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Pyruvate kinase, liver and RBC

Pyruvate Kinase
The protein encoded by this gene is a pyruvate kinase that catalyzes the transphosphorylation of phohsphoenolpyruvate into pyruvate and ATP, which is the rate-limiting step of glycolysis. Defects in this enzyme, due to gene mutations or genetic variations, are the common cause of chronic hereditary nonspherocytic hemolytic anemia (CNSHA or HNSHA). Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Hoxa5, M2-PK, CAN, HAD, Phosphofructokinase-1
Papers using Pyruvate Kinase antibodies
Extracellular metabolism of ATP and other nucleotides
Mahaut-Smith Martyn P et al., In British Journal of Haematology, 1999
... CHRONO-LUME was purchased from Labmedics (Manchester, UK), Pyruvate kinase was obtained from Roche Diagnostics Limited (East Sussex, UK), GF109203X and MRS2179 were purchased from Tocris (Bristol, UK) ...
Papers on Pyruvate Kinase
Reciprocal Changes in Phosphoenolpyruvate Carboxykinase and Pyruvate Kinase with Age Are a Determinant of Aging in Caenorhabditis elegans.
Feng et al., Suzhou, China. In J Biol Chem, Feb 2016
In locomotory muscle of post-fertile Caenorhabditis elegans, we identified a progressive decrease in cytosolic phosphoenolpyruvate carboxykinase (PEPCK-C), a longevity-associated metabolic enzyme, and a reciprocal increase in glycolytic pyruvate kinase (PK) that were necessary and sufficient to limit lifespan.
Two Novel Missense Mutations and a 5bp Deletion in the Erythroid-Specific Promoter of the PKLR Gene in Two Unrelated Patients With Pyruvate Kinase Deficient Transfusion-Dependent Chronic Nonspherocytic Hemolytic Anemia.
Haas et al., Vienna, Austria. In Pediatr Blood Cancer, Feb 2016
Reduced erythrocyte pyruvate kinase activity in their asymptomatic parents provided the diagnostic clues for mutation screening of the PKLR gene and revealed that one child was a compound heterozygote of a novel paternally derived 5-bp deletion in the promoter region (c.-88_-84delTCTCT) and a maternally derived missense mutation in exon nine (c.1174G>A; p.Ala392Thr).
M-Type Pyruvate Kinase Isoforms and Lactate Dehydrogenase A in the Mammalian Retina: Metabolic Implications.
Chidlow et al., Adelaide, Australia. In Invest Ophthalmol Vis Sci, Feb 2016
The molecular switch controlling glycolytic flow is thought to be an isoenzyme of pyruvate kinase (PKM2).
Mitochondrial phenotype of marsupial torpor: Fuel metabolic switch in the Chilean mouse-opossum Thylamys elegans.
Blier et al., Valdivia, Chile. In J Exp Zool A Ecol Genet Physiol, Jan 2016
Here, we analyzed for first time the changes in the maximal activity of key enzymes related to fatty acid (Carnitine palmitoyltransferase and β-Hydroxyacyl CoA dehydrogenase) and carbohydrate (Pyruvate kinase, Phosphofructokinase and Lactate dehydrogenase) catabolism, as well as mitochondrial oxidative capacity (Citrate synthase), in six organs of torpid, arousing and euthermic Chilean mouse-opossums (Thylamys elegans).
Inhibitory and Activating Effects of Some Flavonoid Derivatives on Human Pyruvate Kinase Isoenzyme M2.
Kuzu et al., Çankırı, Turkey. In Arch Pharm (weinheim), Jan 2016
UNASSIGNED: Pyruvate kinase isoenzyme M2 (PKM2) is expressed excessively in many different cancer types and it plays an important role in the control of glucose metabolism.
Generation of a High Number of Healthy Erythroid Cells from Gene-Edited Pyruvate Kinase Deficiency Patient-Specific Induced Pluripotent Stem Cells.
Segovia et al., Madrid, Spain. In Stem Cell Reports, Jan 2016
Pyruvate kinase deficiency (PKD) is a rare erythroid metabolic disease caused by mutations in the PKLR gene.
Pyruvate Kinase Isoform Switching and Hepatic Metabolic Reprogramming by the Environmental Contaminant 2,3,7,8-Tetrachlorodibenzo-p-Dioxin.
Zacharewski et al., Toronto, Canada. In Toxicol Sci, Dec 2015
More specifically, TCDD increased pyruvate kinase isoform M2 (PKM2) gene and protein expression.
Adaptations of energy metabolism during cerebellar neurogenesis are co-opted in medulloblastoma.
Gershon et al., Chapel Hill, United States. In Cancer Lett, Feb 2015
During the physiologic proliferation of neural progenitors, metabolic enzymes generally associated with malignancy, including Hexokinase 2 (Hk2) and Pyruvate kinase M2 (PkM2) configure energy metabolism to support growth.
Pyruvate kinase M2 regulates Hif-1α activity and IL-1β induction and is a critical determinant of the warburg effect in LPS-activated macrophages.
O'Neill et al., Dublin, Ireland. In Cell Metab, Feb 2015
We here show that LPS induces expression of the key metabolic regulator Pyruvate Kinase M2 (PKM2).
Modulation of Malaria Phenotypes by Pyruvate Kinase (PKLR) Variants in a Thai Population.
Gros et al., Montréal, Canada. In Plos One, 2014
Pyruvate kinase (PKLR) is a critical erythrocyte enzyme that is required for glycolysis and production of ATP.
Metabolism of activated T lymphocytes.
Wilson et al., Saskatoon, Canada. In Curr Opin Immunol, 2014
Activated T cells show induced expression of, among other things, Glucose Transporter 1 and several glycolytic enzymes, including ADP-Dependent Glucokinase and the low affinity isoform Pyruvate Kinase-M2 (which promote glycolytic flux), as well Glutamine Transporters and Glycerol-3-phosphate Dehydrogenase 2 which make available glutamate and glycerol-3-phosphate as mitochondrial energy sources.
Pyruvate kinase M2: regulatory circuits and potential for therapeutic intervention.
Bamezai et al., New Delhi, India. In Curr Pharm Des, 2013
Pyruvate kinase isoenzyme type M2 (abbreviations: PKM2, M2-PK) plays a key role in modulating glucose metabolism to support cell proliferation.
Metabolic modulation of epigenetics in gliomas.
Thompson et al., New York City, United States. In Brain Pathol, 2013
Pyruvate kinase M2 (PKM2), an enzyme that plays a critical role in the glycolytic pathway, is a second example of a metabolic enzyme that can affect histone modifications.
Dual roles of PKM2 in cancer metabolism.
Le et al., Shanghai, China. In Acta Biochim Biophys Sin (shanghai), 2013
Pyruvate kinase (PK), which catalyzes the final step of glycolysis, has emerged as a potential regulator of this metabolic phenotype.
ERK1/2-dependent phosphorylation and nuclear translocation of PKM2 promotes the Warburg effect.
Lu et al., Houston, United States. In Nat Cell Biol, 2012
Pyruvate kinase M2 (PKM2) is upregulated in multiple cancer types and contributes to the Warburg effect by unclear mechanisms.
SARS-CoV nucleocapsid protein interacts with cellular pyruvate kinase protein and inhibits its activity.
Lo et al., Taiwan. In Arch Virol, 2012
These results suggest that SARS coronavirus could reduce pyruvate kinase activity via its nucleocapsid protein, and this may in turn cause disease.
Genetic diversity in human erythrocyte pyruvate kinase.
Gros et al., Montréal, Canada. In Genes Immun, 2012
Rich genetic diversity was detected in PKLR, including 59 single-nucleotide polymorphisms and several loss-of-function variants (frequency 1.5%).
Six children with pyruvate kinase deficiency from one small town: molecular characterization of the PK-LR gene.
Zanella et al., Salt Lake City, United States. In J Pediatr, 2011
We identified the pyruvate kinase liver/red cell enzyme gene mutation of 8 children previously diagnosed with pyruvate kinase deficiency who were living in a remote town in the western United States
Acetylation targets the M2 isoform of pyruvate kinase for degradation through chaperone-mediated autophagy and promotes tumor growth.
Lei et al., Shanghai, China. In Mol Cell, 2011
The results reveal an acetylation regulation of pyruvate kinase and the link between lysine acetylation and chaperone-mediated autophagy.
Turning on a fuel switch of cancer: hnRNP proteins regulate alternative splicing of pyruvate kinase mRNA.
Manley et al., New York City, United States. In Cancer Res, 2010
Studies indicate that switching from pyruvate kinase spliced isoform PKM1 to PKM2 promotes aerobic glycolysis and provides a selective advantage for tumor formation, and the alternative splicing is controlled by hnRNP family members.
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