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(Journal of Leukocyte Biology. 2001;69:659-665.)
© 2001 by Society for Leukocyte Biology

Signal transduction pathways for activation of extracellular signal-regulated kinase by arachidonic acid in rat neutrophils

Ling-Chu Chang* and Jih-Pyang Wang*,{dagger}

* Department of Education and Research, Taichung Veterans General Hospital, Taichung, Taiwan 407, and
{dagger} Graduate Institute of Pharmaceutical Chemistry, China Medical College, Taichung, Taiwan 404, Republic of China

Correspondence: Jih P. Wang, Department of Education and Research, Taichung Veterans General Hospital, 160 Chung Kang Road, Sec. 3, Taichung, Taiwan 407, Republic of China. E-mail: w1994{at}vghtc.vghtc.gov.tw

Phosphorylation of extracellular signal-regulated kinase (ERK) in response to arachidonic acid (AA) was rapid and transient, peaking at 1 min and disappearing after 3 min, and it was accompanied by an increase in ERK activity in rat neutrophils. We examined the upstream regulation of AA-stimulated ERK activation using one of the following signaling pathway inhibitors to pretreat rat cells: the ERK kinase inhibitor U0126 or PD98059, the Gi/o inhibitor pertussis toxin (PTX), the tyrosine kinase inhibitor genistein, the phosphatidylinositol 3-kinase (PI3K) inhibitor wortmannin or LY294002, the Ca2+ chelator 1,2-bis(O-aminophenoxy) ethane-N,N,N',N'-tetraacetic acid, or the phospholipase C (PLC) inhibitor U73122. All of these inhibitors attenuated AA-induced ERK activation. Activation of ERK was also effectively attenuated by the cyclooxygenase and lipoxygenase inhibitor BW755C and by the leukotriene biosynthesis inhibitor MK886, but the cyclooxygenase inhibitor indomethacin did not attenuate ERK activation. After exposing cells to three distinct protein kinase C (PKC) inhibitors, we found that Gö6976 significantly attenuated ERK phosphorylation but potentiated ERK activity. Neither Gö6983 nor GF109203X affected AA-induced responses. These data suggest that the lipoxygenase metabolite(s) produced mediates AA-stimulated ERK activation and that this effect is upstream regulated by PT-sensitive G protein, nonreceptor tyrosine kinase, PI3K, and PLC/Ca2+ signaling pathways in rat neutrophils.

Key Words: phosphorylation • kinase activity • protein kinases • lipoxygenase • phosphatidylinositol 3-kinase • phospholipase C




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