PubMed:24548611 JSONTXT

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In the present study, we further investigated the mechanism of ROS production and the signaling pathway mediated by ROS. PTTH-stimulated ROS production was markedly attenuated in a Ca(2+)-free medium. The phospholipase C (PLC) inhibitor, U73122, greatly inhibited PTTH-stimulated ROS production, indicating the involvement of Ca(2+) and PLC. When the PGs were treated with agents that directly elevate the intracellular Ca(2+) concentration (either A23187, or the protein kinase C (PKC) activator, phorbol 12-myristate acetate (PMA)), a great increase in ROS production was observed. We further investigated the action mechanism of PTTH-stimulated ROS signaling. Results showed that in the presence of either an antioxidant (N-acetylcysteine, NAC), or the mitochondrial oxidative phosphorylation inhibitors (rotenone, antimycin A, the uncoupler carbonyl cyanide p-trifluoromethoxyphenylhydrazone (FCCP), and diphenyleneiodonium (DPI)), PTTH-regulated phosphorylation of ERK, 4E-BP, and AMPK was blocked. Treatment with 1mM of H2O2 alone activated the phosphorylation of ERK and 4E-BP, and inhibited AMPK phosphorylation. From these results, we conclude that PTTH-stimulated ROS signaling is Ca(2+)- and PLC-dependent and that ROS signaling appears to lie upstream of the phosphorylation of ERK, 4E-BP, and AMPK."}

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{"project":"PubmedHPO","denotations":[{"id":"T1","span":{"begin":1104,"end":1117},"obj":"HP_0001427"}],"text":"Signaling of reactive oxygen species in PTTH-stimulated ecdysteroidogenesis in prothoracic glands of the silkworm, Bombyx mori.\nOur previous study demonstrated that mitochondria-derived reactive oxygen species (ROS) generation is involved in prothoracicotropic hormone (PTTH)-stimulated ecdysteroidogenesis in Bombyx mori prothoracic glands (PGs). In the present study, we further investigated the mechanism of ROS production and the signaling pathway mediated by ROS. PTTH-stimulated ROS production was markedly attenuated in a Ca(2+)-free medium. The phospholipase C (PLC) inhibitor, U73122, greatly inhibited PTTH-stimulated ROS production, indicating the involvement of Ca(2+) and PLC. When the PGs were treated with agents that directly elevate the intracellular Ca(2+) concentration (either A23187, or the protein kinase C (PKC) activator, phorbol 12-myristate acetate (PMA)), a great increase in ROS production was observed. We further investigated the action mechanism of PTTH-stimulated ROS signaling. Results showed that in the presence of either an antioxidant (N-acetylcysteine, NAC), or the mitochondrial oxidative phosphorylation inhibitors (rotenone, antimycin A, the uncoupler carbonyl cyanide p-trifluoromethoxyphenylhydrazone (FCCP), and diphenyleneiodonium (DPI)), PTTH-regulated phosphorylation of ERK, 4E-BP, and AMPK was blocked. Treatment with 1mM of H2O2 alone activated the phosphorylation of ERK and 4E-BP, and inhibited AMPK phosphorylation. From these results, we conclude that PTTH-stimulated ROS signaling is Ca(2+)- and PLC-dependent and that ROS signaling appears to lie upstream of the phosphorylation of ERK, 4E-BP, and AMPK."}

{"project":"Allie","denotations":[{"id":"SS1_24548611_1_0","span":{"begin":186,"end":209},"obj":"expanded"},{"id":"SS2_24548611_1_0","span":{"begin":211,"end":214},"obj":"abbr"},{"id":"SS1_24548611_1_1","span":{"begin":242,"end":268},"obj":"expanded"},{"id":"SS2_24548611_1_1","span":{"begin":270,"end":274},"obj":"abbr"},{"id":"SS1_24548611_1_2","span":{"begin":322,"end":340},"obj":"expanded"},{"id":"SS2_24548611_1_2","span":{"begin":342,"end":345},"obj":"abbr"},{"id":"SS1_24548611_4_0","span":{"begin":553,"end":568},"obj":"expanded"},{"id":"SS2_24548611_4_0","span":{"begin":570,"end":573},"obj":"abbr"},{"id":"SS1_24548611_5_0","span":{"begin":812,"end":828},"obj":"expanded"},{"id":"SS2_24548611_5_0","span":{"begin":830,"end":833},"obj":"abbr"},{"id":"SS1_24548611_5_1","span":{"begin":846,"end":874},"obj":"expanded"},{"id":"SS2_24548611_5_1","span":{"begin":876,"end":879},"obj":"abbr"},{"id":"SS1_24548611_7_0","span":{"begin":1256,"end":1275},"obj":"expanded"},{"id":"SS2_24548611_7_0","span":{"begin":1277,"end":1280},"obj":"abbr"}],"relations":[{"id":"AE1_24548611_1_0","pred":"abbreviatedTo","subj":"SS1_24548611_1_0","obj":"SS2_24548611_1_0"},{"id":"AE1_24548611_1_1","pred":"abbreviatedTo","subj":"SS1_24548611_1_1","obj":"SS2_24548611_1_1"},{"id":"AE1_24548611_1_2","pred":"abbreviatedTo","subj":"SS1_24548611_1_2","obj":"SS2_24548611_1_2"},{"id":"AE1_24548611_4_0","pred":"abbreviatedTo","subj":"SS1_24548611_4_0","obj":"SS2_24548611_4_0"},{"id":"AE1_24548611_5_0","pred":"abbreviatedTo","subj":"SS1_24548611_5_0","obj":"SS2_24548611_5_0"},{"id":"AE1_24548611_5_1","pred":"abbreviatedTo","subj":"SS1_24548611_5_1","obj":"SS2_24548611_5_1"},{"id":"AE1_24548611_7_0","pred":"abbreviatedTo","subj":"SS1_24548611_7_0","obj":"SS2_24548611_7_0"}],"text":"Signaling of reactive oxygen species in PTTH-stimulated ecdysteroidogenesis in prothoracic glands of the silkworm, Bombyx mori.\nOur previous study demonstrated that mitochondria-derived reactive oxygen species (ROS) generation is involved in prothoracicotropic hormone (PTTH)-stimulated ecdysteroidogenesis in Bombyx mori prothoracic glands (PGs). In the present study, we further investigated the mechanism of ROS production and the signaling pathway mediated by ROS. PTTH-stimulated ROS production was markedly attenuated in a Ca(2+)-free medium. The phospholipase C (PLC) inhibitor, U73122, greatly inhibited PTTH-stimulated ROS production, indicating the involvement of Ca(2+) and PLC. When the PGs were treated with agents that directly elevate the intracellular Ca(2+) concentration (either A23187, or the protein kinase C (PKC) activator, phorbol 12-myristate acetate (PMA)), a great increase in ROS production was observed. We further investigated the action mechanism of PTTH-stimulated ROS signaling. Results showed that in the presence of either an antioxidant (N-acetylcysteine, NAC), or the mitochondrial oxidative phosphorylation inhibitors (rotenone, antimycin A, the uncoupler carbonyl cyanide p-trifluoromethoxyphenylhydrazone (FCCP), and diphenyleneiodonium (DPI)), PTTH-regulated phosphorylation of ERK, 4E-BP, and AMPK was blocked. Treatment with 1mM of H2O2 alone activated the phosphorylation of ERK and 4E-BP, and inhibited AMPK phosphorylation. From these results, we conclude that PTTH-stimulated ROS signaling is Ca(2+)- and PLC-dependent and that ROS signaling appears to lie upstream of the phosphorylation of ERK, 4E-BP, and AMPK."}