Cycloheximide-induced cPLA2 activation is via the MKP-1 down-regulation and ERK activation
Journal
Cellular Signalling
Journal Volume
12
Journal Issue
7
Pages
457-461
Date Issued
2000
Author(s)
Hsu Y.-W.
Abstract
Extracellular signal-regulated kinase (ERK)-dependent phosphorylation is an important regulator for cytosolic phospholipase A2 (cPLA2). In this study, we found that the protein synthesis inhibitor cycloheximide can potentiate thapsigargin-induced arachidonic acid (AA) release concomitant with ERK phosphorylation from murine RAW 264.7 macrophages. The cycloheximide effect is not due to the activation of p38 mitogen-activated protein kinase (MAPK) nor c-Jun NH2-terminal kinase (JNK), because the activator of both MAPKs anisomycin does not elicit AA release. Cycloheximide effect is additive to the tyrosine phosphatase inhibitor orthovanadate since these two stimuli induced sustained ERK activation respectively through inhibition of the translation and activity of MAPK phosphatase-1 (MKP-1). (C) 2000 Elsevier Science Inc.
SDGs
Type
journal article