scholarly journals The effects of glucose, acetate, lactate and insulin on protein degradation in the perfused rat heart

1982 ◽  
Vol 206 (3) ◽  
pp. 467-472 ◽  
Author(s):  
P H Sugden ◽  
D M Smith
Keyword(s):  
Protein Degradation ◽  
Rat Heart ◽  
Plasma Concentrations ◽  
Normal Range ◽  
Perfused Rat Heart ◽  
Rat Hearts ◽  
Insulin Inhibition

Rat hearts were perfused as working preparations by the method of Taegtmeyer, Hems & Krebs [(1980 Biochem. J. 186, 701-711]. In the presence of glucose, insulin significantly inhibited protein degradation at concentrations as low as 50 mu units/ml. Acetate or lactate, when present either as sole fuel for contraction or in combination with glucose, did not inhibit protein degradation. Insulin inhibition or protein degradation was decreased with either lactate as sole fuel. We suggest that the inhibition of protein degradation occurs over the normal range of plasma concentrations of insulin present in vivo and that the presence of glucose may be at least in part necessary for this effect of insulin.

scholarly journals The release of 3′:5′-cyclic monophosphate from the isolated perfused rat heart

1975 ◽  
Vol 152 (2) ◽  
pp. 429-432 ◽  
Author(s):  
John A. O'Brien ◽  
Richard C. Strange
Keyword(s):  
Cyclic Amp ◽  
Rat Heart ◽  
Perfused Rat Heart ◽  
Cyclic Monophosphate ◽  
Isolated Perfused Rat Heart ◽  
Rat Hearts ◽  
Basal Release ◽  
Perfused Rat Hearts ◽  
Isolated Perfused Rat Hearts

Although basal release of cyclic AMP from isolated perfused rat hearts was not measurable, isoprenaline induced substantial release of the nucleotide, suggesting that in vivo the myocardium can contribute to plasma cyclic AMP. Anoxia also increased the amount of cyclic AMP released, but insulin and nicotinate alone or in combination had no effect.

Effect of redox potential on protein degradation in perfused rat heart

1985 ◽  
Vol 248 (6) ◽  
pp. E726-E731
Author(s):  
B. H. Chua ◽  
B. J. Kleinhans
Keyword(s):  
Energy Source ◽  
Redox Potential ◽  
Protein Degradation ◽  
Rat Heart ◽  
Redox State ◽  
Inhibitory Effect ◽  
Experimental Conditions ◽  
Perfused Rat Heart ◽  
Rat Hearts ◽  
Sole Energy

The effect of redox potential on protein degradation was assessed in rat hearts supplied either glucose or pyruvate, and the correlation between redox state and proteolysis was examined after the addition of insulin and leucine. In hearts supplied glucose as the sole energy source, the inhibition of protein degradation by a range of concentrations of insulin was associated with increased ratios of perfusate lactate to pyruvate and intracellular lactate to pyruvate, malate to pyruvate, and NADH to NAD. However, the extent of inhibition did not correlate with the redox state. The inhibitory effect of leucine on protein degradation was not accompanied by any change in redox state of the hearts. In hearts provided with pyruvate, rates of protein degradation continued to be inhibited by insulin even though the perfusate lactate to pyruvate was decreased by 14-fold and the calculated cytosolic NADH-to-NAD ratios were only 3% of those seen in hearts supplied glucose. These results indicated that a correlation between redox state and protein degradation was not apparent in myocardium under the experimental conditions examined.

Reduced high-energy phosphate levels in rat hearts. I. Effects of alloxan diabetes

1976 ◽  
Vol 230 (6) ◽  
pp. 1744-1750 ◽  
Author(s):  
TB Allison ◽  
SP Bruttig ◽  
Crass MF ◽  
RS Eliot ◽  
JC Shipp
Keyword(s):  
Oxidative Metabolism ◽  
Oxygen Delivery ◽  
Rat Heart ◽  
High Energy ◽  
Diabetic Rat ◽  
High Energy Phosphate ◽  
Atp Production ◽  
Rat Hearts

Significant alterations in heart carbohydrate and lipid metabolism are present 48 h after intravenous injection of alloxan (60 mg/kg) in rats. It has been suggested that uncoupling of oxidative phosphorylation occurs in the alloxanized rat heart in vivo, whereas normal oxidative metabolism has been demonstrated in alloxan-diabetic rat hearts perfused in vitro under conditions of adequate oxygen delivery. We examined the hypothesis that high-energy phosphate metabolism might be adversely affected in the alloxan-diabetic rat heart in vivo. Phosphocreatine and ATP were reduced by 58 and 45%, respectively (P is less than 0.001). Also, oxygen-dissociation curves were shifted to the left by 4 mmHg, and the rate of oxygen release from blood was reduced by 21% (P is less than 0.01). Insulin administration normalized heart high-energy phosphate compounds. ATP production was accelerated in diabetic hearts perfused in vitro with a well-oxygenated buffer. These studies support the hypothesis that oxidative ATP production in the alloxan-diabetic rat heart is reduced and suggest that decreased oxygen delivery may have a regulatory role in the oxidative metabolism of the diabetic rat heart.

Leucine as a regulator of whole body and skeletal muscle protein metabolism in humans

1992 ◽  
Vol 263 (5) ◽  
pp. E928-E934 ◽  
Author(s):  
K. S. Nair ◽  
R. G. Schwartz ◽  
S. Welle
Keyword(s):  
Amino Acids ◽  
Protein Degradation ◽  
Protein Metabolism ◽  
Muscle Protein ◽  
Plasma Concentrations ◽  
Essential Amino Acids ◽  
Whole Body ◽  
Skeletal Muscle Protein ◽  
Muscle Protein Metabolism

Leucine has been proposed as an in vivo regulator of protein metabolism, although the evidence for this in humans remains inconclusive. To test this hypothesis, we infused either L-leucine (154 +/- 1 mumol.kg-1 x h-1) or saline intravenously in six healthy men in two separate studies. L-Leucine infusion increased plasma concentrations of leucine and alpha-ketoisocaproate from 112 +/- 6 and 38 +/- 3 mumol/l to 480 +/- 27 (P < 0.001) and 94 +/- 13 mumol/l (P < 0.001), respectively, without any significant change in circulating insulin or C peptide levels. Leucine infusion decreased plasma concentrations of several amino acids and decreased whole body valine flux and valine oxidation (using L-[1-13C]valine as a tracer) and phenylalanine flux (using [2H5]-phenylalanine as a tracer). According to arteriovenous differences across the leg, the net balance of phenylalanine, valine, and lysine shifted toward greater retention during leucine infusion, whereas alanine balance did not change. Valine release and phenylalanine release from the leg (estimated from the dilution of respective tracers) decreased, indicating inhibition of protein degradation by leucine infusion. We conclude that leucine decreases protein degradation in humans and that this decreased protein degradation during leucine infusion contributes to the decrease in plasma essential amino acids. This study suggests a potential role for leucine as a regulator of protein metabolism in humans.

scholarly journals The discovery of a rapidly metabolized polymeric tetraphosphate derivative of adenosine in perfused rat heart

1984 ◽  
Vol 223 (3) ◽  
pp. 627-632 ◽  
Author(s):  
J Mowbray ◽  
W L Hutchinson ◽  
G R Tibbs ◽  
P G Morris
Keyword(s):  
Organic Acid ◽  
Rat Heart ◽  
Purine Nucleoside ◽  
Acid Phosphate ◽  
Perfused Rat Heart ◽  
Rat Hearts ◽  
Adenosine Phosphate ◽  
Perfused Rat Hearts ◽  
Radioactive Labelling

The predicted presence in perfused rat hearts of a rapidly metabolized but hitherto unrecognized form of adenosine phosphate has been confirmed by specific radioactive labelling. The properties of the purified compound suggest that it is a heteropolymer of a small organic acid, phosphate and purine nucleoside in the proportions 1:4:1.

Metabolic inhibition in the perfused rat heart: evidence for glycolytic requirement for normal sodium homeostasis

1998 ◽  
Vol 274 (4) ◽  
pp. H1082-H1089 ◽  
Author(s):  
José Dizon ◽  
Daniel Burkhoff ◽  
Joseph Tauskela ◽  
John Whang ◽  
Paul Cannon ◽  
...  
Keyword(s):  
Oxidative Metabolism ◽  
Rat Heart ◽  
High Energy ◽  
Shift Reagent ◽  
Resonance Spectroscopy ◽  
High Energy Phosphate ◽  
Perfused Rat Heart ◽  
Rat Hearts ◽  
Rapid Pacing ◽  
Subcellular Compartmentalization

Subcellular compartmentalization of energy stores to support different myocardial processes has been exemplified by the glycolytic control of the ATP-sensitive K+ channel. Recent data suggest that the control of intracellular sodium (Nai) may also rely on glycolytically derived ATP; however, the degree of this dependence is unclear. To examine this question, isolated, perfused rat hearts were exposed to hypoxia, to selectively inhibit oxidative metabolism, or iodoacetate (IAA, 100 μmol/l), to selectively inhibit glycolysis. Nai and myocardial high-energy phosphate levels were monitored using triple-quantum-filtered (TQF)23Na and31P magnetic resonance spectroscopy, respectively. The effects of ion exchange mechanisms (Na+/Ca2+, Na+/H+) on Nai were examined by pharmacological manipulation of these channels. Nai, as monitored by shift reagent-aided TQF 23Na spectral amplitudes, increased by ∼220% relative to baseline after 45 min of perfusion with IAA, with or without rapid pacing. During hypoxia, Nai increased by ∼200% during rapid pacing but did not increase in unpaced hearts or when the Na+/H+exchange blocker ethylisopropylamiloride (EIPA, 10 μmol/l) was used. Neither EIPA nor a low-Ca2+perfusate (50 μmol/l) could prevent the rise in Nai during perfusion with IAA. Myocardial function and high-energy phosphate stores were preserved during inhibition of glycolysis with IAA and continued oxidative metabolism. These results suggest that glycolysis is required for normal Na+ homeostasis in the perfused rat heart, possibly because of preferential fueling of Na-K-adenosinetriphosphatase by glycolytically derived ATP.

scholarly journals Measurement of oxidized glutathione and total glutathione in the perfused rat heart

1970 ◽  
Vol 117 (4) ◽  
pp. 661-665 ◽  
Author(s):  
P. L. Wendell
Keyword(s):  
Glutathione Reductase ◽  
Rat Heart ◽  
Enzyme Reaction ◽  
Heart Tissue ◽  
Oxidized Glutathione ◽  
Total Glutathione ◽  
Perfused Rat Heart ◽  
Rat Hearts

1. A method was developed for the assay of GSSG in heart tissue. 2. GSSG and total glutathione were measured in rat hearts perfused under a variety of conditions. About 2% of the total glutathione is present as GSSG. The concentrations of GSSG and GSH remained constant under all the conditions tested. 3. These results are discussed with reference to the equilibrium and rate of the glutathione reductase reaction in the cell. It is concluded that the enzyme reaction does not lie near equilibrium.

scholarly journals Contrasting response of protein degradation to starvation and insulin as measured by release of Nτ-methylhistidine or phenylalanine from the perfused rat heart

1986 ◽  
Vol 237 (2) ◽  
pp. 391-395 ◽  
Author(s):  
D M Smith ◽  
P H Sugden
Keyword(s):  
Protein Degradation ◽  
Rat Heart ◽  
Isotope Dilution Method ◽  
Dilution Method ◽  
Intracellular Protein ◽  
Perfused Rat Heart ◽  
Fractional Rate ◽  
Degradation Rates ◽  
Actin Degradation ◽  
Mixed Protein

An isotope-dilution method is described for the measurement of N tau-methylhistidine release from the perfused rat heart. We argue that release of N tau-methylhistidine is indicative of cardiac actin degradation. N tau-Methylhistidine release is compared with phenylalanine release in the presence of cycloheximide (phenylalanine release being a measure of degradation of mixed proteins). In hearts perfused with glucose plus acetate, the rate of actin degradation was increased by starvation and was not inhibited by insulin. In contrast, the rate of mixed-protein degradation was decreased by starvation and was inhibited by insulin. The fractional rate of degradation of mixed proteins in hearts from fed or starved rats was greater than that for actin. It is suggested that there are at least two pools of intracellular protein, the degradation rates of which differ in terms of their response to insulin and starvation.

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