Mammalian pyruvate dehydrogenase multienzyme complex is inactivated when treated with a leupeptin-sensitive enzyme (termed inactivase) obtained from rat liver lysosomes. However, the inactivation of the overall reaction does not affect any of the component activities of the enzyme complex. By several methods it is demonstrated that treatment with the inactivase provokes the disassembly of the complex into its constituent enzyme components which, though being enzymatically active when assayed separately, are unable to catalyze the coordinated reaction sequence of pyruvate oxidation. The dissociation occurs as a consequence of limited proteolysis of the lipoate acetyltransferase core of the multienzyme complex. Isolated nicked acetyltransferase retains its complete enzymatic activity and behaves as a high-molecular-weight aggregate. The lipoamide dehydrogenase and pyruvate dehydrogenase components, however, are not cleaved by the inactivase.
The human pyruvate dehydrogenase complex (PDC) is a large macromolecular assembly involved in the oxidative decarboxylation of pyruvate yielding acetyl CoA as the end product of this reaction, which subsequently enters the tricarboxylic acid (TCA) cycle. PDC is composed of multiple copies of various enzyme subunits, termed E1, E2 and E3. Human PDC also contains an additional component, E3BP, which has evolved in order to bind E3 to the core of the complex. The individual components of human PDC have now been cloned and overexpressed in E. coli. A His-tag has been engineered into the N-terminus of each protein to facilitate the rapid purification of these subunits using affinity chromatography. With the exception of E1, an alpha2beta2 heterotetramer, all recombinant proteins are soluble and produced in high yield. By using antibodies specific only for lipoylated E2 and E3BP from PDC, and by assaying the catalytically active subunits for activity, it has been found that these proteins are ...
TY - JOUR. T1 - Active pyruvate dehydrogenase and impaired gluconeogenesis in orthotopic hepatomas of rats. AU - Lee, Min Hee. AU - DeBerardinis, Ralph J.. AU - Wen, Xiaodong. AU - Corbin, Ian R.. AU - Sherry, A. Dean. AU - Malloy, Craig R.. AU - Jin, Eunsook S.. PY - 2019/12. Y1 - 2019/12. N2 - Background: Therapies targeting altered activity of pyruvate dehydrogenase (PDH) and pyruvate carboxylase (PC) have been proposed for hepatomas. However, the activities of these pathways in hepatomas in vivo have not been distinguished. Here we examined pyruvate entry into the tricarboxylic acid (TCA) cycle through PDH versus PC in vivo using hepatoma-bearing rats. Methods: Hepatoma-bearing rats were generated by intrahepatic injection of H4IIE cells. Metabolism of 13C-labeled glycerol, a physiological substrate for both gluconeogenesis and energy production, was measured with 13C NMR analysis. The concentration of key metabolites and the expression of relevant enzymes were measured in hepatoma, ...
The SCOP classification for the Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex superfamily including the families contained in it. Additional information provided includes InterPro annotation (if available), Functional annotation, and SUPERFAMILY links to genome assignments, alignments, domain combinations, taxonomic visualisation and hidden Markov model information.
Crucial to glucose homoeostasis in humans, the hPDC (human pyruvate dehydrogenase complex) is a massive molecular machine comprising multiple copies of three distinct enzymes (E1-E3) and an accessory subunit, E3BP (E3-binding protein). Its icosahedral E2/E3BP 60-meric core provides the central structural and mechanistic framework ensuring favourable E1 and E3 positioning and enzyme co-operativity. Current core models indicate either a 48E2+12E3BP or a 40E2+20E3BP subunit composition. In the present study, we demonstrate clear differences in subunit content and organization between the recombinant hPDC core (rhPDC; 40E2+20E3BP), generated under defined conditions where E3BP is produced in excess, and its native bovine (48E2+12E3BP) counterpart. The results of the present study provide a rational basis for resolving apparent differences between previous models, both obtained using rhE2/E3BP core assemblies where no account was taken of relative E2 and E3BP expression levels. Mathematical ...
TY - JOUR. T1 - Role of pyruvate dehydrogenase kinase 4 in regulating PDH activation during acute muscle contraction. AU - Herbst, Eric A.F.. AU - Dunford, Emily C.E.. AU - Harris, Robert A.. AU - Vandenboom, Rene. AU - LeBlanc, Paul J.. AU - Roy, Brian D.. AU - Jeoung, Nam Ho. AU - Peters, Sandra J.. PY - 2012/2/1. Y1 - 2012/2/1. N2 - The oxidation of carbohydrates in mammals is regulated by the pyruvate dehydrogenase (PDH) complex, which is covalently regulated by four PDH kinases (PDK1-4) and two PDH phosphatases (PDP1-2) unique to the PDH complex. To investigate the role that PDK4 plays in regulating PDH activation (PDHa) during muscle contraction, mouse extensor digitorum muscle was removed from wild type (WT) and PDK4-knockout (PDK4-KO) mice after a 24 h fast and stimulated for 3 min either at 10 Hz (low-intensity contraction), 40 Hz (moderate-intensity contraction), or allowed to rest. Force was recorded and muscle PDHa activity and metabolite concentrations were measured. PDHa activity ...
1. The effects of recombinant human tumour necrosis factor alpha (TNF) and murine interleukin-1 alpha (IL-1) on the activation state of the hepatic pyruvate dehydrogenase complex (PDHa), the activity of mitochondrial PDH kinase, hepatic lipogenesis de novo and plasma triacylglycerol (TG) concentrations were studied. 2. Monokine effects depended upon prior nutritional state. In rats fasted for 20 h or 45 h before monokine administration and refeeding (orally or with intravenous glucose), PDHa, TG and hepatic lipogenesis were not increased. In rats fed ad libitum, treatment with TNF plus IL-1 increased the contribution of hepatic lipogenesis to circulating TG to 550% of control values (P = 0.03) and plasma TG concentrations to 159% (P = 0.02), whereas PDHa increased slightly to 120% (P = 0.02) and liver glycogen content fell to 45.8% (P = 0.05) of control values. 3. Intrinsic hepatic PDH kinase activity was not changed by monokine treatment in rats fed ad libitum. 4. The increased lipogenesis de ...
Specific mutants were developed to evaluate the roles of several residues in [Alpha]8 helix of the regulatory (R) domain of human pyruvate dehydrogenase kinase 2 (PDHK2) in the linkage between the Regulatory (R) and catalytic (Cat) domain (Q144A), dichloroacetate (DCA)/pyruvate inhibition (R154C, R158A, I157F) and stimulation by reductive acetylation (L160A, R154C/L160A). All mutants, with the exception of L160A, were active, and were bound to and had their activities enhanced by dihydrolipoyl acetyltransferase (E2). The cross arms between subunits are anchored by W383. Based on the studies on the W383F mutant, W383 provided majority of the intrinsic Trp fluorescence; and ligand(s) binding quenched primarily (pyruvate) or exclusively (ADP or ATP) the fluorescence of W383. The Q144 mutation in the R domain caused 14-fold weaker K[superscript]+ binding with ATP in the Cat domain but did not alter the weaker K[superscript]+ binding with ADP unless Pi was included. Similarly, with 100 mM ...
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
International audience; The multifunctional protein E4 transcription factor 1 (E4F1) is an essential regulator of epidermal stem cell (ESC) maintenance. Here, we found that E4F1 transcriptionally regulates a metabolic program involved in pyruvate metabolism that is required to maintain skin homeostasis. E4F1 deficiency in basal keratinocytes resulted in deregulated expression of dihydrolipoamide acetyltransferase (Dlat), a gene encoding the E2 subunit of the mitochondrial pyruvate dehydrogenase (PDH) complex. Accordingly, E4f1 knock-out (KO) keratinocytes exhibited impaired PDH activity and a redirection of the glycolytic flux toward lactate production. The metabolic reprogramming of E4f1 KO keratinocytes associated with remodeling of their microenvironment and alterations of the basement membrane, led to ESC mislocalization and exhaustion of the ESC pool. ShRNA-mediated depletion of Dlat in primary keratinocytes recapitulated defects observed upon E4f1 inactivation, including increased lactate
The amino acid sequence of pyruvate dehydrogenase E1, which is a consists of two alpha (PDHA1) and two beta (PDHB) subunits. Pyruvate dehydrogenase makes up part of the pyruvate dehydrogenase complex which serves as a link between glycolysis and the tricarboxylic acid acid cycle. ...
Pyruvate dehydrogenase lipoamide kinase isozyme 1, mitochondrial is an enzyme that in humans is encoded by the PDK1 gene. It codes for an isozyme of pyruvate dehydrogenase kinase (PDK). Pyruvate dehydrogenase (PDH) is a part of a mitochondrial multienzyme complex that catalyzes the oxidative decarboxylation of pyruvate and is one of the major enzymes responsible for the regulation of homeostasis of carbohydrate fuels in mammals. The enzymatic activity is regulated by a phosphorylation/dephosphorylation cycle. Phosphorylation of PDH by a specific pyruvate dehydrogenase kinase (PDK) results in inactivation. The mature protein encoded by the PDK4 gene contains 407 amino acids in its sequence. To form the active protein, two of the polypeptide chains come together to form an open conformation. The catalytic domain of PDK1 might exist separately in cells and important for the regulation of the PDK1 substrate. The crystal structural studies suggest that the PIF-pocked is located at the catalytic ...
4JDR: Insight to the Interaction of the Dihydrolipoamide Acetyltransferase (E2) Core with the Peripheral Components in the Escherichia coli Pyruvate Dehydrogenase Complex via Multifaceted Structural Approaches.
Mouse monoclonal Mitochondrial Pyruvate dehydrogenase kinase 1 antibody [4A11] validated for WB, ELISA, IHC, Flow Cyt, ICC/IF and tested in Human, Mouse and…
bdi:100823294 K00627 pyruvate dehydrogenase E2 component (dihydrolipoamide acetyltransferase) [EC:2.3.1.12] , (RefSeq) dihydrolipoyllysine-residue acetyltransferase component 2 of pyruvate dehydrogenase complex, mitochondrial-like (A) MALLLRHSRKLRRVHGVLDCERGSIARHFSASACSTTLKKEDGVSNSSLEYGKKAGSLSI SQDRKSGKDTHKFKVSPQEARGLYSSNRVLISATGVNSLFSCGQVVLARHFSSAADLPAH EEIGMPSLSPTMTEGNIARWVKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVCG DGAKEIKVGEIIAITVEEEGDIEKFKDYKAPASSAAPAESKPQSESTEPKGEEKELPKAA EPKATKTEESSHSGDRVFSSPIARKLAEDNNVPLSSLKGTGPDGRILKADIEEYLSSEAK GTKKEAAAAPGLGHVDLPNSQIRKVTANRLLKSKQTIPHYYLTVDSRVDELIKLRSELNP LQDASGGKKISINDLVIKAAALALRKVPECNSSWMNDFIRQYHNVNINVAVQTEHGLFVP VVRDADKKGLATIADEVKQLALRARDNSLKPEDYEGGTFTVSNLGGPFGIKQFCAIVNPP QAAILAIGSAEKRVIPGTDGQFEVGSFMSATLSCDHRVIDGAIGAEWLKAFKGYLENPTT MLL ...
for pre- and post-N3, respectively). However, the active form of pyruvate dehydrogenase (PDHa) activity decreased to a similar extent in both conditions (0.93 ± 0.17 and 0.43 ± 0.09 mmol/kg wet wt pre- and post-HF; vs. 0.87 ± 0.19 and 0.39 ± 0.05 mmol/kg wet wt pre- and post-N3, respectively). This suggested that the difference in PDK activity did not affect PDHa activation in the basal state, and it was regulated by intramitochondrial effectors, primarily muscle pyruvate concentration. Muscle glycogen content was consistent throughout the study, before and after both diet conditions, whereas muscle glucose-6-phosphate, glycerol-3-phosphate, lactate, and pyruvate were decreased after the high-fat diets. Plasma triglycerides decreased after both high-fat diets but decreased to a greater extent after the N3, whereas plasma free fatty acids increased after both diets, but to a lesser extent after the N3. In summary, PDK activity is decreased after a high-fat diet that is rich in n-3 fatty ...
Introduction: Pyruvate Dehydrogenase (PDH) activity has been shown to be inhibited in animal models of post-cardiac arrest. This depressed activity has been postulated to be directly related to neurologic injury secondary to aerobic metabolic dysfunction and accumulation of toxic metabolites. The objective of this study was to determine if PDH inhibition occurs after cardiac arrest (CA) in humans.. Methods: Patients were enrolled as part of a prospective observational trial of CA at a single urban academic medical center from 1/13 to 4/13. A blood sample was collected as early after ROSC as informed consent could be obtained (,24 hours). Our control group consisted of volunteers with no significant medical history. We used a novel method to measure PDH activity from peripheral blood mononuclear cells isolated from fresh blood. We quantified total PDH in 15mg / ml of isolated protein and determined overall PDH activity (PDH activity / total protein) and specific PDH activity (PDH activity / PDH ...
Tight coupling between cytosolic and mitochondrial metabolism is key for GSIS (glucose-stimulated insulin secretion). In the present study we examined the regulatory contribution of PDH (pyruvate dehydrogenase) kinase 1, a negative regulator of PDH, to metabolic coupling in 832/13 clonal beta-cells. Knockdown of PDH kinase 1 with siRNA (small interfering RNA) reduced its mRNA (,80 %) and protein level (,40 %) after 72 h. PDH activity, glucose-stimulated cellular oxygen consumption and pyruvate-stimulated mitochondrial oxygen consumption increased 1.7- (P , 0.05), 1.6- (P , 0.05) and 1.6-fold (P , 0.05) respectively. Gas chromatography/MS revealed an altered metabolite profile upon silencing of PDH kinase 1, determined by increased levels of the tricarboxylic acid cycle intermediates malate, fumarate and alpha-ketoglutarate. These metabolic alterations were associated with exaggerated GSIS (5-fold compared with 3.1-fold in control cells; P , 0.01). Insulin secretion, provoked by leucine and ...
A Synthetic Peptide, Corresponding To The 14-amino Acid Tryptic Fragment Containing Phosphorylation Sites One And Two Of Bovine Mitochondrial Pyruvate Dehydrogenase, Was Coupled To Limulus Polyphemus Hemocyanin And Used To Produce Rabbit Polyclonal
Background Hypoxia and inflammation have been identified as hallmarks of cancer. metabolic phenotype but has no significant effect on cellular metabolism of HepG2 and JHH-4 hepatoma cells. Although we observed only minor changes in glucose uptake and lactate secretion in PH5CH8 upon OSM treatment, buy 315694-89-4 we identified more pronounced changes in intracellular fluxes based on stable isotope labeling experiments. In particular, glucose oxidation in the tricarboxylic acid (TCA) cycle is reduced through pyruvate dehydrogenase kinase 1 (PDK1)-mediated inhibition of the pyruvate dehydrogenase complex, thereby reducing the oxidative TCA cycle flux. As a result of the impaired mitochondrial glucose and glutamine oxidation, the reductive isocitrate dehydrogenase flux was increased. Conclusions We provide evidence that connects the inflammatory mediator OSM to a hypoxia-like metabolic phenotype. In the human hepatocyte cell line PH5CH, OSM-mediated upregulation Rabbit Polyclonal to MSHR of HIF-1 ...
The PDH (pyruvate dehydrogenase) multi-enzyme complex catalyses a key regulatory step in oxidative glycolysis. Phosphorylation of the E1 subunit of the complex on serine residues results in the inactivation of enzyme activity. A family of four dedicated PDH kinase isoenzymes exists, each of which displays a distinct tissue-specific expression profile. AZD7545 is one of a series of PDH kinase inhibitors developed for the treatment of type 2 diabetes. The isoenzyme-selectivity profile of AZD7545 and related compounds is described and the consequences for their in vivo mode of action are discussed.. ...
Pyruvate dehydrogenase (PDH) is a mitochondrial multienzyme complex that catalyzes the oxidative decarboxylation of pyruvate and is one of the major enzymes responsible for the regulation of homeostasis of carbohydrate fuels in mammals. The enzymatic activity is regulated by a phosphorylation/dephosphorylation cycle. Phosphorylation of PDH by a specific pyruvate dehydrogenase kinase (PDH kinase; PDHK; PDK) results in inactivation. Multiple alternatively spliced transcript variants have been found for this gene. PDH catalyzes the conversion of pyruvate to acetyl-coenzyme A, which enters into the Krebs cycle, providing ATP to the cell. PDH activity is under the control of pyruvate dehydrogenase kinases (PDHKs).. ...
Transcriptional regulation of pyruvate dehydrogenase kinase 4 in skeletal muscle during and after exercise - Volume 63 Issue 2 - Henriette Pilegaard, P. Darrell Neufer
Pro-inflammatory macrophages sustain pyruvate oxidation through pyruvate dehydrogenase for the synthesis of itaconate and to enable cytokine ...
Principal Investigator:KOIKE Kichiko, Project Period (FY):1989 - 1990, Research Category:Grant-in-Aid for General Scientific Research (C), Research Field:Pathological medical chemistry
General purpose of this lecture is to presentation on Citric Acid Cycle. This lecture briefly explain on Pyruvate Dehydrogenase Complex (PDC) and its contr
As the study by Wambolt et al. (1) shows, adaptation turns into maladaptation when an acute stress (ischemia and reperfusion) is superimposed on an adaptive response. The excess production of protons from enhanced glycolytic metabolism results in contractile dysfunction by mechanisms that are not completely understood. The deleterious effects on contraction that accompany enhanced glycolytic flux are prevented by the addition of a drug that promotes pyruvate oxidation, thereby reducing its conversion to lactate. Dichloroacetate, like ranolazine, and probably also l-carnitine, activate the pyruvate dehydrogenase (PDH) complex by inhibiting pyruvate dehydrogenase kinase (PDK) (29-32). Restoring carbon flux through PDH may be all that is necessary to improve postischemic contractile function (30). Dichloroacetate, although not a specific inhibitor of PDK (33), is one member of the growing group of drugs that target metabolism and metabolic efficiency in the normal, stressed, ischemic or ...
We previously found that long-term exposure to fatty acids impairs glucose-induced insulin release. In the present study, we investigated whether impairment is related to decreased pyruvate dehydrogenase (PDH) and increased PDH kinase activity. Rat pancreatic islets were cultured for 48 h in RPMI-1640 medium with or without 0.125 mmol/l palmitate. Potentiation of insulin responses to succinic acid monomethylester (SAM) by 10 mmol/l acetate and pyruvate were subsequently compared in order to assess whether generation of acetyl-coenzyme A (CoA) from pyruvate was deficient in the intact β-cell. Potentiation by acetate was similar in control and palmitate-preexposed islets. In contrast, pyruvate potentiated SAM-induced response by 122% in control but by only 39% in palmitate-exposed islets (P , 0.001). In extracts of palmitate-exposed islets, the active (unphosphorylated) form of PDH was decreased by 50% and total PDH activity (assessed after phosphatase treatment) by 25%. The proportion of active ...
Buy Pdk4 recombinant protein, [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 4, mitochondrial (Pdk4), partial Recombinant Protein-NP_038771.1 (MBS1216721) product datasheet at MyBioSource, Recombinant Proteins
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While the pathologic mechanisms responsible for organ-specific tissue damage in primary biliary cirrhosis (PBC) remain an enigma, it has been suggested that the pathology is mediated by autoreactive T cells infiltrating the intrahepatic bile ducts. Previously, we have documented that there is 100-fold enrichment in the frequency of CD4+ autoreactive T cells in the liver that are specific for peptides encoded by the E2 components of the pyruvate dehydrogenase complexes (PDC-E2). We have also recently characterized the first MHC class I-restricted epitope for PDC-E2, namely amino acid 159-167, a region very similar to the epitope recognized by MHC class II-restricted CD4+ cells and by autoantibodies. The effector functions of these PDC-E2159-167-specific CD8+ cytotoxic T lymphocytes (CTLs) are not well understood. We have taken advantage of tetramer technology and report herein that there is tenfold increase in the frequency of PDC-E2159-167-specific CTLs in the liver as compared with the blood in ...
In the present study, levels of IMAC were assessed noninvasively in skeletal muscle of individuals with type 1 diabetes in euglycemia and hyperglycemia before and after moderate aerobic exercise. The principal finding was a significantly higher increase in IMAC in euglycemia than in hyperglycemia.. The effect of euglycemia and hyperglycemia on exercise-related substrate oxidation has also been assessed in healthy individuals (8), however, without determination of IMAC. Still, previous reports do not suggest genuinely different levels of acylated carnitine in patients with type 1 diabetes compared with nondiabetic control subjects (2). Conversely, a recent study in patients with type 1 diabetes investigated levels of IMAC during exercise in euglycemia but with differing insulin levels (9). The authors reported a similar increase in IMAC in euglycemia and hyperinsulinemia, implying that the flux through the pyruvate dehydrogenase complex (PDC) is independent of insulin concentrations (9). Taken ...
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Macrophage polarization is a process by which macrophages carry out various functional programs responding to signals. Pyruvate Dehydrogenase Kinase (PDK) is a kinase, phosphorylates pyruvate dehydrogenase with ATP to cause…. Read More Read More. ...
Biochemical and structural data for E1s revealed a mechanism of activation of TPP cofactor by forming the conserved hydrogen bond with glutamate residue (Glu59 in human E1) and by imposing a V-conformation that brings the N4 atom of the aminopyrimidine to the distance required for the intramolecular hydrogen bonding with the thiazolium C2 atom. This unique combination of contacts and conformation of TPP leads eventually to formation of the reactive C2-carbanion. After the cofactor TPP reacts with pyruvate, which undergoes decarboxylation, the acetyl portion becomes a hydroxyethyl derivative covalently attached to TPP. In the second reaction, E1 transfers two electrons and the acetyl group to the second substrate, lipoic acid. This reduces the oxidized lipoic acid and transfers the acetyl group to the lipollyl group to form an acetyl thioester. ...
Certain repetitive structures like to fit together, like beta sheets. But theres an additional mechanism to facilitate the evolution of protein-protein interfaces: domain swapping. Suppose a protein domain has an alpha helix (lets say) on its outside. It must fit into an alpha-helix shaped hole, assuming there are no gaps in the hydrophobic core of the domain. But protein molecules are floppy and vibrate in solution. One change of an amino acid facing into the core can destabilize it a little, so now that alpha helix flops around a bit and spends part of its time not fitting into its hole. If another protein of the same type comes along, they both have the same problem, a flopping alpha helix and a hole that fits it. So copy As alpha helix can fit into the helix-shaped hole on copy B, and copy Bs alpha helix can fit into the helix-shaped hole on copy A. Bango, instant binding of two protein molecules. This has been observed, so its not hypothetical ...
Certain repetitive structures like to fit together, like beta sheets. But theres an additional mechanism to facilitate the evolution of protein-protein interfaces: domain swapping. Suppose a protein domain has an alpha helix (lets say) on its outside. It must fit into an alpha-helix shaped hole, assuming there are no gaps in the hydrophobic core of the domain. But protein molecules are floppy and vibrate in solution. One change of an amino acid facing into the core can destabilize it a little, so now that alpha helix flops around a bit and spends part of its time not fitting into its hole. If another protein of the same type comes along, they both have the same problem, a flopping alpha helix and a hole that fits it. So copy As alpha helix can fit into the helix-shaped hole on copy B, and copy Bs alpha helix can fit into the helix-shaped hole on copy A. Bango, instant binding of two protein molecules. This has been observed, so its not hypothetical ...
The skeletal muscle of obese individuals exhibits a depressed ability to metabolize fats. Exercise training is thought to rescue this dampened ability to metabolize fats; mediated by a coordinated increase in the expression of a network of genes that regulate metabolism and fuel utilization. The purpose of this study is to determine the exercise-induced regulation of metabolically important genes in lean and obese individuals. Muscle biopsies (one pre-exercise/baseline and one immediately post-exercise) were obtained from 4 lean (BF% 24.4 ± 5.5; 23.5 yrs ± 1.9) and 13 obese (BF% 39.7 ± 2.4; 26.1 yrs ± 2.3), age-matched, relatively young subjects, free from overt disease, non-smokers, and not taking medications known to alter metabolism. RNA was isolated, quantified, reverse transcribed into cDNA, and evaluated using RT-PCR. The pre-exercise mRNA content of pyruvate dehydrogenase kinase 4 (PDK4) was significantly higher in the obese compared to the lean (P=0.04) and the mRNA content of peroxisome
Lenti ORF particles, Pdk1 (Myc-DDK-tagged) - Mouse pyruvate dehydrogenase kinase, isoenzyme 1 (Pdk1), nuclear gene encoding mitochondrial protein, 200ul, >10^7 TU/mL NM_172665. ...
Studies on patients in the rituximab trial have an energy metabolism deficit, and the key molecule is the enzyme pyruvate dehydrogenase (PDH). Speculate that autoantiboedies may be the cause of this deficit. Upregulation of PDH inhibitors in white blood cells (Norway group - study will finish late 2017 ...
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Compare pyruvate dehydrogenase phosphatase regulatory subunit ELISA Kits from leading suppliers on Biocompare. View specifications, prices, citations, reviews, and more.
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BACKGROUND: Hyperthyroidism increases heart rate, contractility, cardiac output, and metabolic rate. It is also accompanied by alterations in the regulation of cardiac substrate use. Specifically, hyperthyroidism increases the ex vivo activity of pyruvate dehydrogenase kinase, thereby inhibiting glucose oxidation via pyruvate dehydrogenase. Cardiac hypertrophy is another effect of hyperthyroidism, with an increase in the abundance of mitochondria. Although the hypertrophy is initially beneficial, it can eventually lead to heart failure. The aim of this study was to use hyperpolarized magnetic resonance spectroscopy to investigate the rate and regulation of in vivo pyruvate dehydrogenase flux in the hyperthyroid heart and to establish whether modulation of flux through pyruvate dehydrogenase would alter cardiac hypertrophy. METHODS AND RESULTS: Hyperthyroidism was induced in 18 male Wistar rats with 7 daily intraperitoneal injections of freshly prepared triiodothyronine (0.2 mg x kg(-1) x d(-1)). In vivo
Survival during starvation is dependent upon mechanisms that limit oxidative loss of pyruvate in nonneuronal tissues of the body. Pyruvate and other three-carbon compounds that can be converted to glucose must be conserved during starvation. Efficient recycling of these compounds is particularly important in limiting utilization of glucogenic amino acids that otherwise would have to be used to maintain glucose levels during starvation. Limiting amino acid turnover helps keep proteolysis in check and conserves body protein (16,17). Inhibition of pyruvate oxidation is achieved by a combination of regulatory mechanisms that virtually eliminate nonneuronal cell pyruvate dehydrogenase activity during starvation. Most important among these is covalent modification of the complex by phosphorylation. The balance between the relative activities of the PDKs and pPDPs determines the extent to which the complex is inhibited by phosphorylation. It is well established that increased PDK expression in ...
Mutations in the PDHA2 gene have been known to cause one form of pyruvate dehydrogenase deficiency. Pyruvate dehydrogenase deficiency is characterized by the buildup of a chemical called lactic acid in the body and a variety of neurological problems. Signs and symptoms of this condition usually first appear shortly after birth, and they can vary widely among affected individuals. The most common feature is a potentially life-threatening buildup of lactic acid (lactic acidosis), which can cause nausea, vomiting, severe breathing problems, and an abnormal heartbeat. People with pyruvate dehydrogenase deficiency usually have neurological problems as well. Most have delayed development of mental abilities and motor skills such as sitting and walking. Other neurological problems can include intellectual disability, seizures, weak muscle tone (hypotonia), poor coordination, and difficulty walking. Some affected individuals have abnormal brain structures, such as underdevelopment of the tissue ...
TY - JOUR. T1 - Pyruvate-dehydrogenase complex in ataxic patients. T2 - Enzyme deficiency in ataxic encephalopathy plus lactic acidosis and normal activity in Friedreich ataxia. AU - Uziel, G.. AU - Bottacchi, E.. AU - Moschen, G.. AU - Giovanardi-Rossi, P.. AU - Cardace, G.. AU - Di Donato, S.. PY - 1982/12. Y1 - 1982/12. N2 - Pyruvate dehydrogenase complex (PDHC) activity was measured in cultured fibroblasts from 12 patients with Friedreichs ataxia (FA), and in 1 patient with lactic acidosis and ataxia. The activities obtained after extraction of PDHC by different methods were compared. Triton-X-100 extraction yielded enzyme activities 5 to 10 times greater than those obtained with the older methods. With this sensitive technique, PDHC activity was markedly deficient in fibroblasts from the patient with lactic acidosis and ataxia but it was normal in the fibroblasts from FA patients. Mg++activation of the PDHC in FA fibroblasts was normal.. AB - Pyruvate dehydrogenase complex (PDHC) activity ...