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Blood, 1 October 2000, Vol. 96, No. 7, pp. 2592-2598
PHAGOCYTES
Lipopolysaccharide induces Jun N-terminal kinase activation in
macrophages by a novel Cdc42/Rac-independent pathway involving
sequential activation of protein kinase C  and
phosphatidylcholine-dependent phospholipase C
Katarzyna J. Procyk,
Maria
Rita Rippo,
Roberto Testi,
Fred Hofmann,
Peter J. Parker, and
Manuela Baccarini
From the Section of Cell Biology and Microbiology,
Institute of Microbiology and Genetics, Vienna Biocenter, Vienna,
Austria; Department of Experimental Medicine and Biochemical Sciences,
University of Rome "Tor Vergata," Rome, Italy; Institut
für Pharmakologie und Toxikologie, Freiburg, Germany;
Protein Phosphorylation Laboratory, Imperial Cancer Research Fund,
London, United Kingdom.
The activation of kinases of the mitogen-activated protein kinase
superfamily initiated by lipopolysaccharide (LPS) plays an important
role in transducing inflammatory signals. The pathway leading to the
induction of stress-activated protein kinases in macrophages stimulated
with LPS was investigated. The activation of Jun N-terminal kinases
(JNK) by LPS is herbimycin sensitive. Using specific
inhibitors, it was shown that the pathway involves the
activation of phosphoinositide 3-kinase (PI 3-K). However, in contrast
to previous reports, the small GTPases Cdc42 and Rac are not
required downstream of PI 3-K for JNK activation. Instead, the
phosphoinositides produced by PI 3-K stimulate protein kinase C (PKC)
 activation through PDK1. In turn, activation of this atypical PKC
leads to the stimulation of phosphatidylcholine phospholipase C
(PC-PLC) and acidic sphingomyelinase (ASMase). It is therefore proposed that PKC regulates the PC-PLC/ASMase pathway, and it is
hypothesized that the resultant ceramide accumulation mediates the
activation of the SEK/JNK module by LPS.
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