Cloning and Characterization of the Caspase Family Member BmDronc from Bombyx mori (Lepidoptera: Bombycidae) Embryo Cells
2013
Zhang, Jin-Ye | Xu, Wei | Pan, Chun | Yi, Hua-Shan | Hu, Yan-Fen | Song, Juan | Pan, Min-Hui | Lü, Cheng
Caspases are a family of cysteinyl aspartate proteinases known for their essential roles in the regulation of apoptosis. To date, ≈20 caspases have been identified, although few have been cloned and characterized in Bombyx mori (L.). Two caspase-9 variants from the B. mori embryo cell line (BmE), designated BmDroncL and BmDroncS, were cloned. BmDroncL has three classic domains: a caspase recruitment domain and large and small subunits, and is a homologue of Drosophila Dronc, human caspase-9, Aedes Dronc, and fish caspase-9, whereas BmDroncS lacks the large subunit. Instantaneous expression of BmDroncL caused typical apoptosis in Sf-9 cells. Moreover, BmDronc gene expression increased markedly during the silkworm metamorphosis at the larva-pupa and pupa-moth stages, which suggested that BmDronc plays a crucial role during B. mori metamorphosis.
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