ATP‐dependent inactivation of heart muscle pyruvate dehydrogenase and reactivation by Mg<sup>++</sup>

Wieland, O.; Jagow-Westermann, Bärbel

doi:10.1016/0014-5793(69)80156-0

Cited by 81 publications

(17 citation statements)

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“…If this is so, counter-exchange of pyruvate and 3-hydroxybutyrate across the mitochondrial membrane may explain the sparing effect of ketone bodies on glucose utilisation in peripheral tissues, since expulsion of pyruvate would lead to inhibition of the pyruvate dehydrogenase complex. The proportion of this complex in the active (dephospho) form appears to depend on the supply of pyruvate [ 141, possibly because pyruvate protects the complex from kinase attack [15,16]. Incubation of whole rat liver mitochondria with pyruvate has been shown to lead to activation of pyruvate dehydrogenase: also palmityl carnitine and 3-hydroxybutyrate can reverse this effect [ 171.…”

Section: Oxygen Electrode Studiesmentioning

confidence: 99%

Evidence for the role of a specific monocarboxylate transporter in the control of pyruvate oxidation by rat liver mitochondria

Mowbray

1974

FEBS Letters

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Section: Oxygen Electrode Studiesmentioning

confidence: 99%

Evidence for the role of a specific monocarboxylate transporter in the control of pyruvate oxidation by rat liver mitochondria

Mowbray

1974

FEBS Letters

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“…We will further discuss the PDHK and PDHP system in the kinase/phosphatases discussion below. Readers interested in this specific system are referred to the original papers (60,102,123,219,220) as well as the several reviews available on this topic (59,133). Since quantitative measures are one of the focuses of this review, it is interesting to note that Boja et al (24) performed one of the first quantitative MS studies on PDH phosphorylation in isolated heart mitochondria.…”

Section: Phosphorylation Of the Enzymes Of Intermediary Metabolismmentioning

confidence: 99%

“…Protein phosphorylation of mitochondrial PDH, described almost simultaneously by Linn et al (123) and Weiland and colleagues (219,220), was one of the first examples of metabolic control by enzyme phosphorylation. This discovery and the previously described regulation of GP by protein phosphorylation (114) were two of the early examples of acute modulation of enzyme activity by protein phosphorylation events [see the early review (194)], and both of these reactions are important for cardiac energy conversion.…”

Section: Introductionmentioning

confidence: 98%

Cardiac mitochondrial matrix and respiratory complex protein phosphorylation

Covián

Balaban

2012

American Journal of Physiology-Heart and Circulatory Physiology

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Covian R, Balaban RS. Cardiac mitochondrial matrix and respiratory complex protein phosphorylation. Am J Physiol Heart Circ Physiol 303: H940 -H966, 2012. First published August 10, 2012; doi:10.1152/ajpheart.00077.2012.-It has become appreciated over the last several years that protein phosphorylation within the cardiac mitochondrial matrix and respiratory complexes is extensive. Given the importance of oxidative phosphorylation and the balance of energy metabolism in the heart, the potential regulatory effect of these classical signaling events on mitochondrial function is of interest. However, the functional impact of protein phosphorylation and the kinase/phosphatase system responsible for it are relatively unknown. Exceptions include the well-characterized pyruvate dehydrogenase and branched chain ␣-ketoacid dehydrogenase regulatory system. The first task of this review is to update the current status of protein phosphorylation detection primarily in the matrix and evaluate evidence linking these events with enzymatic function or protein processing. To manage the scope of this effort, we have focused on the pathways involved in energy metabolism. The high sensitivity of modern methods of detecting protein phosphorylation and the low specificity of many kinases suggests that detection of protein phosphorylation sites without information on the mole fraction of phosphorylation is difficult to interpret, especially in metabolic enzymes, and is likely irrelevant to function. However, several systems including protein translocation, adenine nucleotide translocase, cytochrome c, and complex IV protein phosphorylation have been well correlated with enzymatic function along with the classical dehydrogenase systems. The second task is to review the current understanding of the kinase/phosphatase system within the matrix. Though it is clear that protein phosphorylation occurs within the matrix, based on 32 P incorporation and quantitative mass spectrometry measures, the kinase/phosphatase system responsible for this process is ill-defined. An argument is presented that remnants of the much more labile bacterial protein phosphoryl transfer system may be present in the matrix and that the evaluation of this possibility will require the application of approaches developed for bacterial cell signaling to the mitochondria.kinase; phosphatase; citric acid cycle; oxidative phosphorylation; protein transport; mitochondria intermembrane space; phosphohistidine; adenine nucleotide translocase; pyruvate dehydrogenase; branched chain ␣-ketoacid dehydrogenase THIS REVIEW ARTICLE is part of a collection on Post-translational Protein Modification in Metabolic Stress. Other articles appearing in this collection, as well as a full archive of all Review collections, can be found online at http://ajpheart. physiology.org/.

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“…The responsible enzyme, the pyruvate dehydrogenase (PDH, EC 1.2.4.1) complex is regulated by either feedback control by acetyl-CoA and NADH [1,2] or by enzymatic phosphorylation and dephosphorylation reactions leading to the inactive form (PDHb) or the active form (PDHa) , respectively [3,4]. Previous work from this laboratory had shown that in heart muscle of normal fed rats about two-thirds of total PDH activity was found as PDH a whereas only about one tenth of total activity was found as PDH a in starved or ketoacidotic alloxan diabetic animals.…”

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confidence: 99%

The effect of insulin on pyruvate dehydrogenase interconversion in heart muscle of alloxan-diabetic rats

Öhlén¹,

Siess²,

Löffler³

et al. 1978

Diabetologia

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Summary.Evidence is presented for regulation by insulin of pyruvate dehydrogenase (PDH) interconversion in rat heart muscle in vivo and in vitro. In the alloxan diabetic rat the active (dephospho) enzyme amounted only to 12% of total PDH and was restored to 42% by insulin. Antilipolytic treatment of the diabetic animals was ineffective, indicating that the action of insulin was independent of a lowering of plasma non-esterified fatty acid concentration. On perfusion of isolated hearts from diabetic rats in the presence of glucose the proportion of pyruvate dehydrogenase in the active form remained low but was fully restored upon addition of insulin (2 mU/ml) to the medium. No effect of insulin was obtained in the absence of glucose. The correlation between the rate of pyruvate decarboxylation in the perfused heart and of pyruvate dehydrogenase activity, in vitro, suggests that in the diabetic heart the entry of pyruvate into the citric acid cycle is largely controlled by covalent modification of the pyruvate dehydrogenase complex rather than by feedback inhibition. The possible role of insulin therein is discussed.

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ATP‐dependent inactivation of heart muscle pyruvate dehydrogenase and reactivation by Mg⁺⁺

Cited by 81 publications

References 2 publications

Evidence for the role of a specific monocarboxylate transporter in the control of pyruvate oxidation by rat liver mitochondria

Evidence for the role of a specific monocarboxylate transporter in the control of pyruvate oxidation by rat liver mitochondria

Cardiac mitochondrial matrix and respiratory complex protein phosphorylation

The effect of insulin on pyruvate dehydrogenase interconversion in heart muscle of alloxan-diabetic rats

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ATP‐dependent inactivation of heart muscle pyruvate dehydrogenase and reactivation by Mg++

Cited by 81 publications

References 2 publications

Evidence for the role of a specific monocarboxylate transporter in the control of pyruvate oxidation by rat liver mitochondria

Evidence for the role of a specific monocarboxylate transporter in the control of pyruvate oxidation by rat liver mitochondria

Cardiac mitochondrial matrix and respiratory complex protein phosphorylation

The effect of insulin on pyruvate dehydrogenase interconversion in heart muscle of alloxan-diabetic rats

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ATP‐dependent inactivation of heart muscle pyruvate dehydrogenase and reactivation by Mg⁺⁺