Global proteomic analysis of protein acetylation affecting metabolic regulation in Daphnia pulex

Changes in iTRAQ-Based Proteomic Profiling of the Cladoceran Daphnia magna Exposed to Microcystin-Producing and Microcystin-Free Microcystis aeruginosa

“…Given the advances in analytical techniques, proteomic analysis has become a new frontier in molecular biology; this technique can be applied to determine the differences or changes in protein expression patterns of organs, cells, or subcellular compartments to a reasonably high level of coverage. Over the past few years, 2D differential in-gel electrophoresis (DIGE) is a quantitative proteomic method that has been successfully applied in Daphnia research which focused on predation risk, , protein acetylation and exposure to copper and paraquat . As an approach for quantifying changes with higher-throughput than DIGE, iTRAQ profiling is an emerging and useful technique to quantify changes in global-scale proteins (especially for less-abundant proteins) among individuals responsive to various environmental stressors. − To the best of our knowledge, the present study is the first to use an iTRAQ approach to identify and quantify proteomes of zooplankton mobilized against environmental pollutants, even though iTRAQ was previously used to study antipredation response in Daphnia .…”

Proteins and Proteoforms: New Separation Challenges

“…Lysine acetylation is also important for p53 functioning and microtubule stabilization, being found in bacteria, yeast, insects, and human cell lines. − Moreover, it plays a role in the regulation of protein synthesis, the citric acid (TCA) cycle, fatty acid metabolism, glycolysis/gluconeogenesis, and secondary metabolism.…”

Global Profiling of Lysine Acetylation and Lactylation in Kupffer Cells

“…Protein lysine acetylation (Kac) is a dynamic and reversible post-translational modification (PTM), and the level of Kac modification in a protein is controlled by lysine acetyltransferases and deacetylases. In 2006, Kim et al reported Kac substrates in nonhistone proteins, and studies on the substrate identification and function of Kac are still being conducted. − Therefore, Kac substrates have been identified in several histone and nonhistone proteins that regulate numerous biological processes. , In particular, studies of the global acetylome in liver or liver-derived cells have also been reported. Large-scale proteomic approaches in mouse liver mitochondria have been performed, , and studies have been conducted in hepatocytes, HepG2 cells, and AML-12 cells. , Although various global acetylome studies have been performed on liver and liver-derived cells, no studies involving KCs have been performed.…”