PubMed Health⌕ Search

Biomedical subjects

N D Eshchenko

Publications and source records attributed to N D Eshchenko.

At least 19 recordsLinked to original sources
PubMed2003

[Lipid peroxidation in rabbit and rat visual system structures].

In our work, the lipid peroxidation (LPO) in the retina, optic chiasma, and visual cortex of rat and rabbit brain was investigated. The contents of the LPO products (diene conjugates, triene conjugates, TBA-reactive products, Schiff bases) and oxidation index (calculated as 232/2 15) were similar in the retina and visual brain cortex of rats. In vivo, lipid oxidation in the optic chiasma was higher as compared with two other parts of visual tract. The similar data were obtained in our experiments with rabbit's visual tract. The sensitivity of tissues to peroxidation in vitro was studied in homogenates incubated with 0.2 mM ascorbate and 10 mkM FeSO4 for 20 min at 37 degrees C. The results of these experiments deviated from the data obtained in vivo, namely: the LPO in optic chiasma was lower than in the retina and the brain cortex. This data are in compliance with lipid composition of investigated parts of the visual tract of both animals. In our opinion, the high level of LPO in optic chiasma demonstrated in vivo is due to low antioxidants level in this part of the visual tract. Our findings also indicate that LPO in retina both in vivo and in vitro experiments are similar to those in the brain cortex and may be attributed to similar lipid composition and activity of antioxidant enzymes (such as superoxiddismutasa and glutathionereductase).

Animals↗
PubMed2000

[Lipogenesis in the brain under hypoxia].

This study investigated the utilization of some radioactive precursors [2(12)C]-acetate, [1-6(14)]-glucose, [5(14)C]-glutamate) for fatty acids and lipid biosynthesis in the rat brain under normal and hypoxic conditions. In severe hemic hypoxia (30-45 min after the injection of 15 mg of NaNO2/100 g body weight) there was a significant increase in 14C incorporation from glutamate into brain lipids (by 2.8 times) and into fatty acids (by 2.2 times) as compared to the control level. Enhanced lipogenesis from glutamate was demonstrated due to the activation of all alpha-ketoglutarate shunt steps. The higher lipogenesis from glutamate in the brain as a possible mechanism for this excitatory amino acid utilization under hypoxia.

Animals↗
PubMed1978

[Participation of glutamate and alanine in amino acid biosynthesis, in lipogenesis, and in gluconeogenesis in the brain].

The participation of glutamate and alanine in lipogenesis and gluconeogenesis of brain was investigated. 5(14)C glutamate was injected intracisternally in an amount of 5 mcCu/l g tissue and 3(14)C-alanine was injected subcutaneously 30 mcCu/100 g body weight. Labels from glutamate and alanine were recovered in different lipid franctions -- in phospholipids, glycerides, free fatty acids and cholesterol, as well as in glucose and glycogen. An intensive incorporation of label from 5(14)C glutamate into various amino acids--aspartic acid, glutamine, serine, glycine and alanine--was demonstrated. The data presented indicate the participation of amino acids in lipogenesis and gluconeogenesis of brain.

Alanine↗
PubMed1976

[Mechanisms regulating citric acid metabolism in the brain].

The changes in the rates of citrate biosynthesis and utilization in rat brain, liver, kidney and heart, produced by hypoxia, action of 2,4-DNP and thyreotoxicosis, were compared with changes of some regulatory parameters under the same conditions. The comparison of citrate-synthase activities, citrate levels in tissues and 14C-incorporation from different precursors into citric acid permitted us to establish that the biosynthesis of citrate in brain was more intensive than in other tissues studied. The main source of acetyl-CoA for citrate-synthase reaction in brain is the oxidation of pyruvate. The ratio of adenine nucleotides plays an important role in the control of citrate-synthase activity in brain, where the oxaloacetate control is not as significant as in liver. NAD-specific isocitrate dehydrogenase reaction was found to be the dominant pathway for citrate oxidation in brain: more than 60 percent of brain citrate were oxidized by NAD-ICDH, while less than 10 percent of citric acid were utilized by this enzyme in other tissues studied. The existance of an adenine nucleotide control of NAD-ICDH activity in brain may be an additional mechanism for the regulation of the first steps of energy metabolism in brain.

Acetyl Coenzyme A↗
PubMed1974

[Changes in the activities of NAD- and NADP-specific isocitrate dehydrogenases in the brain and liver during the postembryonic development of animals].

The activities of NAD- and NADP-specific isocitrate dehydrogenases (ICDH) were investigated in subcellular fractions of rat brain and liver. Animals of different age groups were used: newborn, 10-, 20-, 30-, 40-days old and adult rats. It was shown that NAD-ICDH activity rose sharply in adult brain mitochondria as compared with that of developing animals. The NAD-dependent pathway of isocitrate oxidation predominated in mitochondria of both developing and adult brain. The activity of NADP-ICDH decreased in brain mitochondria and cytoplasm in the course of development. Some changes in the distribution of enzyme activity between subcellular fractions were also found in adult brain. The activity of mitochondrial NADP-ICDH was higher than that of newborn animals.

Age Factors↗
PubMedDate not supplied

The effects of thyroxine isomers on free-radical oxidation processes in subcellular fractions of rat cerebral cortex.

Measurements made by chemiluminescence (CL) were used to estimate effective D- and L-thyroxine concentrations and to study their effects on free-radical oxidation processes in the mitochondrial and synaptosomal fractions of rat cerebral cortex in vitro. These experiments showed that in a model system containing riboflavin, the antioxidant activity of D-T4 was 2.2 times greater than that of L-T4. The effective concentrations for the two forms of thyroxine were I50 = 74.3 +/- 7.1 microM for D-T4 and I50 = 154.7 +/- 12.3 microM for L-T4. Studies of the in vitro effects of thyroxine on the membrane fraction of the cerebral cortex were based on luminol-dependent peroxide CL. At physiological concentrations (10 nM), both isomers of the hormone had identical antioxidant activities, which were stronger in the mitochondrial traction, where the intensity of CL decreased by 69% and 66%, compared with 45% and 46% decreases in the synaptosomal fraction. Since the D-form has no hormonal activity, it is suggested that this effect is associated with the phenolic nature of thyroxine.

Animals↗
PubMedDate not supplied

[Change in the activity of NAD- and NADP-specific malate dehyrdogenases in oxygen deficiency in different tissues].

NAD-dependent malate dehydrogenase (1.1.1.37) activity was markedly decreased under hypoxia in rat brain and liver mitochondria and cytoplasm; most significant decrease was observed in brain cortex mitochondria. NADP-dependent malate dehydrogenase (1.1.1.40) activity was also reduced under these conditions and the most considerable changes were found in liver mitochondria and cytoplasm. Distribution of activities of these enzymes between subcellular fractions of brain and liver did not change under hypoxia. The oxaloacetate level rised by 20% in brain and decreased by 20-25% in liver under hypoxia.

Animals↗