Expression of protein kinase C in relation to the embryonic diapause process in the silkworm, Bombyx mori

In the present study, we investigated the expression of protein kinase C (PKC) signaling during the embryonic diapause process of Bombyx mori. PKC activity, determined using an antibody to phosphorylated substrates of PKC, was found to be significantly higher in developing eggs as compared to that of diapause eggs. In eggs whose diapause initiation was prevented by HCl, non-diapause eggs, and eggs in which diapause had been terminated by chilling of diapausing eggs at 5 °C for 70 days and then were transferred to 25 °C, PKC-dependent phosphorylation levels of multiple proteins showed dramatic stage-dependent increases compared to those of diapause eggs. Higher protein levels of PKC were also detected in developing eggs as compared to those of diapause eggs. Determination of PKC enzymatic activity during the middle embryonic stage showed higher PKC activity in developing eggs compared to diapause eggs, thus further confirming differential regulation of PKC signaling during the embryonic diapause process. Examination of temporal changes in mRNA expression levels of classical PKC (cPKC) and atypical PKC (aPKC) showed no difference between diapause and HCl-treated eggs. These results demonstrated that differential expressions of PKC signaling between diapause and developing eggs are related to the embryonic diapause process of B. mori.