Effects of Exogenous Lanthanum Nitrate on the Active Substance Content and Antioxidant Activity of Caterpillar Medicinal Mushroom Cordyceps militaris (Ascomycetes).

Cordyceps militaris is a medicinal and edible mushroom. Researchers often add exogenous substances to the culture medium to increase the active substance content in C. militaris. However, the effect of earth elements on the active substance content in C. militaris and its antioxidant effects have not been reported. In this study, the active substance content in C. militaris treated with lanthanum nitrate was determined using high-performance liquid chromatography and ultraviolet spectrophotometry, and the effect on the antioxidant capacity of C. militaris after lanthanum nitrate spraying was further explored. The results showed that, in the experimental concentration range, the two concentrations of 10 mg/L and 50 mg/L had a significant influence on the active substance content of C. militaris. When the concentration of lanthanum nitrate was 10 mg/L, the synthesis of pentostatin and cordycepin was promoted. When the concentration of lanthanum nitrate was 50 mg/L, it significantly promoted the synthesis of cordycepin, and the ferric-reducing power and DPPH· scavenging rate of C. militaris treated at this concentration were significantly higher than those of the control group. However, lanthanum nitrate had no significant effect on ergosterol synthesis (P > 0.05). Finally, considering that the residual amount of lanthanum in C. militaris and the residual amount of lanthanum in 50 mg/L lanthanum nitrate-treated C. militaris is within the allowable daily intake of 4.2 mg for humans, the optimal concentration of lanthanum nitrate-treated C. militaris is 50 mg/L.

Paternal reprogramming-escape histone H3K4me3 marks located within promoters of RNA splicing genes.

MOTIVATION: Exposure of mouse embryos to atrazine decreased histone tri-methylation at lysine 4 (H3K4me3) and increased expression of alternatively spliced RNA in the third generation. Specificity protein (SP) family motifs were enriched in the promoters of genes encoding differentially expressed alternative transcripts. RESULTS: H3K4me3 chromatin immunoprecipitation sequencing (ChIP-seq) of mouse sperm, preimplantation embryo development and male gonad primordial germ cells (PGCs) were analysed to identify the paternal reprogramming-escape H3K4me3 regions (RERs). In total, 251 RERs selected harbour H3K4me3 marks in sperm, with signals occurring in the paternal genome during early development and in male gonad PGCs, and 179 genes had RERs within 1 kb of transcription start sites (TSSs). These genes were significantly enriched in the gene ontology term 'RNA splicing', and SP1/SP2/SP3 motifs were enriched in RER-associated H3K4me3 peaks. Overall, the H3K4me3 marks within TSSs of RNA splicing genes survived two rounds of the epigenetic reprogramming process. SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.

Ecotoxicological effects of graphene oxide on the protozoan Euglena gracilis.

Potential environmental risks posed by nanomaterials increase with their extensive production and application. As a newly emerging carbon material, graphene oxide (GO) exhibits excellent electrochemical properties and has promising applications in many areas. However, the ecotoxicity of GO to organisms, especially aquatic organisms, remains poorly understood. Accordingly, this study examined the toxicity of GO with protozoa Euglena gracilis as test organism. Growth inhibition test was initially performed to investigate acute toxic effects. Protozoa were subsequently exposed to GO ranging from 0.5 mg L(-1) to 5 mg L(-1) for 10 d. The growth, photosynthetic pigment content, activities of antioxidant enzymes, ultrastructure of the protozoa, as well as the shading effect of GO, were analyzed to determine the mechanism of the toxicity effect. Results showed that the 96 h EC50 value of GO in E. gracilis was 3.76±0.74 mg L(-1). GO at a concentration of 2.5 mg L(-1) exerted significant (P<0.01) adverse effects on the organism. These effects were evidenced by the inhibition of growth and the enhancement of malondialdehyde content and antioxidant enzyme activities. Shading effect and oxidative stress may be responsible for GO toxicity.

Inhibition mechanism of lanthanum ion on the activity of horseradish peroxidase in vitro.

In order to understand the inhibition mechanism of lanthanum ion (La(3+)) on the activity of horseradish peroxidase (HRP), the effects of La(3+) on the activity, electron transfer and conformation of HRP in vitro were investigated by using cyclic voltammetry (CV), atomic force microscopy (AFM), circular dichroism (CD), high performance liquid chromatography (HPLC), matrix-assisted laser desorption/ionization time-of-flight mass spectroscopy (MALDI-TOF/MS) and inductively coupled plasma mass spectrometry (ICP-MS). It was found that La(3+) can combine with the amide groups of the polypeptide chain in HRP molecule, forming the complex of La(3+) and HRP (La-HRP). The formation of the La-HRP complex causes the destruction of the native structure of HRP molecule, leading to the decrease in the non-planarity of the porphyrin ring in the heme group of HRP molecule, and then in the exposure extent of active center, Fe(III) of the porphyrin ring of HRP molecule. Thus, the direct electrochemical and catalytic activities of HRP are decreased. It is a possible inhibition mechanism of La(3+) on the activity of peroxidase.

Inhibition mechanism of Tb(III) on horseradish peroxidase activity.

The inhibition mechanism of Tb(III) on horseradish peroxidase (HRP) in vitro was discussed. The results from MALDI-TOF/MS and X-ray photoelectron spectroscopy (XPS) showed that Tb(III) mainly interacts with the O-containing groups of the amides in the polypeptide chains of the HRP molecules and forms the complex of Tb(III)-HRP, and, in the complex, the molar ratio Tb(III)/HRP is 2 : 1. The results from CD and atomic force microscopy (AFM) indicated that the coordination effect between Tb(III) and HRP can lead to the conformation change in the HRP molecule, in which the contents of alpha-helix and beta-sheet conformation in the peptide of the HRP molecules is decreased, and the content of the random coil conformation is increased. Meanwhile, the coordination effect also leads to the decrease in the content of inter- and intrapeptide-chain H-bonds in the HRP molecules, resulting in the HRP molecular looseness and/or aggregation. Thus, the conformation change in the HRP molecules can significantly decrease the electrochemical reaction of HRP and its electrocatalytic activity for the reduction of H2O2.

One of the possible mechanisms for the inhibition effect of Tb(III) on peroxidase activity in horseradish (Armoracia rusticana) treated with Tb(III).

One of the possible mechanisms for the inhibition effect of Tb(III) on peroxidase activity in horseradish (Armoracia rusticana) treated with Tb(III) was investigated using some biophysical and biochemical methods. Firstly, it was found that a large amount of Tb(III) can be distributed on the cell wall, that some Tb(III) can enter into the horseradish cell, indicating that peroxidase was mainly distributed on cell wall, and thus that Tb(III) would interact with horseradish peroxidase (HRP) in the plant. In addition, peroxidase bioactivity was decreased in the presence of Tb(III). Secondly, a new peroxidase-containing Tb(III) complex (Tb-HRP) was obtained from horseradish after treatment with Tb(III); the molecular mass of Tb-HRP is near 44 kDa and the pI is about 8.80. Thirdly, the electrocatalytic activity of Tb-HRP is much lower than that of HRP obtained from horseradish without treatment with Tb(III). The decrease in the activity of Tb-HRP is due to the destruction (unfolding) of the conformation in Tb-HRP. The planarity of the heme active center in the Tb-HRP molecule was increased and the extent of exposure of Fe(III) in heme was decreased, leading to inhibition of the electron transfer. The microstructure change in Tb-HRP might be the result of the inhibition effect of Tb(III) on peroxidase activity in horseradish.

Subcellular location of horseradish peroxidase in horseradish leaves treated with La(III), Ce(III) and Tb(III).

The agricultural application of rare-earth elements (REEs) would promote REEs inevitably to enter in the environment and then to threaten the environmental safety and human health. Therefore, the distribution of the REEs ion, (141)Ce(III) and effects of La(III), Ce(III) and Tb(III) on the distribution of horseradish peroxidase (HRP) in horseradish mesophyll cells were investigated with electron microscopic radioautography and transmission electron microscopic cytochemistry. It was found for the first time that REEs ions can enter into the mesophyll cells, deposit in both extra and intra-cellular. Compared to the normal condition, after the horseradish leaves treated with La(III) or Tb(III), HRP located on the tonoplast is decreased and HRP is mainly located on the cell wall, while HRP is mainly located on the plasma membrane after the horseradish leaves were treated with Ce(III). This also indicated that REEs ions may regulate the plant growth through changing the distribution of enzymes.

Spectroscopic studies of interactions involving horseradish peroxidase and Tb3+.

The spectroscopic properties of interactions involving horseradish peroxidase (HRP) and Tb3+ in the simulated physiological solution was investigated with some electrochemical and spectroscopic methods, such as cyclic voltammetry (CV), circular dichroism (CD), X-ray photoelectron spectroscopy (XPS) and synchronous fluorescence (SF). It was found that Tb3+ can coordinate with oxygen atoms in carbonyl groups in the peptide chain of HRP, form the complex of Tb3+ and HRP (Tb-HRP), and then lead to the conformation change of HRP. The increase in the random coil content of HRP can disturb the microstructure of the heme active center of HRP, in which the planarity of the porphyrin cycle in the heme group is increased and then the exposure extent of the electrochemical active center is decreased. Thus Tb3+ can inhibit the electrochemical reaction of HRP and its electrocatalytic activity for the reduction of H2O2 at the Au/Cys/GC electrode. The changes in the microstructure of HRP obstructed the electron transfer of Fe(III) in the porphyrin cycle of the heme group, thus HRP catalytic activity is inhibited. The inhibition effect of Tb3+ on HRP catalytic activity is increased with the increasing of Tb3+ concentration. This study would provide some references for better understanding the rare earth elements and heavy metals on peroxidase toxicity in living organisms.

[Spectra studies on the interaction of Mn2+ and poly N-isopropylacrylamide].

The interaction of Mn2+ and poly (N-isopropylacrylamide) (PNIPAAm) was studied by using UV-Vis, FTIR and fluorescence spectroscopic methods. The results indicated that Mn2+ could be bonded to oxygen atoms of carbonyl in PNIPAAm and form the complex of Mn2+ -PNIPAAm. It was found that there existed efficient Förster energy transfer from Mn2+ to PNIPAAm due to the emission spectra of Mn2+ overlapping the excitation spectra of PNIPAAm and that the emission peak of Mn2+ at 561 nm disappeared in Mn2+ -PNIPAAm complex. Therefore the fluorescence intensity at 307 nm was increased by 314%.