Metabolism of the human heart

Bing, Richard J.; Siegel, A.; Ungar, I; Gilbert, Mads

doi:10.1016/0002-9343(54)90365-4

Cited by 410 publications

(86 citation statements)

References 27 publications

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“…There have been a number of studies on the control mechanisms regulating fatty acid oxidation in the myocardium (Bing et al, 1954;Bing, 1965;Opie, 1968Opie, , 1969a. Since the membrane transport of fatty acids can be viewed as more or less a physicochemical process (Opie, 1969a,b;Neely & Morgan, 1974), the intracellular availability of fatty acids and fatty acyl-CoA esters plays a dominant role in governing the rate of fatty acid oxidation in the ventricle (Randle et al, 1966;Oram et al, 1973;Neely & Morgan, 1974).…”

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confidence: 99%

Phosphatidate phosphohydrolase and palmitoyl-coenzyme A hydrolase in cardiac subcellular fractions of hyperthyroid rabbits and cardiomyopathic hamsters

Kako

Patterson

1975

Biochemical Journal

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Activities of phosphatidate phosphohydrolase and palmitoyl-CoA hydrolase were determined in cardiac subcellular fractions prepared from rabbits which had received tri-iodothyronine and from hamsters with hereditary cardiomyopathy (strain BIO 14.6). 1. Both mitochondrial and microsomal fractions of hyperthyroid rabbit hearts produced 4-5 times as much diacylglycerol 3-phosphate from glycerol 3-phosphate and palmitate as did those of euthyroid hearts. 2. Phosphatidate phosphohydrolase, measured with phosphatidate emulsion, was activated by 1 mM-Mg2+ in all but the mitochondrial fraction of euthyroid rabbit hearts. The activation was more pronounced in subcellular fractions isolated from hyperthyroid hearts, so that the measured activities were significantly increased above those of the controls. The highest activity was found in the microsomal and lysosomal fractions. 3. In the absence of Mg2+ during incubation, the difference in phosphohydrolase activities between eu-and hyper-thyroid states was not significant. 4. The phosphohydrolase of subcellular fractions of control hamsters did not respond to addition of 0.5-8.0mM-Mg2+. The enzyme from cardiomyopathic hearts was slightly inhibited by this bivalent cation and therefore significant increases in activity were observed only in the absence of Mg2+ from the assay system. 5. The rate of reaction by soluble phosphatidate phosphohydrolase was similar regardless of the nature of the substrate. Both when microsomal-bound phosphatidate was used as the substrate and when phosphatidate suspension was used, the activity of soluble enzyme was lower than that of the microsomal and lysosomal enzymes measured with phosphatidate suspension; this was especially so when the assay was carried out in the absence of Mg2+. Neither tri-iodothyronine nor cardiomyopathy influenced the soluble phosphohydrolase activity in the two species. 6. Neither tri-iodothyronine nor cardiomyopathy significantly changed palmitoyl-CoA hydrolase activities in subcellular fractions. 7. Microsomal diacylglycerol acyltransferase and myocardial triacylglycerol content were also unchanged in the hyperthyroid state.

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confidence: 99%

Phosphatidate phosphohydrolase and palmitoyl-coenzyme A hydrolase in cardiac subcellular fractions of hyperthyroid rabbits and cardiomyopathic hamsters

Kako

Patterson

1975

Biochemical Journal

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“…As an energy producing organelle, the mitochondria encompasses about 1/3 of the cellular volume in cardiomyocytes (Schaper et al, 1985). Mitochondrial fatty acid and glucose oxidation represent the major sources of ATP generation in healthy hearts (Bing et al, 1954;Taegtmeyer, 1994;Stanley and Chandler, 2002). Although increased mitochondrial respiratory activity is observed during the early stages of cardiac hypertrophy, the oxidative phosphorylation rate decreases upon progression to decompensated hypertrophy or HF (Lindenmayer et al, 1971;Sordahl et al, 1973).…”

Section: Role Of Sirt3 In Ameliorating Cardiac Hypertrophymentioning

confidence: 99%

Roles of SIRT3 in heart failure: from bench to bedside

Liu

Song

et al. 2016

J. Zhejiang Univ. Sci. B

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Heart failure (HF) represents the most common endpoint of most cardiovascular diseases (CVDs) which are the leading causes of death around the world. Despite the advances in treating CVDs, the prevalence of HF continues to increase. It is believed that better results of prognosis are obtained from prevention rather than additional treatment for HF. Therefore, it is reasonable to prevent the development of CVDs or other complications to HF. Most types of HF are attributed to contractile dysfunction, cardiac hypertrophy or remodeling, and ischemic injuries. SIRT3 is a mitochondrial nicotinamide adenine dinucleotide (NAD + )-dependent deacetylase whose substrates vary from metabolic biogenesis-associated proteins to stress-responsive proteins. In recent years, a number of studies have highlighted the cardio-protective role of SIRT3 and, as such, efforts have been made to induce over-expression or increased activity of this protein. In this review, we provide an overview of the roles of SIRT3 in cardiac hypertrophy induced by pressure overload or agonists and cardiomyocytes ischemic injuries. Moreover, we will introduce the application of SIRT3 agonists in the prevention of cardiac hypertrophy and ischemia reperfusion injury.

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“…Under normal conditions, about 70% of the energy is derived from mitochondrial oxidation of FA (9). The transport route of FA into the myocyte starts in the blood plasma of the capillaries (Fig.…”

Section: Physiological Backgroundmentioning

confidence: 99%

“…FA are important substrates for the heart, because they are the heart's main source of energy under normal conditions (9). The transport route of FA from the blood into the heart muscle cells (myocytes) is one with many constraints (58), which have been subject of investigation in the last decades (Fig.…”

Section: Section I Introductionmentioning

confidence: 99%