Influence of Multiwalled Carbon Nanotubes Dispersed in Natural Organic Matter on Speciation and Bioavailability of Copper

The dispersion of multiwalled carbon nanotubes (MWNTs) by natural organic matter (NOM) may influence the bioavailability of MWNTs and other contaminants. The speciation and bioavailability of copper (Cu) in MWNTs-associated NOM was studied using Daphnia magna. Cu titration data indicated that the binding affinity of Cu for MWNTs-associated NOM was lower than that for NOM alone. The free Cu2+ ion activity was increased even by the addition of a low nontoxic concentration of 1.0 mg/L MWNTs. The 96 h LC50 of MWNTs was determined to be 2.48 mg/L. The Fourier transform infrared (FTIR) spectra results showed clearly different features in Cu spiked between NOM and MWNTs-associated NOM, indicating that the interruption of Cu binding was probably due to steric stabilization of the MWNTs dispersed in NOM, which inhibited the complexation by rendering the functional groups in NOM less favorable to Cu. The mortality and biochemical reactive oxygen species (ROS) production in the D. magna bioassay were enhanced in MWNTs-associated NOM compared to NOM alone because of increased free Cu2+ ion activity as expected from the titration and FTIR results. This study suggests the bioavailability of Cu is enhanced by the presence of MWNTs interacting with NOM

Global Proteomic Analysis of Lysine Succinylation in Zebrafish (Danio rerio)

Lysine succinylation (Ksu) is a novel identified post-translational modification that is conserved from prokaryotes to eukaryotes. As a kind of acylation, Ksu was reported to have different functions than other acylations at lysine residues. However, recent studies on Ksu have mainly focused on plants and bacteria. Ksu studies in vertebrates are still rare; thus, the biological function of Ksu in mammals needs to be studied further. In this study, we performed global Ksu mapping in Danio rerio (zebrafish) using mass spectrometry-based proteomics with the enrichment of Ksu peptides by immunoprecipitation technology. As a result, we identified 552 Ksu sites in 164 proteins. The raw data are available via ProteomeXchange with the identifier PXD013173. Compared with our previous studies on lysine acetylation and crotonylation, Ksu plays a major role in diverse metabolic processes such as carbon metabolism and the tricarboxylic acid circle. In addition, we defined five new succinylation motifs: (su)­KA, (su)­KxxxxA, (su)­KxxxxL, (su)­KxA, and (su)­KxV. In conclusion, our results provide a proteome-wide database to study Ksu in zebrafish, and our bioinformatics results facilitated the understanding of the role of Ksu in central metabolism

Global Proteomic Analysis of Lysine Succinylation in Zebrafish (Danio rerio)

Lysine succinylation (Ksu) is a novel identified post-translational modification that is conserved from prokaryotes to eukaryotes. As a kind of acylation, Ksu was reported to have different functions than other acylations at lysine residues. However, recent studies on Ksu have mainly focused on plants and bacteria. Ksu studies in vertebrates are still rare; thus, the biological function of Ksu in mammals needs to be studied further. In this study, we performed global Ksu mapping in Danio rerio (zebrafish) using mass spectrometry-based proteomics with the enrichment of Ksu peptides by immunoprecipitation technology. As a result, we identified 552 Ksu sites in 164 proteins. The raw data are available via ProteomeXchange with the identifier PXD013173. Compared with our previous studies on lysine acetylation and crotonylation, Ksu plays a major role in diverse metabolic processes such as carbon metabolism and the tricarboxylic acid circle. In addition, we defined five new succinylation motifs: (su)­KA, (su)­KxxxxA, (su)­KxxxxL, (su)­KxA, and (su)­KxV. In conclusion, our results provide a proteome-wide database to study Ksu in zebrafish, and our bioinformatics results facilitated the understanding of the role of Ksu in central metabolism

Global Proteomic Analysis of Lysine Succinylation in Zebrafish (Danio rerio)

Lysine succinylation (Ksu) is a novel identified post-translational modification that is conserved from prokaryotes to eukaryotes. As a kind of acylation, Ksu was reported to have different functions than other acylations at lysine residues. However, recent studies on Ksu have mainly focused on plants and bacteria. Ksu studies in vertebrates are still rare; thus, the biological function of Ksu in mammals needs to be studied further. In this study, we performed global Ksu mapping in Danio rerio (zebrafish) using mass spectrometry-based proteomics with the enrichment of Ksu peptides by immunoprecipitation technology. As a result, we identified 552 Ksu sites in 164 proteins. The raw data are available via ProteomeXchange with the identifier PXD013173. Compared with our previous studies on lysine acetylation and crotonylation, Ksu plays a major role in diverse metabolic processes such as carbon metabolism and the tricarboxylic acid circle. In addition, we defined five new succinylation motifs: (su)­KA, (su)­KxxxxA, (su)­KxxxxL, (su)­KxA, and (su)­KxV. In conclusion, our results provide a proteome-wide database to study Ksu in zebrafish, and our bioinformatics results facilitated the understanding of the role of Ksu in central metabolism

Global Proteomic Analysis of Lysine Succinylation in Zebrafish (Danio rerio)

Lysine succinylation (Ksu) is a novel identified post-translational modification that is conserved from prokaryotes to eukaryotes. As a kind of acylation, Ksu was reported to have different functions than other acylations at lysine residues. However, recent studies on Ksu have mainly focused on plants and bacteria. Ksu studies in vertebrates are still rare; thus, the biological function of Ksu in mammals needs to be studied further. In this study, we performed global Ksu mapping in Danio rerio (zebrafish) using mass spectrometry-based proteomics with the enrichment of Ksu peptides by immunoprecipitation technology. As a result, we identified 552 Ksu sites in 164 proteins. The raw data are available via ProteomeXchange with the identifier PXD013173. Compared with our previous studies on lysine acetylation and crotonylation, Ksu plays a major role in diverse metabolic processes such as carbon metabolism and the tricarboxylic acid circle. In addition, we defined five new succinylation motifs: (su)­KA, (su)­KxxxxA, (su)­KxxxxL, (su)­KxA, and (su)­KxV. In conclusion, our results provide a proteome-wide database to study Ksu in zebrafish, and our bioinformatics results facilitated the understanding of the role of Ksu in central metabolism

Global Proteomic Analysis of Lysine Succinylation in Zebrafish (Danio rerio)

Lysine succinylation (Ksu) is a novel identified post-translational modification that is conserved from prokaryotes to eukaryotes. As a kind of acylation, Ksu was reported to have different functions than other acylations at lysine residues. However, recent studies on Ksu have mainly focused on plants and bacteria. Ksu studies in vertebrates are still rare; thus, the biological function of Ksu in mammals needs to be studied further. In this study, we performed global Ksu mapping in Danio rerio (zebrafish) using mass spectrometry-based proteomics with the enrichment of Ksu peptides by immunoprecipitation technology. As a result, we identified 552 Ksu sites in 164 proteins. The raw data are available via ProteomeXchange with the identifier PXD013173. Compared with our previous studies on lysine acetylation and crotonylation, Ksu plays a major role in diverse metabolic processes such as carbon metabolism and the tricarboxylic acid circle. In addition, we defined five new succinylation motifs: (su)­KA, (su)­KxxxxA, (su)­KxxxxL, (su)­KxA, and (su)­KxV. In conclusion, our results provide a proteome-wide database to study Ksu in zebrafish, and our bioinformatics results facilitated the understanding of the role of Ksu in central metabolism

Global Proteomic Analysis of Lysine Succinylation in Zebrafish (Danio rerio)

Lysine succinylation (Ksu) is a novel identified post-translational modification that is conserved from prokaryotes to eukaryotes. As a kind of acylation, Ksu was reported to have different functions than other acylations at lysine residues. However, recent studies on Ksu have mainly focused on plants and bacteria. Ksu studies in vertebrates are still rare; thus, the biological function of Ksu in mammals needs to be studied further. In this study, we performed global Ksu mapping in Danio rerio (zebrafish) using mass spectrometry-based proteomics with the enrichment of Ksu peptides by immunoprecipitation technology. As a result, we identified 552 Ksu sites in 164 proteins. The raw data are available via ProteomeXchange with the identifier PXD013173. Compared with our previous studies on lysine acetylation and crotonylation, Ksu plays a major role in diverse metabolic processes such as carbon metabolism and the tricarboxylic acid circle. In addition, we defined five new succinylation motifs: (su)­KA, (su)­KxxxxA, (su)­KxxxxL, (su)­KxA, and (su)­KxV. In conclusion, our results provide a proteome-wide database to study Ksu in zebrafish, and our bioinformatics results facilitated the understanding of the role of Ksu in central metabolism

Effects of VPA on zebrafish survival, hatching status, and development.

NA: not available due to significantly decreased hatching rate. The results are shown as the mean ± standard deviation (N = 4). Asterisk (*) denotes statistical significance (p < 0.05).</p

Commonly observed GO enrichments in this and previous studies.

Commonly observed GO enrichments in this and previous studies.</p

Gene transcription confirmation by using qRT-PCR analysis.

The results are shown as the mean ± SEM (N = 4). Asterisks (*) and arrows indicate significant differences from the control and significant trend of the slope, respectively (p < 0.05).</p