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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

Animal Cells and Systems 2005년 9권 3호 p.173 ~ 179
허규정,
소속 상세정보
허규정 ( Hur Kyu-Chung ) - Ewha Womans University Department of Biology

Abstract


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.

키워드

apoptosis; cAMP; cAMP-dependent protein kinase A (PKA); JNK; p38 kinase

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