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J. Biol. Chem., Vol. 266, Issue 4, 2647-2651, Feb, 1991
RM Crowl, TJ Stoller, RR Conroy and CR Stoner
Serum levels of phospholipase A2 (PLA2) activity have been shown to be
elevated in cases of septic shock and rheumatoid arthritis. The cellular
origin of serum PLA2, however, is not known. In this report, we demonstrate
that human group II PLA2 expression and secretion are induced in hepatoma
cells (HepG2) following treatment with interleukin- 6 (IL-6), tumor
necrosis factor (TNF), and interleukin-1 (IL-1). Of the three cytokines,
IL-6 is the most potent. Significant synergy is observed between IL-6 and
IL-1 and between IL-6 and TNF, but not between IL-1 and TNF. PLA2 induction
does not occur in human YT cells, which are known to have receptors for
both IL-1 and IL-6, indicating that the regulatory mechanism involved is
cell type-specific. The results of RNA blot analysis indicate that the PLA2
gene is regulated in HepG2 cells at the pretranslational level. Induction
of PLA2 synthesis in HepG2 cells in response to these cytokines resembles
the induction of the acute phase plasma proteins which are synthesized in
cultured hepatocytes and hepatoma cells following exposure to the same
cytokines and in liver in response to inflammation and infection. In
addition, a putative IL-6-responsive element, which is homologous to a
similar element found in several acute phase genes, is present in the
5'-promoter-proximal region of the PLA2 gene. These results suggest that
serum PLA2 is synthesized in and secreted from liver cells in response to
inflammatory stimuli, mediated primarily by IL-6, and therefore should be
classified as an acute phase protein.
Induction of phospholipase A2 gene expression in human hepatoma cells by mediators of the acute phase response
Department of Molecular Genetics, Hoffmann-La Roche Inc., Nutley, New Jersey 07110.
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