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KMID : 1161520050090030173
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Animal Cells and Systems
2005 Volume.9 No. 3 p.173 ~ p.179
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Protein Kinase a functions as a negative regulator of c-jun n-terminal kinase but not of p38 mitogen-activated protein Kinase in PC12 cells
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Hur Kyu-Chung
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Abstract
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Cyclic?AMP?dependent protein kinase (PKA) seems to function as a negative regulator of the c?Jun NH2?terminal kinase (JNK) signaling pathway. We demonstrate here that the activity of the PKA catalytic subunit (PKAc) is reduced in apoptotic PC12 pheochromocytoma cells. Apoptotic progress was inhibited by dibutyryl cyclic AMP (dbcAMP), an analog of cAMP. The rescue by dbcAMP was attributable to inhibition of the JNK but not of the p38 signaling pathway, due to the induction of PKA activity. JNK was present in immunocomplexes of PKAc, and PKAc phosphorylated JNK in vitro. Presence of p38 kinase, however, was not prominent in immunocomplexes of PKAc. Our data suggest that JNK is a target point of negative regulation by PKAc in the JNK signaling pathway.
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KEYWORD
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apoptosis, cAMP, cAMP-dependent protein kinase A (PKA), JNK, p38 kinase
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