scholarly journals CYTOCHROMES OF MITOCHONDRIES AND ACTIVITY OF HEME METABOLISM ENZYMES IN THE LIVER UNDER DIFFERENT NUTRIENT REGIMES

2021 ◽  
Vol 67 (2) ◽  
pp. 37-43
Author(s):  
G.P. Kopylchuk ◽  
◽  
Z.-M. I. Grynenkiv ◽  
O.M. Voloshchuk ◽  
◽  
...  
Keyword(s):  
Heme Oxygenase ◽  
Simultaneous Increase ◽  
Key Enzymes ◽  
Aminolevulinate Synthase ◽  
Heme Metabolism ◽  
Metabolism Enzymes ◽  
Sucrose Diet ◽  
High Sucrose Diet ◽  
High Sucrose ◽  
Mitochondrial Cytochromes

The content of mitochondrial cytochromes and the activity of key enzymes of heme metabolism in the liver of rats under conditions of different dietary supply of protein and sucrose were investigated. The quantitative determination of mitochondrial cytochrome was performed by differential spectrophotometry, δ-aminolevulinate synthase activity was determined spectrophotometrically taking into account the molar extinction coefficient of 0.023x10(3) M(-1)sm(-1). Hemoxygenase activity was determined using the amount of formed bilirubin. It was found that under conditions of consumption of high-sucrose diet a significant decrease in the content of all mitochondrial cytochromes is noted: the content of cytochromes aa3, b and c1 decreases within 1.2-1.7 times, and content of cytochrome c decreases in two times. In the case of excessive consumption of sucrose on the background of alimentary protein deprivation the content of cytochromes b and c1 in the liver of rats does not differ statistically from similar indicators of the group of animals kept on a high-sucrose diet. At the same time, the content of cytochromes aa3 and c is significantly reduced. According to the activity of δ-aminolevulinate synthase under conditions of consumption of a high-sucrose diet, the studied enzymatic activity decreases by about 1.5 times with a simultaneous increase in the activity of heme oxygenase. Thus, there is a marked decrease in heme synthesis against the background of increased catabolism, which explains the decrease in the content of cytochromes in the mitochondria of the liver of rats under conditions of excess sucrose in the diet. The maximum increase in the activity of heme oxygenase (almost threefold) is observed in animals that were kept on a high-sugar diet deficient in protein content. Thus, dietary protein deficiency is a critical factor affecting the heme metabolism in the mitochondria of liver cells. The established changes in the content of mitochondrial cytochromes and the activities of key enzymes of heme metabolism in the liver could be considered as prerequisites for deepening its energy imbalance in conditions of different supply of sucrose and protein in diet.

Hepatic Transcriptomic Signature of High-Sucrose Diet in Nonobese Model of Metabolic Syndrome and Prediabetes

Diabetes ◽  
2018 ◽  
Vol 67 (Supplement 1) ◽  
pp. 1723-P
Author(s):  
IRENA MARKOVÁ ◽  
MARTINA HÜTTL ◽  
HANA MALINSKA ◽  
ONDREJ SEDA ◽  
LUDMILA KAZDOVA
Keyword(s):  
Metabolic Syndrome ◽  
Sucrose Diet ◽  
Transcriptomic Signature ◽  
High Sucrose Diet ◽  
High Sucrose

Motor learning impairment in rats under a high sucrose diet

2021 ◽  
Vol 234 ◽  
pp. 113384
Author(s):  
Nayely Flores-Fuentes ◽  
Carolina Hernandez-Cruz ◽  
Karina Bermeo ◽  
Antonio Barajas-Martinez ◽  
Valeria Nayely Hernandez-Serratos ◽  
...  
Keyword(s):  
Motor Learning ◽  
Sucrose Diet ◽  
High Sucrose Diet ◽  
Learning Impairment ◽  
High Sucrose

scholarly journals Metabolic control of daily locomotor activity mediated by tachykinin in Drosophila

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Sang Hyuk Lee ◽  
Eunjoo Cho ◽  
Sung-Eun Yoon ◽  
Youngjoon Kim ◽  
Eun Young Kim
Keyword(s):  
Locomotor Behavior ◽  
Sensory Inputs ◽  
Sucrose Diet ◽  
High Nutrient ◽  
Intracellular Ca ◽  
High Sucrose Diet ◽  
Locomotor Activities ◽  
Locomotor Behaviors ◽  
High Sucrose ◽  
Over Time

AbstractMetabolism influences locomotor behaviors, but the understanding of neural curcuit control for that is limited. Under standard light-dark cycles, Drosophila exhibits bimodal morning (M) and evening (E) locomotor activities that are controlled by clock neurons. Here, we showed that a high-nutrient diet progressively extended M activity but not E activity. Drosophila tachykinin (DTk) and Tachykinin-like receptor at 86C (TkR86C)-mediated signaling was required for the extension of M activity. DTk neurons were anatomically and functionally connected to the posterior dorsal neuron 1s (DN1ps) in the clock neuronal network. The activation of DTk neurons reduced intracellular Ca2+ levels in DN1ps suggesting an inhibitory connection. The contacts between DN1ps and DTk neurons increased gradually over time in flies fed a high-sucrose diet, consistent with the locomotor behavior. DN1ps have been implicated in integrating environmental sensory inputs (e.g., light and temperature) to control daily locomotor behavior. This study revealed that DN1ps also coordinated nutrient information through DTk signaling to shape daily locomotor behavior.

Effects on Serum Lipids of Different Dietary Fats Associated with a High Sucrose Diet

1973 ◽  
Vol 44 (6) ◽  
pp. 601-604 ◽  
Author(s):  
J. I. Mann ◽  
G. S. Watermeyer ◽  
E. B. Manning ◽  
J. Randles ◽  
A. S. Truswell
Keyword(s):  
Serum Lipids ◽  
Saturated Fat ◽  
Dietary Fats ◽  
Complex Carbohydrate ◽  
The Third ◽  
Sucrose Diet ◽  
Daily Energy ◽  
Dietary Period ◽  
High Sucrose Diet ◽  
High Sucrose

1. Each of nine volunteers was fed three different diets. The percentage of total daily energy provided by fat, carbohydrate and protein remained constant, but the nature of the fat and carbohydrate was altered. The first diet contained ordinary amounts of sucrose and predominantly saturated fat. During the second dietary period, fat remained saturated, but the quantity of sucrose was increased at the expense of complex carbohydrate. In the third dietary period, the sucrose intake remained high, but fat was supplied chiefly in the polyunsaturated form. 2. A small but statistically significant increase of serum fasting cholesterol and triglyceride was observed during the second dietary period, but on the third diet levels of both lipids fell to concentrations not significantly different from those seen on the first diet.

scholarly journals The redox state of free nicotinamide–adenine dinucleotide phosphate in the cytoplasm of rat liver

1969 ◽  
Vol 115 (4) ◽  
pp. 609-619 ◽  
Author(s):  
R. L. Veech ◽  
L. V. Eggleston ◽  
H. A. Krebs
Keyword(s):  
Malic Enzyme ◽  
Redox State ◽  
Carbohydrate Diet ◽  
Redox States ◽  
Low Carbohydrate Diet ◽  
A Value ◽  
Low Carbohydrate ◽  
Sucrose Diet ◽  
High Sucrose Diet ◽  
High Sucrose

1. The concentrations of the oxidized and reduced substrates of the ‘malic’ enzyme (EC 1.1.1.40) and isocitrate dehydrogenase (EC 1.1.1.42) were measured in freeze-clamped rat livers. By assuming that the reactants of these dehydrogenase systems are at equilibrium in the cytoplasm the [free NADP+]/[free NADPH] ratio was calculated. The justification of the assumption is discussed. 2. The values of this ratio obtained under different nutritional conditions (well-fed, 48hr.-starved, fed with a low-carbohydrate diet, fed with a high-sucrose diet) were all of the same order of magnitude although characteristic changes occurred on varying the diet. The value of the ratio fell on starvation and on feeding with the low-carbohydrate diet and rose slightly on feeding with the high-sucrose diet. 3. The mean values of the ratio were calculated to be between 0·001 and 0·015, which is about 100000 times lower than the values of the cytoplasmic [free NAD+]/[free NADH] ratio. 4. The differences in the redox state of the two nicotinamide–adenine dinucleotide couples can be explained on a simple physicochemical basis. The differences are the result of equilibria that are determined by the equilibrium constants of a number of highly active readily reversible dehydrogenases and transaminases and the concentrations of the substrates and products of these enzymes. 5. The decisive feature is the fact that the NAD and NADP couples share substrates. This sharing provides a link between the redox states of the two couples. 6. The application of the method of calculation to data published by Kraupp, Adler-Kastner, Niessner & Plank (1967), Goldberg, Passonneau & Lowry (1966) and Kauffman, Brown, Passonneau & Lowry (1968) shows that the redox states of the NAD and NADP couples in cardiac-muscle cytoplasm and in mouse-brain cytoplasm are of the same order as those in rat liver. 7. The determination of the equilibrium constant at 38°, pH7·0 and I 0·25 (required for the calculation of the [free NADP+]/[free NADPH] ratio), gave a value of 3·44×10−2m for the ‘malic’ enzyme (with CO2 rather than HCO3− as the reactant) and a value of 1·98×10−2m−1 for glutathione reductase.

Sign in / Sign up

Export Citation Format

Share Document