Signaling of reactive oxygen species in PTTH-stimulated ecdysteroidogenesis in prothoracic glands of the silkworm, Bombyx mori
| Autor: | Shi-Hong Gu, Yun-Chih Hsieh, Pei-Ling Lin |
|---|---|
| Rok vydání: | 2013 |
| Předmět: |
MAPK/ERK pathway
Physiology Oxidative phosphorylation Antimycin A Biology AMP-Activated Protein Kinases chemistry.chemical_compound Animals Phosphorylation Extracellular Signal-Regulated MAP Kinases Protein kinase C chemistry.chemical_classification Reactive oxygen species Phospholipase C AMPK Ecdysteroids Bombyx Cell biology Biochemistry chemistry Insect Science Insect Hormones Larva Type C Phospholipases Insect Proteins Calcium Reactive Oxygen Species Oxidation-Reduction Signal Transduction |
| Zdroj: | Journal of insect physiology. 63 |
| ISSN: | 1879-1611 |
| Popis: | Our 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 1 mM of H 2 O 2 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. |
| Databáze: | OpenAIRE |
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