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J Biol Chem, Vol. 274, Issue 9, 5469-5473, February 26, 1999
From the Departments of Biochemistry and
§ Medicine/Infectious Disease, Wake Forest University
Medical Center, Winston-Salem, North Carolina 27157-1016
Acetyl-CoA:1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine
acetyltransferase, along with phospholipase A2, is a key
regulator of platelet-activating factor biosynthesis via the remodeling pathway. We have now obtained evidence in human neutrophils indicating that this enzyme is regulated by a specific member of the
mitogen-activated protein kinases, namely the p38 kinase. We earlier
demonstrated that tumor necrosis factor-
(TNF-) as well as
N-formyl-methionyl-leucyl-phenylalanine treatment leads to
increased phosphorylation and activation of p38 kinase in human
neutrophils. Strikingly, in the present study these stimuli increased
the catalytic activity of acetyltransferase up to 3-fold, whereas
4-phorbol 12-myristate 13-acetate, which activates the
extracellular-regulated kinases (ERKs) but not p38 kinase, had no
effect. Furthermore, a selective inhibitor of p38 kinase, SB 203580, was able to abolish the TNF-- and
N-formyl-methionyl-leucyl-phenylalanine-induced activation
of acetyltransferase. The same effect was not observed in the presence
of an inhibitor that blocked ERK activation (PD 98059). Complementing
the findings in intact cells, we have shown that recombinant, activated
p38 kinase added to microsomes in the presence of Mg2+ and
ATP increased acetyltransferase activity to the same degree as in
microsomes obtained from TNF--stimulated cells. No activation of
acetyltransferase occurred upon treatment of microsomes with either recombinant, activated ERK-1 or ERK-2. Finally, the increases in
acetyltransferase activity induced by TNF- could be ablated by
treating the microsomes with alkaline phosphatase. Thus
acetyltransferase appears to be a downstream target for p38
kinase but not ERKs. These data from whole cells as well as cell-free
systems fit a model wherein stimulus-induced acetyltransferase
activation is mediated by a phosphorylation event catalyzed directly by
p38 kinase.
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