Examination of the signal transduction pathways leading to activation of extracellular signal‐regulated kinase by formyl‐methionyl‐leucyl‐phenylalanine in rat neutrophils

FEBS Letters

Chang, Ling-Chu¹  Wang, Jih-Pyang¹ 

[1] Department of Education and Research, Taichung Veterans General Hospital, Taichung 407, Taiwan, ROC

关键词: Neutrophil;    Extracellular signal-regulated kinase;    Tyrosine kinase;    Protein kinase C;    Intracellular calcium;    Phosphatidylinositol 3-kinase;   

DOI  :  10.1016/S0014-5793(99)00717-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The signaling pathways leading to extracellular signal-regulated kinase (ERK) activation in formyl-methionyl-leucyl-phenylalanine (fMLP)-stimulated rat neutrophils were examined. fMLP-stimulated ERK activation based on immunoblot analysis with antibodies against the phosphorylation form of ERK was attenuated by the pretreatment of cells with pertussis toxin but not with a dual cyclo-oxygenase/lipoxygenase inhibitor BW755C. Exposure of cells to the tyrosine kinase inhibitor genistein, phosphatidylinositol 3-kinase (PI3K) inhibitors wortmannin and LY294002, or protein kinase C (PKC) inhibitors Gö6976, Gö6983, and GF109203X inhibited fMLP-stimulated ERK phosphorylation in a concentration-dependent manner. In addition, both the phospholipase C (PLC) inhibitor U73122 and the Ca²⁺ chelator BAPTA attenuated ERK activation. These results indicate that G_i/o protein, tyrosine kinase, PI3K, PKC, and PLC/Ca²⁺, but not arachidonate metabolites, act upstream of fMLP-stimulated ERK activation.

【 授权许可】

Unknown