, 25999-26005, Oct, 1994
A Roshak, G Sathe and LA Marshall
Studies were conducted to characterize a human monocyte model where the
role of the 85-kDa phospholipase A2 (PLA2) in prostanoid formation could be
evaluated. The presence of an immunologically related 85-kDa PLA2 and type
II 14-kDa PLA2 was demonstrated in human monocytes and their roles examined
in lipopolysaccharide (LPS)-induced monocyte prostaglandin E2 (PGE2)
formation. Exposure of human monocytes to LPS over 18 h resulted in the
up-regulation of the mitogen-inducible cyclooxygenase-2 and was accompanied
by production and release of prostaglandin E2 but not leukotriene C4. This
coincided with a 2-fold increase in the 85-kDa PLA2 protein and activity
levels. In contrast, there was no effect on the type II 14-kDa-like PLA2
activity measured in the 100,000 x g particulate fraction nor did LPS
induce the release of type II 14-kDa PLA2 into the medium. Treatment with
cycloheximide over 18 h resulted in a time-dependent decrease in cytosolic
85-kDa PLA2 protein and activity (half-life = 4 h), but there was no change
in the particulate type II 14-kDa-like PLA2 activity. Monocytes were
therefore exposed to an 85-kDa PLA2 initiation site-directed antisense
oligonucleotide which specifically decreased the cytosolic 85-kDa PLA2
protein levels and activity in a concentration-dependent manner. This had
no effect on the cyclooxygenase-2 (protein mass or the ability to convert
arachidonic acid to PGE2) or the particulate fraction sn-2 acylhydrolytic
activity but was associated with a decrease in LPS- induced PGE2
production. Taken together, these data support a role for the cytosolic
85-kDa PLA2 in LPS-induced monocyte PGE2 formation.
Suppression of monocyte 85-kDa phospholipase A2 by antisense and effects on endotoxin-induced prostaglandin biosynthesis
Department of Inflammation and Respiratory Pharmacology, SmithKline Beecham Pharmaceuticals, King of Prussia, Pennsylvania 19406.
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