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Pyruvate kinase

About: Pyruvate kinase is a research topic. Over the lifetime, 5683 publications have been published within this topic receiving 180020 citations. The topic is also known as: ATP:pyruvate 2-O-phosphotransferase & phosphoenolpyruvate kinase.


Papers
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Journal ArticleDOI
01 Apr 2004-Diabetes
TL;DR: Mechanisms that regulate PDK4 gene expression, previously established to be increased by glucocorticoids and decreased by insulin, were studied and transfection studies with E1A suggest that interactions between p300/CBP and GR as well as FOXO factors are important for glucOCorticoid-stimulated hPDK4 expression.
Abstract: Starvation and diabetes increase pyruvate dehydrogenase kinase-4 (PDK4) expression, which conserves gluconeogenic substrates by inactivating the pyruvate dehydrogenase complex. Mechanisms that regulate PDK4 gene expression, previously established to be increased by glucocorticoids and decreased by insulin, were studied. Treatment of HepG2 cells with dexamethasone increases the relative abundance of PDK4 mRNA, and insulin blocks this effect. Dexamethasone also increases human PDK4 (hPDK4) promoter activity in HepG2 cells, and insulin partially inhibits this effect. Expression of constitutively active PKBα abrogates dexamethasone stimulation of hPDK4 promoter activity, while coexpression of constitutively active FOXO1a or FOXO3a, which are mutated to alanine at the three phosphorylation sites for protein kinase B (PKB), disrupts the ability of PKBα to inhibit promoter activity. A glucocorticoid response element for glucocorticoid receptor (GR) binding and three insulin response sequences (IRSs) that bind FOXO1a and FOXO3a are identified in the hPDK4 promoter. Mutation of the IRSs reduces the ability of glucocorticoids to stimulate PDK4 transcription. Transfection studies with E1A, which binds to and inactivates p300/CBP, suggest that interactions between p300/CBP and GR as well as FOXO factors are important for glucocorticoid-stimulated hPDK4 expression. Insulin suppresses the hPDK4 induction by glucocorticoids through inactivation of the FOXO factors.

162 citations

Journal ArticleDOI
Prachi Anand1, K. Y. Murali1, Vibha Tandon1, P.S. Murthy1, Ramesh Chandra1 
TL;DR: With the high margin of safety of CND, it can be developed as a potential therapeutic candidate for the treatment of diabetes and shown to increase the glucose uptake through glucose transporter (GLUT4) translocation in peripheral tissues.

162 citations

Journal ArticleDOI
TL;DR: In this paper, the authors examined the miRNA and proteomic profiles of blood outgrowth endothelial cells (BOECs) from patients with heritable pulmonary arterial hypertension (PAH) caused by mutations in the bone morphogenetic protein receptor type 2 (BMPR2) gene and patients with idiopathic PAH to determine mechanisms underlying abnormal endothelial glycolysis.
Abstract: Background:Pulmonary arterial hypertension (PAH) is characterized by abnormal growth and enhanced glycolysis of pulmonary artery endothelial cells. However, the mechanisms underlying alterations in energy production have not been identified. Methods:Here, we examined the miRNA and proteomic profiles of blood outgrowth endothelial cells (BOECs) from patients with heritable PAH caused by mutations in the bone morphogenetic protein receptor type 2 (BMPR2) gene and patients with idiopathic PAH to determine mechanisms underlying abnormal endothelial glycolysis. We hypothesized that in BOECs from patients with PAH, the downregulation of microRNA-124 (miR-124), determined with a tiered systems biology approach, is responsible for increased expression of the splicing factor PTBP1 (polypyrimidine tract binding protein), resulting in alternative splicing of pyruvate kinase muscle isoforms 1 and 2 (PKM1 and 2) and consequently increased PKM2 expression. We questioned whether this alternative regulation plays a criti...

162 citations

Journal ArticleDOI
TL;DR: A permeabilization method which allows the assay of several intracellular enzymes within the boundaries of the yeast cell wall is described and the kinetic properties of hexokinase and pyruvate kinase examined in the permeabilized cells are essentially the same as in cell-free extracts.
Abstract: A permeabilization method which allows the assay of several intracellular enzymes within the boundaries of the yeast cell wall is described. The kinetic properties of hexokinase and pyruvate kinase examined in the permeabilized cells, including the allosteric activation of the latter by fructose bisphosphate, are essentially the same as in cell-free extracts.

161 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023215
2022201
2021147
2020166
2019150
2018138