A Knockout of the IFITM3 Gene Increases the Sensitivity of WI-38 VA13 Cells to the Influenza A Virus.

One of the ways to regulate the sensitivity of human cells to the influenza virus is to knock out genes of the innate immune response. Promising targets for the knockout are genes of the interferon-inducible transmembrane protein (IFITM) family, in particular the gene, whose product limits the entry of a virus into the cell by blocking the fusion of the viral and endosomal membranes. In this study, by means of genome-editing system CRISPR/Cas9, monoclonal cell lines with an knockout were obtained based on WI-38 VA13 cells (human origin).

[Synthesis, structure, and biological properties of some 8alpha-analogues of steroid estrogens with fluorine in position 2].

A total synthesis of 8alpha analogues of steroid estrogens with fluorine in position 2 was achieved. Structural features of these compounds were studied by the example of 17beta-acetoxy-2-fluoro-3-methoxy-8alpha-estra-1,3,5(10)-triene. It was shown that the 8alpha analogues of 2-fluorosubstituted steroid estrogens have a low uterotropic activity and retain the osteoprotective and hypocholesterolemic activities.

[Synthesis and biological properties of 6-oxa-D-homo-8alpha analogues of steroid estrogens].

Modifications of 6-oxa-D-homo-8alpha-analogues of steroid estrogens were found to lead to a complete loss of the uterotropic and hypertriglyceridemic activities. These compounds may be promising for the design on their basis of inhibitors of the steroid hormone metabolism and transporters of other compounds to the estrogen target organs.

[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 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.

[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.

[Change in the tricarboxylic acid cycle dehydrogenase activity under the action of thyroxine in the brain of animals of varying age].

The effect of thyroxin on the activities of tricarboxylic acid cycle enzymes and NADP-malate dehydrogenase in the rat brain was studied. Experiments were conducted on 20- and 40-day old and on adult rats. Injection of L-thyroxin (50 microgram/100 g body weight) to thyroidectomized rats induced some changes in the activities of citrate-syntase, dehydrogeases of TAC and malic enzymes in the mitochondrial and cytoplasmic fractions of the brain.

[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.

[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.

[Participation of thyroxine in the regulation of the rate of isocitrate dehydrogenase reactions in the brain and liver].

A study was made of the effect of thyroxin on the activity of NAD- and NADP-dependent isocitratedehydrogenases in the brain and the liver of chick embryos. It was found that in both of the organs thyroxin accelerated isocitrate oxidation in the mitochondria through the NAD-dependent route and elevated the velocity of the NADP-isocitratedehydrogenase reaction in the citoplasm. At the same time the activity of the mitochondrial NADP-dependent isocitratedehydrogenase increased after the administration of the hormone to the embryos only in the mitochondria of the brain cells; this was apparently associated with the intensive biosynthesis of specific lipids in the developing brain.

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

NAD-dependent malate dehydrogenase (1.1.1.

[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.