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Plays a Central Role in Activation of the p42/44 Mitogen-Activated Protein Kinase by Endotoxin in Alveolar Macrophages1
Department of Medicine, University of Iowa College of Medicine and Veterans Administration Medical Center, Iowa City, IA
Human alveolar macrophages respond to endotoxin (LPS) by activation
of a number of mitogen-activated protein kinase pathways, including the
p42/44 (extracellular signal-related kinase (ERK)) kinase pathway. In
this study, we evaluated the role of the atypical protein kinase C
(PKC) isoform, PKC 
, in LPS-induced activation of the ERK kinase
pathway. Kinase activity assays showed that LPS activates PKC ,
mitogen-activated protein/ERK kinase (MEK, the upstream activator of
ERK), and ERK. LPS did not activate Raf-1, the classic activator of
MEK. Pseudosubstrate-specific peptides with attached myristic acid are
cell permeable and can be used to block the activity of specific PKC
isoforms in vivo. We found that a peptide specific for PKC
partially blocked activation of both MEK and ERK by LPS. We also found
that this peptide blocked in vivo phosphorylation of MEK after LPS
treatment. In addition, we found that LPS caused PKC to bind to MEK
in vivo. These observations suggest that MEK is an LPS-directed target
of PKC . PKC has been shown in other systems to be
phosphorylated by phosphatidylinositol (PI) 3-kinase-dependent kinase.
We found that LPS activates PI 3-kinase and causes the formation of a
PKC /PI 3-kinase-dependent kinase complex. These data implicate the
PI 3-kinase pathway as an integral part of the LPS-induced PKC
activation. Taken as a whole, these studies suggest that LPS activates
ERK kinase, in part, through activation of an atypical PKC isoform, PKC
.
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