Overuse of acetochlor pollutes soil and rivers, causing threats to the ecosystem. Studies found that acetochlor exposure could damage multiple organs and tissues in fish and mammal. Tea polyphenols (TP), a natural antioxidant that extracted from tea, has been widely used in food and feed additions. However, the mechanism by which acetochlor causes tissue damage is unclear, and its mitigating agent has yet to be developed. Therefore, we established acetochlor exposure and TP mitigation models by treating Ctenopharyngodon idellus kidney (CIK) cells with 20 μM acetochlor and/or 2.5 μg/mL TP for 24 h, and detected the programmed cell death and its related pathways. The results showed that acetochlor exposure modified antioxidant enzyme activities, induced oxidative stress, resulted in the decline of MMP and ATP levels, enhanced glycolysis and lactate accumulation, and triggered apoptosis and necroptosis in CIK cells. However, TP could inhibit CYP450s expression, activate Nrf2 pathway, enhance antioxidant capacity, further effectively alleviate acetochlor-induced CIK cell death. Overall, the present study proved that acetochlor exposure triggered mitochondrial damage and lactate accumulation-mediated apoptosis and necroptosis through CYP450s/ROS/MAPK/NF-κB pathway. Furthermore, TP could alleviate effectively cell death through relieving oxidative stress and lightening Warburg-like effect.
Cao Liwei,Su Sisi,Regenstein Joe M.,Xiong Shanbai,Liu Ru
The role of Ca 2+ in gelation of myosin extracted from silver carp ( Hypophthalmichthys molitrix ) was investigated. Compared with the control, myosin with CaCl 2 showed higher turbidity and larger particle size, indicating that CaCl 2 contributed to myosin aggregation. Addition of CaCl 2 decreased the myosin thermostability and promoted the unfolding of myosin α-helical structure during heating. Moreover, CaCl 2 could increase surface hydrophobicity at low temperatures (20–40 °C) and promoted hydrophobic interactions. Meanwhile, it decreased the temperature of disulfide bond formation by about 10 °C. Addition of 10–40 mM CaCl 2 favored activation of the Ca 2+ -ATPase activity at 20 to 30 °C, but not obvious with elevated temperatures. Ca 2+ -ATPase activity of myosin was undetectable when heated above 60 °C because of severe structural damage of myosin heads. G’ at both the first and second peaks increased with increasing CaCl 2 concentration. Therefore, CaCl 2 was beneficial for gelation of myosin by inducing the unfolding of myosin and enhancing disulfide bonds along with hydrophobic interactions between neighboring myosin molecules.
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