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作者Lin, J. L.;Lin, P. L.;Gu, S. H.
出版日期2009
著作名稱Phosphorylation of glycogen synthase kinase 3β in relation to diapause processing in the silkworm, Bombyx mori.
刊名Journal of Insect Physiology
55
6
頁數593-598
被收錄索引SCI
關鍵字Bombyx mori; ERK phosphorylation; GSK-3
摘要Glycogen synthase kinase 3 (GSK-3) is a multifunctional protein kinase that plays important role in regulating both glycogen synthesis and protein synthesis. In the present study, we investigated GSK-3β phosphorylation of the silkworm eggs by immuno-blotting with a conserved phospho-specific antibody to GSK-3β. Results showed that the temporal changes in GSK-3β phosphorylation are closely related to changes in glycogen levels previously reported by other researchers. In diapause eggs an abrupt decrease in phosphorylation of GSK-3β was found with the onset of diapause and the phosphorylation level of GSK-3β reached a minimum level within 1 week after oviposition. However, when diapause eggs were incubated at 25°C for 15 days and then transferred to 5°C, a greatly increased GSK-3β phosphorylation was observed 5 days after transferring to 5°C and maintained at high levels throughout the chilling period. In both non-diapause eggs and the eggs whose diapause initiation was avoided by HCl, the levels in the phosphorylation of GSK-3β appeared to maintain relatively high for several days and then greatly decreased 2 or 3 days before hatching. Moreover, GSK-3β phosphorylation increased dramatically when dechorionated eggs were incubated in medium. The addition of the mitogen-activated protein kinases (MAPK)/extracellular signal-regulated kinases (ERK) kinases (MEK) inhibitor, U0126, did not inhibit GSK-3β phosphorylation in dechorionated eggs, although U0126 inhibit ERK phosphorylation dose-dependently. This result showed that ERK phosphorylation is not upstream signaling for GSK-3β phosphorylation and that both may be two distinct signaling pathways that are involved in diapause processing in B. mori eggs.
系統號NO000002816

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