Project description:Pyruvate Dehydrogenase Kinase 4 (Pdk4) is a pyruvate dehydrogenase inhibiton gene that strongly regulates metabolism. We studied the expression of Pdk4 in the young and aged mouse heart in both healthy conditions and after ischemic insult.
Project description:We have previously shown that in Arabidopsis the three enzymes of lower glycolysis phosphoglycerate mutase (PGAM), enolase and pyruvate kinase form a complex which play an important role in co-sub-cellar localization the mitochondria to the chloroplast. Given that their metabolites of these mutants, the complementation of pgam mutant and overexpression of PGAM are still unclear, here, we present the gas chromatography mass spectrometry-based metabolomics data and plant growth phenotypes of them. Compared with wild type, both sugar and amino acid are significantly changed at mutants of phosphoglycerate mutase, enolase, pyruvate kinase. Overexpression the PGAM could decrease the content of 3PGA, sugar and several amino acids and increase the content of alanine and pyruvate. In addition, pgam mutant could not be fully complemented by nuclear sub-localized, the side-directed-mutated and the E.coli PGAM at plant phenotype and metabolites profiling, especially the content of 3PGA, serine and intermediates of TCA cycle. These data suggested that the low glycolysis complex play an important role at both mitochondria-chloroplast co-subcellar localization and the metabolites exchange.
Project description:Activation of CD4+ T cells requires metabolic reprograming to sustain demands of cellular building blocks and ATP. Pyruvate dehydrogenase kinase (PDK) is an enzyme regulating pyruvate dehydrogenase complex subunit alpha 1 (PDHE1-alpha), which converts pyruvate to acetyl-CoA. Gene expression analysis of TCR-stimulated CD4+ T cells with PDK4 deletion exhibited the reduced calcium signaling and aerobic glycolysis pathway.
Project description:Next-generation sequencing (NGS) has been used to study the histone acetylation in Arabidopsis etiolated seedlings under air and ethylene treatment. The goal of this study is to investigate how pyruvate dehydrogenase complex is involved in histone acetylation changes in response to ethylene.
Project description:Purpose: In this study, we compared transcriptome profiling (RNA-seq) between normal mouse embryonic stem cell (E14) and Hexokinase2 (Hk2)/ Pyruvate Kinase M2 (Pkm2) overexpressed E14 cell. Result: Using an optimized data analysis workflow, we mapped over 4 billion sequence reads per sample to the mouse genome (build mm9) and identified 28698 transcripts in 5 samples. Conclusion: Our study represents the first detailed analysis of Hk2/ Pkm2 overexpressed E14 cell transcriptomes, generated by RNA-seq technology We compared transcriptome profiling (RNA-Seq) between normal mouse embryonic stem cell (E14) and E14 cells over-expressing Hexokinase2 (Hk2)/Pyruvate Kinase M2 (Pkm2)
Project description:Pyruvate kinase (PK) catalyzes the conversion of phosphoenolpyruvate to pyruvate during glycolysis. The PK isoform PKM2 has additional roles in regulation of gene transcription and protein phosphorylation. PKM2 controls macrophage metabolic remodeling in inflammation, but its role in T cell biology is poorly understood. These results show that TEPP-46, an activator of PKM2, reduces CD4+ T cell activation, proliferation, and cytokine production by inhibiting essential signaling pathways and preventing glycolysis.
Project description:Series of 6 repetitions of hybridization of treatment (cue1) and control (WT) each. Comparison of Arabidopsis cue1-1 mutant lacking phosphoenol pyruvate translocator versus WT. S.J. Streatfield et al., Plant Cell 11 (1999), pp.1609-1622 Keywords: repeat sample
Project description:The catalase-negative, facultative anaerobe Streptococcus pneumoniae D39 is naturally resistant to hydrogen peroxide (H2O2) produced endogenously by pyruvate oxidase (SpxB). Here, we investigate the adaptive response to endogenously produced H2O2. We show that lactate oxidase, which converts lactate to pyruvate, positively impacts pyruvate flux through SpxB and that ∆lctO mutants produce significantly lower H2O2. In addition, both the SpxB and pyruvate dehydrogenase complex (PDHC) pathways contribute to acetyl-CoA production during aerobic growth, and the pyruvate format lyase (PFL) pathway is the major acetyl-CoA pathway during anaerobic growth. Microarray analysis of the D39 strain cultured under aerobic vs. strict anaerobic conditions show up-regulation of spxB, a rhodanese-like protein (spd0091), tpxD, sodA, piuB, piuD and an Fe-S protein biogenesis operon under H2O2-producing conditions. Proteome profiling of H2O2-induced sulfenylation reveals that sulfenylation levels correlate with cellular H2O2 production, with endogenous sulfenylation of ≈50 proteins. Deletion of tpxD increases cellular sulfenylation 5-fold and has an inhibitory effect on ATP generation. Two major targets of protein sulfenylation are glyceraldehyde-3-phosphate dehydrogenase (GapA) and SpxB itself, but also include pyruvate kinase, LctO, AdhE and acetate kinase (AckA). Sulfenylation of GapA is inhibitory, while the effect on SpxB activity is negligible, consistent with this cell-abundant protein functioning as a “sink” for endogenous H2O2. Strikingly, four enzymes of capsular polysaccharide biosynthesis are sulfenylated, as are enzymes associated nucleotide biosynthesis via ribulose-5-phosphate. We propose that LctO/SpxB-generated H2O2 functions as a signaling molecule to down-regulate capsule production and drive altered flux through sugar utilization pathways.
Project description:Next-generation sequencing (NGS) has been used to study the differential gene expression in Arabidopsis etiolated seedlings under air and ethylene treatment. The goal of this study is to investigate how pyruvate dehydrogenase complex is involved in transcriptional regulation in response to ethylene.