Curcumin-supplemented diets increase superoxide dismutase activity and mean lifespan in Drosophila.

Curcumin is a polyphenolic bioactive compound in turmeric. We examined if antioxidant effects of curcumin are associated with lifespan extension in Drosophila. In this experiment, females and males of Drosophila were fed diets either containing no curcumin (C0) or supplemented with curcumin at 0.5 (C1) and 1.0 (C2) mg/g of diet. The levels of malondialdehyde (MDA), enzyme activity of superoxide dismutase (SOD), and expression of seven age-related genes in females and males were analyzed. We found that C1 and C2 increased mean lifespan by 6.2 % and 25.8 % in females, and by 15.5 % and 12.6 % in males, respectively. Meanwhile, C1 and C2 significantly decreased MDA levels and increased SOD activity in both genders. Diets C1 in females and C2 in males are effective in extending mean lifespan and improving levels of two physiological and biochemical measures related to aging in Drosophila. Lifespan extension of curcumin in Drosophila was associated with the up-regulation of Mn-SOD and CuZn-SOD genes, and the down-regulation of dInR, ATTD, Def, CecB, and DptB genes. The present results suggest that curcumin increases mean lifespan of Drosophila via regulating gene expression of the key enzyme SOD and reducing accumulation of MDA and lipid peroxidation. This study provided new insights for understanding the anti-aging mechanism of curcumin in Drosophila.

Molecular identification of cDNA, immunolocalization, and expression of a putative odorant-binding protein from an Asian honey bee, Apis cerana cerana.

An odorant-binding protein cDNA (Acer-ASP2) was cloned and characterized from antennae of adult workers of an Asian honey bee, Apis cerana cerana F. (Hymenoptera: Apidae). The full-length open reading frame of Acer-ASP2 cDNA was 429 bp, encoding 142 amino acids. Protein signature analyses revealed that it contained six conserved cysteines with an N-terminal signal sequence of 19 amino acids. The deduced protein sequence shares high homology with Amel-ASP2 from the honey bee, Apis mellifera L., and low similarity with odorant-binding proteins from other species of insects. Immunocytochemical localization showed that Acer-ASP2 was concentrated in the lymph of olfactory sensilla, such as sensilla placodea and sensilla trichodea A. Real-time polymerase chain reaction of Acer-ASP2 transcripts showed that Acer-ASP2 was expressed on antennae but not in other general anatomical regions of the body. Temporally, Acer-ASP2 was expressed at a relatively high level in adults during two periods (9 and 27 vs. 1, 15, and 30 days). This timing is correlated with the production of beeswax and searching behavior for nectar/pollen, respectively. Thus, Acer-ASP2 is a species-specific gene that we propose to be involved in the acquisition of odorant molecules from nectar, pollen, and other general odorant sources.