Relevant bibliographies by topics / Rat pyruvate dehydrogenase

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Academic literature on the topic 'Rat pyruvate dehydrogenase'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Rat pyruvate dehydrogenase"

1

Mistry, S. C., D. A. Priestman, A. L. Kerbey, and P. J. Randle. "Evidence that rat liver pyruvate dehydrogenase kinase activator protein is a pyruvate dehydrogenase kinase." Biochemical Journal 275, no. 3 (May 1, 1991): 775–79. http://dx.doi.org/10.1042/bj2750775.

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It is shown here that rat liver pyruvate dehydrogenase (PDH) kinase activator protein (KAP) catalyses ATP-dependent inactivation and [32P]phosphorylation of pig heart PDHE1 and of yeast (Saccharomyces cerevisiae) PDH complex devoid of PDH kinase activity, that fluorosulphonylbenzoyladenosine inactivates rat liver KAP and the intrinsic PDH kinase of rat liver PDH complex, and that KAP, like PDH kinase, is inactivated by thiol-reactive reagents. It is concluded that KAP is a free PDH kinase.
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JOHNSON, Sam A., and Richard M. DENTON. "Insulin stimulation of pyruvate dehydrogenase in adipocytes involves two distinct signalling pathways." Biochemical Journal 369, no. 2 (January 15, 2003): 351–56. http://dx.doi.org/10.1042/bj20020920.

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In isolated rat adipocytes, the insulin stimulation of pyruvate dehydrogenase can be partially inhibited by inhibitors of PI3K (phosphoinositide 3-kinase) and MEK1/2 (mitogen-activated protein kinase/extracellular signal-regulated kinase kinase). In combination, U0126 and wortmannin completely block the insulin stimulation of pyruvate dehydrogenase. It is concluded that the effect of insulin on pyruvate dehydrogenase in rat adipocytes involves two distinct signalling pathways: one is sensitive to wortmannin and the other to U0126. The synthetic phosphoinositolglycan PIG41 can activate pyruvate dehydrogenase but the activation is only approx. 30% of the maximal effect of insulin. This modest activation can be completely blocked by wortmannin alone, suggesting that PIG41 acts through only one of the pathways leading to the activation of pyruvate dehydrogenase.
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Carter, Tonia C., and Haldane G. Coore. "Effects of pyruvate on pyruvate dehydrogenase kinase of rat heart." Molecular and Cellular Biochemistry 149-150, no. 1 (August 1995): 71–75. http://dx.doi.org/10.1007/bf01076565.

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4

Curi, R., P. Newsholme, and E. A. Newsholme. "Metabolism of pyruvate by isolated rat mesenteric lymphocytes, lymphocyte mitochondria and isolated mouse macrophages." Biochemical Journal 250, no. 2 (March 1, 1988): 383–88. http://dx.doi.org/10.1042/bj2500383.

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1. The activities of pyruvate dehydrogenase in rat lymphocytes and mouse macrophages are much lower than those of the key enzymes of glycolysis and glutaminolysis. However, the rates of utilization of pyruvate (at 2 mM), from the incubation medium, are not markedly lower than the rate of utilization of glucose by incubated lymphocytes or that of glutamine by incubated macrophages. This suggests that the low rate of oxidation of pyruvate produced from either glucose or glutamine in these cells is due to the high capacity of lactate dehydrogenase, which competes with pyruvate dehydrogenase for pyruvate. 2. Incubation of either macrophages or lymphocytes with dichloroacetate had no effect on the activity of subsequently isolated pyruvate dehydrogenase; incubation of mitochondria isolated from lymphocytes with dichloroacetate had no effect on the rate of conversion of [1-14C]pyruvate into 14CO2, and the double-reciprocal plot of [1-14C]pyruvate concentration against rate of 14CO2 production was linear. In contrast, ADP or an uncoupling agent increased the rate of 14CO2 production from [1-14C]pyruvate by isolated lymphocyte mitochondria. These data suggest either that pyruvate dehydrogenase is primarily in the a form or that pyruvate dehydrogenase in these cells is not controlled by an interconversion cycle, but by end-product inhibition by NADH and/or acetyl-CoA. 3. The rate of conversion of [3-14C]pyruvate into CO2 was about 15% of that from [1-14C]pyruvate in isolated lymphocytes, but was only 1% in isolated lymphocyte mitochondria. The inhibitor of mitochondrial pyruvate transport, alpha-cyano-4-hydroxycinnamate, inhibited both [1-14C]- and [3-14C]-pyruvate conversion into 14CO2 to the same extent, and by more than 80%. 4. Incubations of rat lymphocytes with concanavalin A had no effect on the rate of conversion of [1-14C]pyruvate into 14CO2, but increased the rate of conversion of [3-14C]pyruvate into 14CO2 by about 50%. This suggests that this mitogen causes a stimulation of the activity of pyruvate carboxylase.
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Katz, L. A., A. P. Koretsky, and R. S. Balaban. "Activation of dehydrogenase activity and cardiac respiration: a 31P-NMR study." American Journal of Physiology-Heart and Circulatory Physiology 255, no. 1 (July 1, 1988): H185—H188. http://dx.doi.org/10.1152/ajpheart.1988.255.1.h185.

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31P-NMR studies were performed to determine the tissue phosphate and oxygen consumption effects of known maneuvers on the activation of pyruvate dehydrogenase during work jumps in the perfused rat heart. In control studies of the glucose-perfused heart, work jumps, with pacing, resulted in a 32% increase in oxygen consumption (QO2) from 1.72 +/- 0.09 to 2.29 +/- 0.12 mmol O2.h-1.g dry wt-1. During this transition no significant change in the high energy phosphates were detected. In contrast, work jumps did cause changes in the phosphates when the activation of pyruvate dehydrogenase was blocked with 2.5 micrograms of ruthenium red per milliliter or maximally stimulated with 11 mM pyruvate before the increase in work. The observed increase in QO2 and inorganic phosphate and calculated increase in ADP are consistent with these phosphates controlling mitochondrial respiration under these conditions. These results suggest that the activation of pyruvate dehydrogenase and/or other dehydrogenases may be an important step in the orchestration of work and QO2.
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Kilgour, E., and R. G. Vernon. "Catecholamine activation of pyruvate dehydrogenase in white adipose tissue of the rat in vivo." Biochemical Journal 241, no. 2 (January 15, 1987): 415–19. http://dx.doi.org/10.1042/bj2410415.

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Intraperitoneal injections of noradrenaline or adrenaline into rats increased the proportion of pyruvate dehydrogenase in the active state in white adipose tissue; this effect of catecholamines was also apparent in streptozotocin-diabetic rats, showing that it was not due to an increase in serum insulin concentration. The catecholamine-induced increase in pyruvate dehydrogenase of white adipose tissue in vivo was completely blocked by prior injection of either the beta-antagonist propranolol or the alpha 1-antagonist prazosin. Cervical dislocation of conscious rats increased pyruvate dehydrogenase activity of white adipose tissue, which was prevented by prior injection of propranolol. Adrenaline (30 nM) activated pyruvate dehydrogenase in white adipocytes in vitro; the maximum effect of adrenaline required activation of both alpha 1- and beta-receptors. The results show that catecholamines activate pyruvate dehydrogenase of white adipose tissue both in vivo and in vitro and that this effect is mediated by a combination of alpha 1- and beta-adrenergic receptors.
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7

McCormack, J. G., E. A. Longo, and B. E. Corkey. "Glucose-induced activation of pyruvate dehydrogenase in isolated rat pancreatic islets." Biochemical Journal 267, no. 2 (April 15, 1990): 527–30. http://dx.doi.org/10.1042/bj2670527.

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1. Rat pancreatic islets were isolated and then maintained in culture for 2-4 days before being incubated in groups of 100 in the presence of different glucose (0-20 mM) or CaCl2 (1.2-4.2 mM) concentrations, or with uncoupler. 2. Increases in extracellular glucose concentration resulted in increases in the amount of active, non-phosphorylated, pyruvate dehydrogenase in the islets, with half-maximal effects around 5-6 mM-glucose. Increasing extracellular glucose from 3 to 20 mM resulted in a 4-6-fold activation of pyruvate dehydrogenase within 2 min. 3. The total enzyme activity was unchanged, and averaged 0.4 m-unit/100 islets at 37 degrees C. 4. These changes in active pyruvate dehydrogenase were broadly similar to changes in insulin secretion by the islets. 5. Increasing extracellular Ca2+ or adding uncoupler also activated pyruvate dehydrogenase to a similar degree, but only the former was associated with increased insulin secretion.
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8

De Marcucci, O. L., A. Hunter, and J. G. Lindsay. "Low immunogenicity of the common lipoamide dehydrogenase subunit (E3) of mammalian pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase multienzyme complexes." Biochemical Journal 226, no. 2 (March 1, 1985): 509–17. http://dx.doi.org/10.1042/bj2260509.

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The production of high-titre monospecific polyclonal antibodies against the purified pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase multienzyme complexes from ox heart is described. The specificity of these antisera and their precise reactivities with the individual components of the complexes were examined by immunoblotting techniques. All the subunits of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes were strongly antigenic, with the exception of the common lipoamide dehydrogenase component (E3). The titre of antibodies raised against E3 was, in both cases, less than 2% of that of the other subunits. Specific immunoprecipitation of the dissociated N-[3H]ethylmaleimide-labelled enzymes also revealed that E3 alone was absent from the final immune complexes. Strong cross-reactivity with the enzyme present in rat liver (BRL) and ox kidney (NBL-1) cell lines was observed when the antibody against ox heart pyruvate dehydrogenase was utilized to challenge crude subcellular extracts. The immunoblotting patterns again lacked the lipoamide dehydrogenase band, also revealing differences in the apparent Mr of the lipoate acetyltransferase subunit (E2) from ox kidney and rat liver. The additional 50 000-Mr polypeptide, previously found to be associated with the pyruvate dehydrogenase complex, was apparently not a proteolytic fragment of E2 or E3, since it could be detected as a normal component in boiled sodium dodecyl sulphate extracts of whole cells. The low immunogenicity of the lipoamide dehydrogenase polypeptide may be attributed to a high degree of conservation of its primary sequence and hence tertiary structure during evolution.
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Priestman, David A., Sharad C. Mistry, Alan L. Kerbey, and Philip J. Randle. "Purification and partial characterization of rat liver pyruvate dehydrogenase kinase activator protein (free pyruvate dehydrogenase kinase)." FEBS Letters 308, no. 1 (August 10, 1992): 83–86. http://dx.doi.org/10.1016/0014-5793(92)81056-r.

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10

Schadewaldt, P., E. Lammers, and W. Staib. "Influence of insulin and glucose on pyruvate catabolism in perfused rat hindlimbs." Biochemical Journal 227, no. 1 (April 1, 1985): 177–82. http://dx.doi.org/10.1042/bj2270177.

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The effects of insulin and glucose on the oxidative decarboxylation of pyruvate in isolated rat hindlimbs was studied in non-recirculating perfusion with [1-14C]pyruvate. Insulin increased the calculated pyruvate decarboxylation rate in a concentration-dependent manner. At supramaximal insulin concentrations, the calculated pyruvate decarboxylation rate was increased by about 40% in perfusions with 0.15-1.5 mM-pyruvate. Glucose up to 20 mM had no effect. In the presence of insulin and low physiological pyruvate concentrations (0.15 mM), glucose increased the calculated pyruvate oxidation. This effect was abolished by high concentrations of pyruvate (1 mM). The data provide evidence that in resting perfused rat skeletal muscle insulin primarily increased the activity of the pyruvate dehydrogenase complex. The effect of glucose was due to increased intracellular pyruvate supply.
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Dissertations / Theses on the topic "Rat pyruvate dehydrogenase"

1

Denyer, G. "Regulation of hepatic pyruvate dehydrogenase complex by reversible phosphorylation." Thesis, University of Oxford, 1987. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.233529.

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Peters, Sandra Jane. "Dietary regulation of rat and human skeletal muscle pyruvate dehydrogenase kinase activity." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2001. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp04/NQ56290.pdf.

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Blann, Lara S. R. "The development of pyruvate dehydrogenase in the rat heart and liver during the suckling weaning transition." Thesis, University of Surrey, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.386947.

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Wesso, Iona. "An investigation of the effects of donor age on some haematological characteristics of the Wistar rat (Rattus Norwegicus)." University of the Western Cape, 1986. http://hdl.handle.net/11394/8484.

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>Magister Scientiae - MSc
Knowledge of haematological 'normdata', of experimental animals, and the biological variables that affect it is essential in order to recognise variations from the normal. In addition, the haemopoietic system may be regarded in principle as good material for studies of the cellular events associated with ageing. These considerations, together with the well documented effects of age on various physiological processes, prompted an investigation into the effects of donor age on several blood parameters. Review of the literature revealed that age-related changes in blood parameters have been reported for several species, but the documentation thereof is incomplete, inconsistent and inconclusive in many respects. Blood samples from male Wistar rats of nine different biological ages, ranging from birth to 96 weeks of age, were analysed for haematological and biochemical parameters. These included the blood cell counts, erythrocytic indices, haemoglobin concentration, haematocrit, erythrocytic 2,3-diphosphoglycerate and adenosine triphosphate levels, and erythrocytic glucose 6-phosphate dehydrogenase and pyruvate kinase activities. Data was obtained which demonstrates that all blood parameters measured underwent significant, although not al~ays regular, age-related changes. These changes were found to be more marked during the first month of life than at any other period. Evidence is also presented to show that the depressed haemoglobin concentration during the early postnatal life may not imply a condition of 'physiologic anaemia' as was previously thought. Since the blood profile exhibits only slight changes from about 24 weeks of age, it does not seem that the haemopoietic system of the old rat deteriorates significantly as to constitute a limiting factor for the animal's life. However, the importance of taking an animal's age into account when blood parameters constitute experimental results is emphasised. The second phase of this study involved a detailed investigation of the effect of the animal's age on erythrocytes in particular. These cells have limited life-spans, and are often used as models in studies of cellular ageing. Special emphasis was therefore placed on comparing the relative effects of host and cellular ageing on the properties of these cells. Erythrocytes from rats between one and 48 weeks of age were separated into two populations by a modification of the conventional density gradient centrifugation technique. The two populations were assumed to differ in mean cell age and were analysed for erythrocytic indices, phosphate ester concentrations and the activities of glucose 6-phosphate dehydrogenase and pyruvate kinase. Evidence is presented to show that ageing rat erythrocytes exhibit a decrease in volume, phosphate ester content and enzyme activities while the cellular haemoglobin concentration increases. Differences in the mean cell age however, does not seem to account for the donor-age-related effects observed in the whole blood parameters. Rather, the significant differences found in the characteristics of similarly aged red cells, between variously aged donors, demonstrate that the biological age of the organism influences the red cells and probably the ageing thereof in vivo. The contribution of the changing status of the erythrocyte's environment of progressively older animals, to alterations which take place in the ageing red cell is discussed.
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Khoza, Thandeka. "Characterization of the interaction between rat pyruvate dehydrogenase kinase 4 and adp." Thesis, 2009. http://hdl.handle.net/10539/6978.

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The primary role of pyruvate dehydrogenase kinase (PDK) is to regulate the activity of pyruvate dehydrogenase complex (PDC) with respect to the metabolic clearance of glucose via a phosphorylation mechanism. Therefore, inhibition of PDK is predicted to be important in the treatment of diabetes. ADP binds to the active site of PDK; and has been shown to inhibit PDK activity. This research work was aimed at studying one of the isoforms of PDK, specifically the rodent form, PDK4 (rPDK4) and further elucidating the binding properties of ADP to rPDK4. The hypothetical structure of rPDK4 was modelled based on the coordinates of the published rPDK2 structure. The overall structural topology of rPDK2 appears to be preserved in rPDK4. Further, the ADP binding site between rPDK2 and rPDK4 was conserved at both the primary and tertiary level, and this suggested the mechanism of ADP binding to rPDK2 would be similar to that of rPDK4. A histidine tagged-rPDK4 protein was expressed and purified using affinity and gel filtration chromatography. It was determined to be a homodimer (97 kDa) comprising two identical subunits. The rPDK4 protein was further identified to be rPDK4 using Western blot analysis as it reacted positively with an anti-rPDK4 monoclonal antibody. The purified rPDK4 protein contained kinase activity since it was able to undergo autophosphorylation and subsequently phosphorylate a peptide that contained the E1a subunit sites that are known to be phosphorylated by PDKs. The structure of rPDK4 protein was also characterised using circular dichroism and fluorescence spectroscopy.The spectroscopic data of rPDK4 was consistent with published data on the structure of rPDK4. The binding of ADP and ATP was studied using fluorescence quenching as both these ligands quench the intrinsic tryptophan fluorescence of rPDK4. The dissociation constant (Kd) values for ADP and ATP were determined to be 37 and 17.4 μM, respectively. The moderate affinity binding of ATP will greatly favour the exchange of ADP for a molecule of ATP to prevent PDK inhibition by ADP.
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Book chapters on the topic "Rat pyruvate dehydrogenase"

1

Carter, Tonia C., and Haldane G. Coore. "Effects of pyruvate on pyruvate dehydrogenase kinase of rat heart." In Signal Transduction Mechanisms, 71–75. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-2015-3_8.

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2

Cockburn, Brian N., and Haldane G. Coore. "Starvation reduces pyruvate dehydrogenase phosphate phosphatase activity in rat kidney." In Signal Transduction Mechanisms, 131–36. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-2015-3_14.

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