Ganoderma lucidum polysaccharide alleviates Cd toxicity in common carp (Cyprinus carpio): Neuropeptide, growth performance and lipid accumulation.

Cadmium (Cd) is the most common heavy metal and is easily detected in aquatic environments on a global scale. Common carp (Cyprinus carpio) is a common cultural species in aquaculture. This study aimed the polysaccharide from Ganoderma lucidum in ameliorating Cd-induced toxicity in common carp. The study included a blank control group (CK, without Cd and GPL) and LGPL group (2 g/kg LGPL + 0.5 mg/L Cd) and HGPL group (4 g/kg HGPL + 0.5 mg/L Cd). The fish were sampled at 2 and 4 weeks, and bioaccumulation, neurotransmitters, lipid accumulation, and growth performance were measured. Ganoderma lucidum polysaccharide administration can significant protect against Cd toxicity by reducing Cd bioaccumulation in tissues, regulating neurotransmitters, decreasing lipid accumulation, and enhancing growth performance. Our results suggested that administering Ganoderma lucidum polysaccharides can alleviate waterborne Cd toxicity in common carp.

Modeling a new water channel that allows SET9 to dimethylate p53.

SET9, a protein lysine methyltransferase, has been thought to be capable of transferring only one methyl group to target lysine residues. However, some reports have pointed out that SET9 can dimethylate Lys372 of p53 (p53-K372) and Lys4 of histone H3 (H3-K4). In order to understand how p53 can be dimethylated by SET9, we measured the radius of the channel that surrounds p53-K372, first on the basis of the crystal structure of SET9, and we show that the channel is not suitable for water movement. Second, molecular dynamic (MD) simulations were carried out for 204 ns on the crystal structure of SET9. The results show that water leaves the active site of SET9 through a new channel, which is made of G292, A295, Y305 and Y335. In addition, the results of molecular docking and MD simulations indicate that the new water channel continues to remain open when S-adenosyl-L-methionine (AdoMet) or S-adenosyl-L-homocysteine (AdoHcy) is bound to SET9. The changes in the radii of these two channels were measured in the equilibrium phase at the constant temperature of 300 K. The results indicate that the first channel still does not allow water to get into or out of the active site, but the new channel is large enough to allow this water to circulate. Our results indicate that water can be removed from the active site, an essential process for allowing the dimethylation reaction to occur.