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Biomedical subjects

V I Sergienko

Publications and source records attributed to V I Sergienko.

At least 19 recordsLinked to original sources
PubMed2001

Immunochemical assay of glia-specific antigens as a criterion for blood-brain barrier permeability in rats during acute intoxication with sodium barbital.

Enzyme immunoassay showed penetration of two glia-specific antigens, glial fibrillar acid protein GFAP and specific brain glycoprotein alpha(2)GP, through the blood-brain barrier in rats treated with toxic doses of sodium barbital. The permeability of the blood-brain barrier was completely normalized 3 days after treatment. This method can be used in clinical practice for evaluation of the severity of impairment and dynamics of normalization of blood-brain barrier properties during acute intoxication with barbiturates.

Animals↗
PubMed2000

Oxidative stress in keratinocytes as an etiopathogenetic factor of psoriasis.

A new etiopathogenetic concept of psoriasis is proposed, which considers psoriasis as a typical inflammatory process characterized by increased antioxidant activity and overexpression of apoptotic receptors. Under these conditions, hyperstimulation of germinative layer cells proliferation dramatically accelerates keratinocyte passage towards apoptotic effect of atmospheric oxygen and its reactive species dooming to death cells with enhanced expression of apoptotic receptors. Oxidative stress of nondifferentiated keratinocytes triggers the formation of defective horny layer, the key mechanism of psoriasis.

Apoptosis↗
PubMed1997

Hypochlorite-induced peroxidation of egg yolk phosphatidylcholine is mediated by hydroperoxides.

Using a chemiluminescent method, the consumption of HOCl/OCl- was investigated during interaction with liposomes prepared from dimyristoylphosphatidylcholine (DMPC) or egg yolk phosphatidylcholine (EYPC). The concentration of HOCl/OCl-decreased with time in the suspension of EYPC that contain unsaturated lipids and did not change in DMPC liposome suspensions. HOCl/OCl- was consumed more rapidly in peroxidized EYPC. The amount of double bonds was lowered by 40% in peroxidized liposomes and decreased by approximately one-third under the action of HOCl/OCl- in both native and peroxidized EYPC samples. Second-order rate constants for the interaction between HOCl and phospholipid double bonds of 0.50 M-1 s-1 were calculated for native EYPC on basis of the consumption of HOCl/OCl- or from the decrease in concentration of double bonds. In peroxidized EYPC this reaction constant was similar as determined following changes in double bonds. It is concluded that the consumption of HOCl/OCl- increased in peroxidized liposomes due to additional reactions with lipid peroxidation products. tert-Butyl hydroperoxide and cumene hydroperoxide, or organic peroxides or epoxides (cis-9,10-epoxystearic acid; cholesterol-5 alpha,6 alpha-epoxide; trans-2,3-epoxy-butane; cis-2,3-epoxy-butane) were incorporated into liposomes and investigated in respect to their ability (1) to increase the consumption of HOCl/OCl- in DMPC liposomes, (2) to generate a non-enhanced chemiluminescence with HOCl/OCl- and (3) to evoke an accumulation of lipid peroxidation products (TBARS) in EYPC liposomes in the absence and presence of NaOCl. None of peroxides or epoxides tested showed any effect on the consumption of HOCl/OCl- or the generation of chemiluminescence. Nor increase of TBARS both in the absence or presence of HOCl/OCl-. In contrast, tert-butyl hydroperoxide and cumene hydroperoxide increased the consumption of HOCl/OCl- in DMPC liposomes and mediated a higher accumulation of TBARS in EYPC liposomes in the presence of HOCl/OCL- over the control. These data suggest that lipid peroxidation in EYPC can be initiated by the reaction of HOCl/OCL- with organic hydroperoxides.

Animals↗
PubMed1997

Products of the reaction of cholesterol with hypochlorite anion.

Products of the reaction of cholesterol with hypochlorite (OCI) in various systems (egg phosphatidylcholine liposomes, low-density lipoproteins, and aqueous colloidal dispersion of cholesterol) were separated and analyzed by TLC, HPLC, and gas chromatography-mass spectrometry. The reactions of hypochlorite with cholesterol result in the same reaction products in all treated systems. Eighteen fractions were isolated from the reaction mixture by normal-phase HPLC in hexane-isopropanol (95:5 v/v); these were then examined by gas chromatography-mass spectrometry. Six products less polar than cholesterol were isolated from the reaction mixture; two of them were identified as 4,6-cholesten-3-one and 4-cholesten-3,6-dione. Among the oxidation products more polar than cholesterol, nine compounds were identified; they are 5,7-cholestadien-3 beta-ol,3,5-cholestadien-7-one, 4-cholesten-3 beta, 6 beta-diol, 5-cholesten-3 beta, 7 beta-diol, cholestan-3 beta, 5 alpha, 6 beta-triol, 5 alpha-cholestan-3 beta-ol-6-one, 5-cholesten-3 beta-ol-7-one, 5 alpha, 6 alpha-epoxycholestan-3 beta-ol, and 5 alpha-cholesten-3,6-dione.

Cholesterol↗
PubMed1997

Effect of sodium chloride, chlorite, and perchlorate on the hypochlorite-induced peroxidation of phospholipid liposomes.

The abilities of sodium hypochlorite (NaClO), chlorite (NaClO2), chlorate (NaClO3), and perchlorate (NaClO4) to initiate lipid peroxidation (LP) in liposomes formed from unsaturated phosphatidylcholine were compared. It was shown that only NaClO induced an intensive accumulation of LP products (thiobarbituric acid-reactive substances and diene conjugates) in the liposomes as a result of their co-incubation. The other oxochlorates produced no similar effects and did not affect the hypochlorite-induced LP. This indicates that the observed hypochlorite-induced LP does not result from the presence of chlorite, chlorate, or perchlorate anion admixtures in the medium.

Animals↗
PubMed1995

Hypochlorite induces lipid peroxidation in blood lipoproteins and phospholipid liposomes.

The accumulation of lipid peroxidation products reacting with 2-thiobarbituric acid (TBARS) has been observed both in very low density blood lipoprotein (VLDL) and suspensions of liposomes prepared from VLDL phospholipids incubated with hypochlorite. Butylated hydroxytoluene (BHT) completely inhibited TBARS formation at a concentration of 100 microM, at which it decreased the concentration of hypochlorite in the absence of liposomes only by 7%. The formation of lipid peroxidation products in course of the incubation of egg yolk phospholipid liposomes with hypochlorite has been revealed using three methods: (1) measurement of TBARS, (2) measurement of additional amounts of TBARS resulting from the introduction of excess Fe2+ to peroxidized liposomes (delta TBARS), and (3) measurement of the chemiluminescence flash amplitude appeared upon the addition of Fe2+ to the suspension. The results obtained by all these methods were similar: Lipid peroxidation products were accumulated during the first 2 to 3 h of liposome incubation with 100 microM hypochlorite, and the amount of lipid peroxidation products accumulated after incubation was directly proportional to the initial hypochlorite concentration. These data suggest that hypochlorite can initiate lipid peroxidation both in lipoproteins and phospholipid liposomes.

Butylated Hydroxytoluene↗
PubMed1995

[Interactions of various amino acids, dipeptides and glutathione with hypochlorite anion (CLO-)].

The specific features of interaction between sodium hypochlorite and various amino compounds were examined. It is shown that in the first reaction munite, methionine and glutathione are the most active in neutralizing hypochlorite anion, while histidine, glycine, alanine, dipeptides and taurine are less active. The chloroamino complexes formed by dipeptides and taurine are the most resistant.

Alanine↗
PubMed1995

[Molecular mechanisms of the effects of sodium hypochlorite on thrombocytes and lipoproteins].

Hypochlorite seems to inhibit platelet aggregation in the platelet-rich plasma (PRP) by modifying fibrinogen receptors. The hypochlorite-inactivated isolated platelets are completely repaired by native plasma. Platelet aggregation in PRP is suppressed by hypochlorite by its direct interaction with cells and indirectly due to plasma modification. The indirect action of hypochlorite is a reversible reaction between the platelet active groups and the products of plasma modification. The reaction may involve sulphur-containing groups. The spin-probe method shows that hypochlorite penetrates into the lipid phase of human blood lipoproteins. It initiates lipid peroxidation and causes the disturbance of the lipid structure and the protein please.

Animals↗
PubMed1995

[Interaction of hypochlorite with hydroperoxides and other oxidation products of phosphatidylcholine liposomes].

The chemiluminescence in the presence of luminol has been used to measure the amount of hypochlorite and its reduction during the interaction with oxidized and non-oxidized liposomes from egg yolk phosphatidylcholine as well as with organic peroxides (tert-butylhydroperoxide, cumene hydroperoxide, di-tert-butylperoxide, tert-butylperbenzoate, di-benzoylperoxide), and epoxides (cis- and trans-2,3-epoxy-butane, cholesterol-5 alpha,6 alpha-epoxide, and cis-9,10-epoxystearic acid). Since hypochlorite did not react with the saturated phospholipid, dimyristoylphosphatidylcholine (DMPC), and the reduction of double bonds in egg yolk phosphatidylcholine liposomes occurred at the same rate in both oxidized and non-oxidized liposomes, it may be suggested that hypochlorite interacted precisely with LPO products. None of the epoxides tested in this study, similar to di-tert-butylperoxide, tert-butylperbenzoate, di-benzoylperoxide, incorporated into liposomes reacted with hypochlorite. In contrast, tert-butylhydroperoxide and cumene hydroperoxide effectively reacted with it. The data obtained suggest that epoxides, dialkyl-, diacyl-, and alkyl-acyl-peroxides are not involved in hypochlorite-induced LPO. At the same time, organic hydroperoxides commonly present in certain amounts in the biomembrane lipid phase in vivo may play a role lf an intermediate; its interaction with HOCl/OCl- gives rise to free radical formation followed by accumulation of LPO products.

Free Radicals↗
PubMed1994

Peroxidation of egg yolk phosphatidylcholine liposomes by hypochlorous acid.

The powerful neutrophil-derived oxidant hypochlorous acid HOCl/OCl- is assumed to contribute to tissue injury in a number of pathological states accompanied by massive accumulation of neutrophils. The production of malondialdehyde to indicate lipid peroxidation was studied in egg yolk phosphatidylcholine liposomes upon treatment with NaOCl as a source for hypochlorous acid. Its accumulation was inhibited by alpha-tocopherol and butylated hydroxytoluene. Singlet oxygen, hydroxyl radicals or superoxide anion radicals derived from direct reactions of hypochlorous acid seem not to be involved in initiation of lipid peroxidation because the malondialdehyde accumulation was unaffected by hydrogen peroxide, catalase, superoxide dismutase, ferrous sulphate or ferric chloride. Double bonds of fatty acid residues seem to be the primary target for NaOCl. Their number is continuously diminished in liposomes (2 mg lipids/ml) after incubation with increasing amounts of NaOCl at 37 degrees C for 40 min as detected by two independent methods (iodine bromide reduction and 1H-NMR spectroscopy). A 1:1 molar ratio between the loss of double bonds and NaOCl added was found only at low NaOCl concentrations. Then double bonds are decreased with a lower efficiency. A continuous increase of lipid peroxidation products was only observed up to 0.5-0.7 mmol/l NaOCl. The yield of lipid hydroperoxides kept constant at higher NaOCl concentrations. However, diene conjugates and malondialdehyde exhibit a maximum at 0.7-1 mmol/l or 0.5 mmol/l NaOCl, respectively, while the concentration of these products decreases at higher doses of NaOCl. The decrease of malondialdehyde was more pronounced than for diene conjugates. These results were discussed from the background that at minimum two (diene conjugates) or three (malondialdehyde) double bonds in a fatty acid residue are necessary for formation of lipid peroxidation products.

Egg Yolk↗
PubMed1994

Peroxidation of human blood lipoproteins induced by exogenous hypochlorite or hypochlorite generated in the system of "myeloperoxidase + H2O2 + Cl-".

Oxidation of human plasma lipoprotein (LP) was studied in the presence of exogenous hypochlorite anion (OCl-) or OCl- generated in the "myeloperoxidase + H2O2 + Cl-" system. OCl- effectively initiates peroxidation of lipids extracted from LP and those within LP particles, as can be judged from accumulation of secondary (thiobarbituric acid [TBA] reactive) and final (Schiff bases) products of lipid peroxidation (LPO) in LP after incubation with myeloperoxidase or exogenous OCl-. Very low density and low density lipoproteins classified as atherogenic LP are more sensitive to OCl(-)-induced LPO than high density lipoproteins. These data allow us to propose that OCl- secreted by activated neutrophils and monocyte-macrophages can produce oxidative modification of LP in vivo. The latter is known as a risk factor in the development of atherosclerosis.

Chlorides↗
PubMed1993

[Capacity of hypochlorite to penetrate into the lipid phase of human blood lipoproteins].

In order to elucidate the possibility of hypochlorite (NaOCl) presenting in aqueous media to penetrate into the surface proteolipid layer of low density lipoproteins (LDL), the kinetics of NaOCl-induced oxidation of spin probes localized within the lipid phase was studied. The paramagnetic analogs of stearic acid were employed as spin probes that contained doxyl groups localized at different positions on the carbon chain (at positions 5, 13 and 16). It was shown that all the three probes are oxidated by hypochlorite with the same rate both in aqueous media and in LDL. The results obtained indicate that hypochlorite in water may interact with groups in the lipid phase of LDL, including unsaturated--HC = CH--bonds.

Electron Transport↗