Title : Interleukin-1 stimulates Jun N-terminal/stress-activated protein kinase by an arachidonate-dependent mechanism in mesangial cells.

Pub. Date : 1999 May

PMID : 10231436






5 Functional Relationships(s)
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1 Free arachidonic acid (AA) activates several protein kinases, and because IL-1 rapidly stimulates phospholipase A2 (PLA2) activity release AA, IL-1-induced activation of JNK1/SAPK may be mediated by AA release. Arachidonic Acid mitogen-activated protein kinase 8 Homo sapiens
2 Pretreatment of MCs with aristolochic acid, a PLA2 inhibitor, concordantly reduced IL-1-regulated [3H]AA release and JNK1/SAPK activity, suggesting that cytosolic AA in part mediates IL-1-induced JNK1/SAPK activation. aristolochic acid I mitogen-activated protein kinase 8 Homo sapiens
3 Pretreatment of MCs with aristolochic acid, a PLA2 inhibitor, concordantly reduced IL-1-regulated [3H]AA release and JNK1/SAPK activity, suggesting that cytosolic AA in part mediates IL-1-induced JNK1/SAPK activation. aristolochic acid I mitogen-activated protein kinase 8 Homo sapiens
4 This effect was AA specific, as only AA and its precursor linoleic acid stimulated JNK1/SAPK activity. Linoleic Acid mitogen-activated protein kinase 8 Homo sapiens
5 Furthermore, stimulation of MCs with the exogenous cyclooxygenase-, lipoxygenase-, phosphodiesterase-, and epoxygenase-derived arachidonate metabolites, in contrast to AA itself, did not activate JNK1/SAPK. Arachidonic Acid mitogen-activated protein kinase 8 Homo sapiens