Abstract
We investi-gated whether JNK is activated by interleukin-1β (IL-lβ) in mesangial cells. We performed in-gel kinase assays with His-c-jun-(1-79), which contains the amino-terminal activation domain of c-jun and a mutant His-c-jun in which Ser-63 and Ser-73 of His-c-jun were mutated to Ala as the substrates. JNK1 (p45) and JNK2 (p54) isoforms phosphorylated His-c-jun in mesangial cells. IL-1β produced a time- and concentration-dependent increase in JNK activity. IL-1β did not phosphorylate the mutant, His-c-jun. The IL-1β-activated JNK activity was independent of serum and suppressed by neither tyrosine kinase inhibitors nor protein kinase C inhibitors. JNK was also stimulated by anisomycin and okadaic acid but not by phorbol 12-myristate 13-acetate. The protein synthesis inhibitors and okadaic acid potentiated the IL-1β-induced JNK activity. Together, these studies indicate that the novel JNK group of protein kinases may play an important role in the signal transduction pathway initiated by proinflammatory cytokines, such as IL-1β in mesangial cells.
Original language | English |
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Pages (from-to) | F634-F641 |
Journal | American Journal of Physiology |
Volume | 270 |
Issue number | 4 PART 2 |
State | Published - 1996 |
Keywords
- Phosphorylation
- Protein kinase c
- Tyrosine kinase mesangial cell