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

机译:环己酰亚胺诱导的cPLA(2)激活是通过MKP-1下调和ERK激活

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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 rmacrophages. 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. All rights reserved. [References: 28]
机译:细胞外信号调节激酶(ERK)依赖的磷酸化是胞质磷脂酶A(2)(cPLA(2))的重要调节剂。从鼠RAW 264.7巨噬细胞释放伴随ERK磷酸化的蛋白。环己酰亚胺的作用不是由于p38丝裂原活化蛋白激酶(MAPK)的激活,也不是c-Jun NH2末端激酶(JNK)的激活,因为这两种MAPK茴香霉素的激活剂均不会引起AA释放。由于这两种刺激分别通过抑制MAPK磷酸酶-1(MKP-1)的翻译和活性而诱导了持续的ERK活化,因此环己酰亚胺的作用与酪氨酸磷酸酶抑制剂原钒酸盐相加。 (C)2000 Elsevier Science Inc.保留所有权利。 [参考:28]

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