4-hydroxy-2-nonenal and n-hexanal

The process of lipid oxidation generates a diverse array of small aldehydes and carbonyl-containing compounds, which may occur in free form or esterified within phospholipids and cholesterol esters. These aldehydes mostly result from fragmentation of fatty acyl chains following radical oxidation, and the products can be subdivided into alkanals, alkenals (usually α,β-unsaturated), γ-substituted alkenals and bis-aldehydes. Isolevuglandins are non-fragmented di-carbonyl compounds derived from H

Topics: Acrolein; Aldehydes; Animals; Humans; Isoprostanes; Lactoglobulins; Lipid Peroxidation; Oxidative Stress; Protein Processing, Post-Translational

Lipid oxidation and metmyoglobin (MMb) reduction are popular issues in meat color research. This study evaluated the effects of aldehyde products, particularly 4-hydroxy-2-nonenal (HNE) and hexenal, of lipid oxidation on the oxymyoglobin stability, mitochondrial membrane permeability, MMb reduction ability, electron transport chain-mediated MMb reduction, and nicotinamide adenine dinucleotide reduced form (NADH)-dependent MMb reductase activity of bovine Longissimus muscle. The results indicated that HNE and hexenal accelerate the oxidation rate of oxymyoglobin, significantly increase the permeability of the mitochondrial membrane, and inhibit electron transport chain-mediated MMb reduction. However, HNE and hexenal were found to exert no effect on the activity of NADH-dependent MMb reductase. Thus, the aldehyde products of lipid oxidation could damage the microstructure of mitochondria and inhibit mitochondria-mediated MMb reduction, which is disadvantageous in terms of the color stability of fresh bovine Longissimus muscle.

Topics: Aldehydes; Animals; Cattle; Cell Membrane Permeability; Color; Electron Transport Chain Complex Proteins; Lipid Metabolism; Meat; Metmyoglobin; Mitochondrial Membranes; Muscle, Skeletal; Myoglobin; Oxidation-Reduction

Double bonds in polyunsaturated fatty acids (PUFA) and lipids are one of the major targets of reactive oxygen species (ROS). The resulting lipid peroxidation products (LPP) represent a group of chemically diverse compounds formed by several consecutive oxidative reactions. Oxidative cleavage leads to the formation of small aliphatic and lipid-bound aldehydes and ketones (oxoLPPs). These strong electrophiles can readily react with nucleophilic substrates, for example, side chains in proteins which can alter structure, function, and cellular distribution of the modified proteins. Despite growing interest in the field of oxidative lipidomics, only a few dominantly formed oxoLPP were identified. Due to the chemical and physical properties, aliphatic oxoLPPs are usually analyzed using gas chromatography-mass spectrometry (GC- MS), while nonvolatile lipid-bound oxoLPPs require liquid chromatography-mass spectrometry (LC-MS). To overcome the need for the two analyses, we have developed a new derivatization strategy to capture all oxoLPP independent to their properties with electrospray ionization (ESI) MS allowing simultaneous detection of aliphatic and lipid-bound oxoLPPs. Thus, the 7-(diethylamino)coumarin-3-carbohydrazide (CHH) derivatization reagent allowed us to identify 122 carbonyl compounds in a mixture of four PUFA and phosphatidylcholines (PC) oxidized in vitro.

Topics: Aldehydes; Coumarins; Hydrazines; Lipid Peroxidation; Lipids; Phospholipids; Spectrometry, Mass, Electrospray Ionization; Statistics as Topic

Peroxides are often used as models to induce oxidative damage in cells in vitro. The aim of the present study was to elucidate the role of lipid peroxidation in peroxide-induced cell death. To this end (i) the ability to induce lipid peroxidation in C6 rat astroglioma cells of hydrogen peroxide (H2O2), cumene hydroperoxide (CHP) and t-butyl hydroperoxide (t-BuOOH) (ii) the relation between peroxide-induced lipid peroxidation and cell death in terms of time and concentration dependency and (iii) the capability of the lipid peroxidation chain breaking alpha-tocopherol to prevent peroxide-induced lipid peroxidation and/or cell death were investigated. Lipid peroxidation was characterised by measuring thiobarbituric acid reactive substances (TBARS) and, by HPLC, malondialdehyde (MDA), 4-hydroxynonenal (4-HNE) and hexanal. Within 2 h CHP, t-BuOOH and H2O2 induced cell death with EC50 values of 59+/-9 microM, 290+/-30 microM and 12+/-1.1 mM, respectively. CHP and t-BuOOH, but not H2O2 induced lipid peroxidation in C6 cells with EC50 values of 15+/-14 microM and 130+/-33 microM, respectively. The TBARS measured almost exclusively consisted of MDA. 4-HNE was mostly not detectable. The concentration of hexanal slightly increased with increasing concentrations of organic peroxides. Regarding time and concentration dependency lipid peroxidation preceded cell death. Pretreatment with alpha-tocopherol (10 microM, 24 h) prevented both, peroxide-induced lipid peroxidation and cell death. The results strongly indicate a major role of lipid peroxidation in the killing of C6 cells by organic peroxides but also that lipid peroxidation is not involved in H2O2 induced cell death.

Topics: Aldehydes; alpha-Tocopherol; Animals; Antioxidants; Benzene Derivatives; Cell Death; Cell Line, Tumor; Chromatography, High Pressure Liquid; Dose-Response Relationship, Drug; Drug Combinations; Glioma; Hydrogen Peroxide; Lipid Peroxidation; Malondialdehyde; Oxidants; Oxidative Stress; Peroxides; Rats; tert-Butylhydroperoxide; Thiobarbituric Acid Reactive Substances

Most mammalian species express high concentrations of ALDH3A1 in corneal epithelium with the exception of the rabbit, which expresses high amounts of ALDH1A1 rather than ALDH3A1. Several hypotheses that involve catalytic and/or structural functions have been postulated regarding the role of these corneal ALDHs. The aim of the present study was to characterize the biochemical properties of the rabbit ALDH1A1. We have cloned and sequenced the rabbit ALDH1A1 cDNA, which is 2,073 bp in length (excluding the poly(A+) tail), and has 5' and 3' nontranslated regions of 46 and 536 bp, respectively. This ALDH1A1 cDNA encodes a protein of 496 amino acids (Mr = 54,340) that is: 86-91% identical to mammalian ALDH1A1 proteins, 83-85% identical to phenobarbital-inducible mouse and rat ALDH1A7 proteins, 84% identical to elephant shrew ALDH1A8 proteins (eta-crystallins), 69-73% identical to vertebrate ALDH1A2 and ALDH1A3 proteins, 65% identical to scallop ALDH1A9 protein (omega-crystallin), and 55-57% to cephalopod ALDH1C1 and ALDH1C2 (omega-crystallins). Recombinant rabbit ALDH1A1 protein was expressed using the baculovirus system and purified to homogeneity with affinity chromatography. We found that rabbit ALDH1A1 is catalytically active and efficiently oxidizes hexanal (Km = 3.5 microM), 4-hydroxynonenal (Km = 2.1 microM) and malondialdehyde (Km = 14.0 microM), which are among the major products of lipid peroxidation. Similar kinetic constants were observed with the human recombinant ALDH1A1 protein, which was expressed and purified using similar experimental conditions. These data suggest that ALDH1A1 may contribute to corneal cellular defense against oxidative damage by metabolizing toxic aldehydes produced during UV-induced lipid peroxidation.

Topics: Aldehyde Dehydrogenase; Aldehyde Dehydrogenase 1 Family; Aldehydes; Amino Acid Sequence; Animals; Baculoviridae; Base Sequence; Blotting, Western; Cloning, Molecular; Cornea; DNA, Complementary; Excitatory Amino Acid Antagonists; Gene Expression Regulation, Enzymologic; Humans; Immunoenzyme Techniques; Isoenzymes; Malondialdehyde; Molecular Sequence Data; Phenobarbital; Rabbits; Recombinant Proteins; Retinal Dehydrogenase; Sequence Homology, Amino Acid

Oxidized lipoproteins inhibit TNF-alpha secretion by human THP-1 macrophages due, at least in part, to aldehydes derived from the oxidation of polyunsaturated fatty acids. This study extends these findings by investigating the effect of three aldehydes (2,4-decadienal (2,4-DDE), hexanal and 4-hydroxynonenal (4-HNE)) on TNF-alpha and IL-1beta mRNA expression. The 2,4-DDE and 4-HNE showed considerable biological activity which induced cytotoxicity on THP-1 macrophages at concentration of 50 microM. Hexanal, on the other hand, had a lower cytotoxic capacity and concentration of 1000 microM was needed for the effect to be observed. Exposure of THP-1 macrophages to aldehydes for 24 h inhibited TNF-alpha mRNA expression but increased or did not affect IL-1beta mRNA levels. The inhibitory action of 2,4-DDE was dose dependent and began at 5 microM (46%, P<0.001). The effect of 4-HNE was less inhibitory than 4-DDE but only when cytotoxic concentrations were used (50 microM). Very high concentrations of hexanal (200 microM) were needed to inhibit TNF-alpha expression (23%, P<0.001). This downregulation of TNF-alpha gene expression by 2,4-DDE was parallel to a lower protein production. These data indicate that low levels of 2,4-DDE may modulate inflammatory action by inhibiting TNF-alpha mRNA gene expression and that the biological activity of 2,4-DDE may be involved in the development of atherosclerosis.

Topics: Aldehydes; Dose-Response Relationship, Drug; Down-Regulation; Gene Expression; Humans; Interleukin-1; Macrophages; RNA, Messenger; Tumor Cells, Cultured; Tumor Necrosis Factor-alpha

Radiation-induced lipid peroxidation and its association with antioxidant vitamins in the bone marrow (BM), of rats subjected to total body irradiation (TBI) of X-rays at a dose of 3 Gy was investigated. The concentration of vitamin C in the BM decreased at 4 h, and reached about 2% of the control level at 24 h after irradiation. The concentration of vitamin E in the BM also decreased to 43% at 24 h. Corresponding to the decrease in vitamin E concentration, the concentration of 4-hydroxynonenal (HNE) in the BM increased 2.5-fold at 24 h. Similarly, increases in the concentrations of hexanal and thiobarbituric acid-reactive substances (TBA-RS) were detected in the BM. In the plasma, these parameters of lipid peroxidation were unchanged up to 48 h, but were increased at 96 h after irradiation. Four days of vitamin E administration to rats (p.o. 460 mg/kg body weight) prior to the 3 Gy X-irradiation increased the vitamin E concentration in the BM to 1.3-fold the control level, but did not attenuate the increases in HNE and hexanal in the BM. The slight accumulation of vitamin E in the BM as a result of the vitamin E treatment may be partly related to this lack of vitamin E effect.

Topics: Aldehydes; Animals; Antioxidants; Bone Marrow; Cysteine Proteinase Inhibitors; Lipid Peroxidation; Male; Rats; Rats, Wistar; Time Factors; Vitamin E; Vitamins; Whole-Body Irradiation

Inhibition of conceptal biosynthesis of all-trans-retinoic acid (t-RA) by aldehydes generated from lipid peroxidation was investigated. Oxidative conversion of all-trans-retinal (t-RAL, 18 microM) to t-RA catalyzed by rat conceptal cytosol (RCC) was sensitive to inhibition by trans-2-nonenal (tNE), nonyl aldehyde (NA), 4-hydroxy-2-nonenal (4HNE), and hexanal. With an initial molar ratio of aldehyde/t-RAL of 2:1, tNE, NA, and 4HNE caused 70, 65, and 40% reductions of t-RA synthesis, respectively. Hexanal reduced generation of t-RA by approximately 50% as the ratio of aldehyde/t-RAL was raised to 20:1. tNE significantly increased the Km of the reaction and kinetic analyses indicated a mixed competitive/noncompetitive inhibition. By contrast, analogous reactions catalyzed by adult rat hepatic cytosol (ARHC) were highly resistant to inhibition by the same aldehydes. Significant inhibition (> 40% reduction of t-RA generation) by 4HNE, NA, and tNE were achieved at high molar ratios of aldehyde/t-RAL (> 175:1). Hexanal did not inhibit the reaction significantly even at very high ratios of aldehyde/t-RAL (> 2,000:1). Interestingly, when reduced glutathione (GSH, 10 mM) alone or GSH plus glutathione S-transferase (GST) were added to RCC-catalyzed reactions, additions of tNE or 4HNE showed either no significant inhibition or a partial lack of inhibition. Results suggested that GSH-dependent conjugation with 4HNE proceeded slowly compared to conjugation with tNE. To test the hypothesis that GST-catalyzed GSH conjugation can effectively prevent inhibition of t-RA synthesis by aldehydic products of lipid peroxidation, triethyltin bromide (TEB, a potent inhibitor of GST, 20 microM) was added to ARHC-catalyzed reactions when hexanal or tNE were present in the incubations. Eighty and 60% of hexanal and tNE inhibition, respectively, were observed. This was apparently due to TEB blockage of GST-catalyzed GSH conjugation reactions and thus strongly supported the stated hypothesis.

Topics: Aldehydes; Animals; Embryo, Mammalian; Female; Glutathione; Glutathione Transferase; Kinetics; Lipid Peroxidation; Pregnancy; Rats; Rats, Sprague-Dawley; Tretinoin

Oxidative stress is known to cause oxidative protein modification and the generation of reactive aldehydes derived from lipid peroxidation. Extent and kinetics of both processes were investigated during oxidative damage of isolated rat liver mitochondria treated with iron/ascorbate. The monofunctional aldehydes 4-hydroxynonenal (4-HNE), n-hexanal, n-pentanal, n-nonanal, n-heptanal, 2-octenal, 4-hydroxydecenal as well as thiobarbituric acid reactive substances (TBARS) were detected. The kinetics of aldehyde generation showed a lag-phase preceding an exponential increase. In contrast, oxidative protein modification, assessed as 2,4-dinitrophenylhydrazine (DNPH) reactive protein-bound carbonyls, continuously increased without detectable lag-phase. Western blot analysis confirmed these findings but did not allow the identification of individual proteins preferentially oxidized. Protein modification by 4-HNE, determined by immunoblotting, was in parallel to the formation of this aldehyde determined by HPLC. These results suggest that protein oxidation occurs during the time of functional decline of mitochondria, i.e. in the lag-phase of lipid peroxidation. This protein modification seems not to be caused by 4-HNE.

Topics: Aldehydes; Animals; Antibodies; Blotting, Western; Chromatography; Fatty Acids; Glutathione; Kinetics; Lipid Peroxidation; Mitochondria, Liver; Oxidative Stress; Phenylhydrazines; Proteins; Rats; Rats, Wistar; Spectrophotometry; Thiobarbituric Acid Reactive Substances

Previous studies suggest oxygen free radicals' involvement in the etiology of cardiomyopathy with cataracts. To investigate the role of free radicals in the pathogenesis of the cardiomyopathy with cataracts and complex I deficiency, fibroblasts from patients were assessed for hydroxyl radical formation and aldehydic lipid peroxidation products with and without redox active agents that increase free radicals. The rate of hydroxyl radical formation in patient cells was increased over 2-10-fold under basal conditions, and up to 20-fold after menadione or doxorubicin treatment compared with normal cells. We also found an overproduction of aldehydes in patient cells both under basal conditions and after treatment. Both hydroxyl radicals and toxic aldehydes such as hexanal, 4-hydroxynon-2-enal, and malondialdehyde were elevated in cells from patients with three types of complex I deficiency. In contrast, acyloins, the less toxic conjugated products of pyruvate and saturated aldehydes, were lower in the patient cells. Our data provide direct evidence for the first time that complex I deficiency is associated with excessive production of hydroxyl radicals and lipid peroxidation. The resultant damage may contribute to the early onset of cardiomyopathy and cataracts and death in early infancy in affected patients with this disease.

Topics: Aldehydes; Cardiomyopathies; Cataract; Cells, Cultured; Fatal Outcome; Female; Fibroblasts; Humans; Hydroxyl Radical; Infant, Newborn; Lipid Peroxidation; Malondialdehyde; NAD(P)H Dehydrogenase (Quinone); Skin

We have investigated the cytotoxic and chemotactic potencies of malondialdehyde (MDA), hexanal, 4-hydroxyhexenal (HHE), 4-hydroxynonenal (HNE) and 4-hydroxyoctenal (HOE), which are aldehydes found in oxidised low density lipoprotein (LDL), for human monocyte-macrophages. They were toxic in the following order: hexanal

Topics: Aldehydes; Chemotactic Factors; Cytotoxins; Humans; Lipoproteins, LDL; Macrophages; Malondialdehyde; Monocytes; Oxidation-Reduction

Cytokines produced by mononuclear leukocytes infiltrating pancreatic islets are candidate mediators of islet beta-cell destruction in autoimmune insulin-dependent diabetes mellitus. Cytokines may damage islet beta-cells by inducing oxygen free radical production in the beta-cells. Lipid peroxidation and aldehyde production are measures of oxygen free radical-mediated cell injury. In the current study, we used a HPLC technique to measure levels of different aldehydes produced in rat islets incubated with cytokines. The cytokine combination of interleukin-1beta (10 U/ml), tumor necrosis factor-alpha (10(3) U/ml), and interferon-gamma (10(3) U/ml), and the oxidant, t-butylhydroperoxide, induced significant increases in islet levels of the same aldehydes: butanal, pentanal, 4-hydroxynonenal (4-HNE), and hexanal. Cytokine-induced aldehyde production was associated with islet beta-cell destruction. Thus, cytokine-induced increases in malondialdehyde (MDA; at 4 h) and 4-HNE (at 8 h) preceded islet cell destruction (at 16 h), and the addition of 4-HNE, hexanal, MDA, and pentanal (1-200 microM) to th islets, but not other aldehydes at similar concentrations, produced dose-dependent destruction of islet beta-cells. Furthermore, an antioxidant (lazaroid U78518E) prevented cytokine-induced increases in 4-HNE, hexanal, and MDA and significantly inhibited cytokine-induced decreases in insulin and DNA in the islets. In contrast, N(G)-monomethyl-L-arginine, an inhibitor of nitric oxide synthase, prevented cytokine-induced nitrite production, but did not prevent cytokine-induced increases in 4-HNE, hexanal, and MDA or decreases in insulin and DNA in the islets. These results suggest that cytokines may damage islet beta-cells by inducing oxygen free radicals, lipid peroxidation, and, consequently, the formation of cytotoxic aldehydes in the islet cells.

Topics: Aldehydes; Animals; Cell Death; Chromatography, High Pressure Liquid; Cytokines; Interferon-gamma; Interleukin-1; Islets of Langerhans; Male; Malondialdehyde; Rats; Rats, Sprague-Dawley; Tumor Necrosis Factor-alpha

The relative contribution of the aldehyde dehydrogenase (EC 1.2.1.3, ALDH) and glutathione (GSH) conjugate system to the degradation of (E)-4-hydroxy-2-nonenal (4HN), a toxic breakdown product arising from lipid peroxidation, was investigated in rat liver. Significant increases in the contents of 4HN and hexanal (HA) and a decrease of ALDH but not alcohol dehydrogenase (EC 1.1.1.2, ADH) activity were recognized in rat liver following administration of carbon tetrachloride (3 ml/kg, p.o.). Hepatic ALDH activity was correlated with HA production (r = -0.82, P < 0.01) but not with 4HN. When lipid peroxidation was induced by t-butyl hydroperoxide, the ratio of HA to 4HN production in the liver of rats pretreated with the ALDH inhibitor, cyanamide (100 mg/kg, i.p.) was higher than that in controls, whereas the ratio was lower in the liver of rats pretreated with the glutathione-depleting agent, phorone (250 mg/kg, i.p.). These results suggest that 4HN in rat liver is metabolized by the GSH-conjugate system in preference to degradation by ALDH.

Topics: Alcohol Dehydrogenase; Aldehyde Dehydrogenase; Aldehydes; Animals; Biodegradation, Environmental; Carbon Tetrachloride; Cyanamide; Glutathione; Ketones; Kinetics; Lipid Peroxidation; Liver; Male; Peroxides; Rats; Rats, Wistar; Reactive Oxygen Species; tert-Butylhydroperoxide; Thiobarbituric Acid Reactive Substances

Indices of lipid peroxidation were investigated in muscle tissues of 1) calves depleted of vitamin E and/or Se and 2) calves depleted of vitamin E and Se and fed daily supplements of polyunsaturated fatty acids (PUFA). Calves deficient in both vitamin E and Se or deficient in vitamin E alone showed elevated muscle concentrations of thiobarbituric acid-reactive substances (TBARS), ascorbate-induced TBARS (ATBARS), ascorbate-induced hexanal and iron-induced 4-hydroxynonenal (HNE). Muscle tissue of calves depleted of Se alone showed no increases in these indices of lipid peroxidation. Two further groups of calves were fed diets either sufficient or deficient in both vitamin E and Se. Both of these groups were then fed linseed oil, protected against ruminal hydrogenation, as a source of PUFA. The deficient animals had higher muscle concentrations of all three indices of lipid peroxidation than the supplemented calves. Furthermore, feeding PUFA to vitamin E and Se deficient animals increased muscle concentrations of induced HNE to levels above those in deficient animals not fed PUFA supplements.

Topics: Aldehydes; Animals; Ascorbic Acid; Cattle; Cattle Diseases; Creatine Kinase; Erythrocytes; Fatty Acids, Unsaturated; Glutathione Peroxidase; Lipid Peroxidation; Malondialdehyde; Muscles; Random Allocation; Selenium; Thiobarbituric Acid Reactive Substances; Vitamin E; Vitamin E Deficiency

Effects of lipid peroxide breakdown products, (E)-4-hydroxy-2-nonenal (4-HN) and n-hexanal, on mouse lung lesion were examined. When 4-HN was injected i.v., the plasma level of 4-HN increased just after the injection and then decreased immediately. The amounts of 4-HN increased in the liver and lung were ca. 0.085 and 0.43% to the dose administered, respectively, 5 min after the injection. Reduced glutathione (GSH) content and both GSH peroxidase (GSH-Px) and GSH reductase (GSSGR) activities in the lung were decreased significantly by 4-HN treatment. On the other hand, in the case of i.v. injection of n-hexanal into mice, the amount of n-hexanal detected in the lung was 5.0% to that of 4-HN, and no effect on the activities of GSH-Px and GSSGR and the content of GSH was observed. These results suggest that 4-HN generated from lipid peroxides would be transferred into the lung and cause the lung lesion through the inhibition of GSH-dependent antioxidative defense systems.

Topics: Aldehydes; Animals; Glutathione; Glutathione Peroxidase; Glutathione Reductase; Injections, Intravenous; Lipid Peroxidation; Liver; Lung; Male; Mice; Thiobarbituric Acid Reactive Substances

Peroxidation of lipids produces carbonyl compounds; some of these, e.g., malonaldehyde and 4-hydroxynonenal, are genotoxic because of their reactivity with biological nucleophiles. Analysis of the reactive carbonyl compounds is often difficult. The methylhydrazine method developed for malonaldehyde analysis was applied to simultaneously measure the products formed from linoleic acid, linolenic acid, arachidonic acid, and squalene upon ultraviolet-irradiation (UV-irradiation). The photoreaction products, saturated monocarbonyl, alpha,beta-unsaturated carbonyls, and beta-dicarbonyls, were derivatized with methylhydrazine to give hydrazones, pyrazolines, and pyrazoles, respectively. The derivatives were analyzed by gas chromatography and gas chromatography-mass spectrometry. Lipid peroxidation products identified included formaldehyde, acetaldehyde, acrolein, malonaldehyde, n-hexanal, and 4-hydroxy-2-nonenal. Malonaldehyde levels formed upon 4 hr of irradiation were 0.06 micrograms/mg from squalene, 2.4 micrograms/mg from linolenic acid, and 5.7 micrograms/mg from arachidonic acid. Significant levels of acrolein (2.5 micrograms/mg) and 4-hydroxy-2-nonenal (0.17 micrograms/mg) were also produced from arachidonic acid upon 4 hr irradiation.

Topics: Acetaldehyde; Acrolein; Aldehydes; Arachidonic Acid; Arachidonic Acids; Chromatography, Gas; Formaldehyde; Gas Chromatography-Mass Spectrometry; Linoleic Acid; Linoleic Acids; Linolenic Acids; Lipid Peroxidation; Lipids; Malondialdehyde; Monomethylhydrazine; Squalene; Ultraviolet Rays

In order to evaluate the pro-hemolytic action exerted by different classes of biogenic aldehydes, normal red cells obtained from human beings of both sexes were incubated at 37 degrees C under iso or hypo-osmotic conditions in the presence of hydroxyalkenals or alkanals, in a concentration compatible with those actually recovered during red cell lipid peroxidation. None of the tested aldehydes showed a direct hemolytic effect, i.e. red cell lysis in iso-osmotic conditions. Conversely, almost all assayed alkanals and hydroxyalkenals exhibited a pre-lytic damage of human erythrocytes, as detected in the red cells suspended in hypo-osmotic medium. The highest pro-hemolytic effect was displayed by hexanal, nonanal, 2-nonenal and 4-hydroxynonenal.

Topics: Aldehydes; Erythrocytes; Female; Hemolysis; Humans; Lipid Peroxidation; Male

The addition of lipid peroxidation end-products, 4-hydroxynonenal (HNE) or hexanal (HEX) to the incubation medium of rat hepatocytes caused significant decrease of cell cytochrome P-450 content and inactivation of total cell glucose-6-phosphatase. Both the tested aldehydes exerted a marked inhibition of triglyceride secretion by liver cells. The reported results on intact cells furtherly support a possible damaging effect of aldehydes in pathological conditions in which a stimulation of lipid peroxidation occurs.

Topics: Aldehydes; Animals; Cytochrome P-450 Enzyme System; Glucose-6-Phosphatase; Liver; Male; Rats; Rats, Inbred Strains; Triglycerides

The addition of lipid peroxidation end-products, 4-hydroxypentenal (HPE), 4-hydroxynonenal (HNE) or hexanal (HEX) to the incubation medium of rat hepatocytes caused a significant decrease of cytochrome P-450 content and inactivation of total cell glucose-6-phosphatase. In particular, the two hydroxyalkenals exerted their inhibitory action at micromolar concentration. These results on intact cells further support a possible damaging effect of aldehydes in pathological conditions in which a stimulation of lipid peroxidation occurs.

Topics: Aldehydes; Animals; Cytochrome P-450 Enzyme System; Glucose-6-Phosphatase; In Vitro Techniques; Lipid Peroxides; Liver; Male; Rats; Rats, Inbred Strains