PM15 Biomarkers
Exhibit Hall
8:00 AM - Monday
(PM237) Profiling proteins of the midge, Chirnomus riparius Meigen, related to cadmium toxicity.
Yoo, Dong-Hun1, Son, Jino1, Park, Byeoung-Soo2, Kim, Mihyang2, Lee, Sung-Eun2, Cho, Kijong1, 1 Korea University, Seoul, South Korea2 Seoul National University, Seoul, South Korea
ABSTRACT- Among the non-essential heavy metals, cadmium is one of the most hazardous elements in the aquatic environment. Toxic effects of individual heavy metal on aquatic insects have been reported frequently, but little information exists concerning protein changes. The effect of cadmium on larvae of the midge Chironomus riparius Meigen was tested in water-only exposure system. After static contamination of third-instar larvae for 48 h, LC10 and LC50 values were 115.8 and 444.8 mg/L, respectively. The survivors after exposure at the experimental conditions were prepared for the further proteomic studies. Using two-dimensional electrophoresis, proteins with differences in expression in the whole extracts of Cd-treated larvae were compared to non Cd-treated ones as control. The proteins with different expression levels were identified using MALDI-TOF analysis. Fourteen proteins were disappeared and 5 proteins such as cytochrome P450 and aryl sulfatase A were newly identified. Furthermore, 4 proteins were decreased and 3 proteins containing caltalase and HSC70 were increased after exposure to cadmium. According to the proteomic results cadmium primarily caused damages to transporter proteins in the cell membrane, increasing the permeability of the cells. Cytochrome P450 aromatase, aryl sulfastase A and catalase were enhanced may play important roles in the detoxification of cadmium toxicity in the midge.
Key words: cadmium, Chironomus riparius, proteomics, protein identification