Cycloheximide-induced cPLA(2) activation is via the MKP-1 down-regulation and ERK activation.

Abstract:

:Extracellular signal-regulated kinase (ERK)-dependent phosphorylation is an important regulator for cytosolic phospholipase A(2) (cPLA(2)). 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 NH(2)-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).

journal_name

Cell Signal

journal_title

Cellular signalling

authors

Lin WW,Hsu YW

doi

10.1016/s0898-6568(00)00090-5

subject

Has Abstract

pub_date

2000-07-01 00:00:00

pages

457-61

issue

7

eissn

0898-6568

issn

1873-3913

pii

S0898-6568(00)00090-5

journal_volume

12

pub_type

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