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PubMed1987

Acetaldehyde and ethanol biosynthesis in leaves of plants.

Leaves of terrestrial plants are aerobic organs, and are not usually considered to possess the enzymes necessary for biosynthesis of ethanol, a product of anaerobic fermentation. We examined the ability of leaves of a number of plant species to produce acetaldehyde and ethanol anaerobically, by incubating detached leaves in N(2) and measuring headspace acetaldehyde and ethanol vapors. Greenhouse-grown maize and soybean leaves produced little or no acetaldehyde or ethanol, while leaves of several species of greenhouse-grown woody plants produced up to 241 nanograms per milliliter headspace ethanol in 24 hours, corresponding to a liquid-phase concentration of up to 3 milligrams per gram dry weight. When leaves of 50 plant species were collected in the field and incubated in N(2), all higher plants produced acetaldehyde and ethanol, with woody plants generally producing greater amounts (up to 1 microgram per milliliter headspace ethanol concentration). Maize and soybean leaves from the field produced both acetaldehyde and ethanol. Production of fermentation products was not due to phylloplane microbial activity: surface sterilized leaves produced as much acetaldehyde and ethanol as did unsterilized controls. There was no relationship between site flooding and foliar ethanol biosynthesis: silver maple and cottonwood from upland sites produced as much acetaldehyde and ethanol anaerobically as did plants from flooded bottomland sites. There was no relationship between flood tolerance of a species and ethanol biosynthesis rates: for example, the flood intolerant species Quercus rubra and the flood tolerant species Quercus palustris produced similar amounts of ethanol. Cottonwood leaves produced more ethanol than did roots, in both headspace and enzymatic assays. These results suggest a paradox: that the plant organ least likely to be exposed to anoxia or hypoxia is rich in the enzymes necessary for fermentation.

Journal Article↗
PubMed1991

Formation of a 37 kilodalton liver protein-acetaldehyde adduct in vivo and in liver cell culture during chronic alcohol exposure.

With the use of antibodies that can recognize acetaldehyde adducts and the application of various immunological techniques, several protein-AAs have now been shown to form in vivo during chronic alcohol ingestion. These protein-AAs include the 37-kDa liver protein-AA, the CytP450IIE1-AA, hemoglobin-AA, two serum protein-AAs with molecular weights of 50 kDa and 103 kDa, and collagen type I protein-AA in liver. If acetaldehyde is the agent responsible for alcoholic liver injury, acetaldehyde toxicity in chronic alcohol ingestion must be linked to the ability of acetaldehyde to form adducts with proteins and perhaps other macromolecules. This is at least one mechanism of acetaldehyde-mediated liver injury. For proteins that serve critical functions, acetaldehyde adduct formation may alter their functions and thereby produce organ damage. Acetaldehyde adduct formation can also elicit humoral or cytotoxic immune responses and these responses may also lead to organ injury.

Animals↗
PubMed2002

Modification of the acetaldehyde concentration during alcoholic fermentation and effects on fermentation kinetics.

We studied the kinetic effects of increasing the residual acetaldehyde concentration during alcoholic fermentation, especially during the stationary phase. We added this compound via pulse or continuous injections. The yeast response depended on the amount of acetaldehyde added: high concentrations inhibited fermentation while low concentrations led to stimulation. When regular small additions were made, up to 100 mM acetaldehyde could be added and this caused a very significant drop in the fermentation duration. We also modulated the acetaldehyde concentration by modifying the alcohol dehydrogenase-catalyzed reaction. Two approaches were tested (i) adding aldehydes (propanal and furfural) that competitively inhibited the reduction of acetaldehyde and (ii) adding electron acceptors that reduced the quantity of NADH available. Several possible mechanisms responsible for (i) the impact of acetaldehyde on fermentation kinetics and (ii) the modulation of the residual acetaldehyde concentration are discussed.

Journal Article↗
PubMedDate not supplied

Acetaldehyde stimulates collagen and noncollagen protein production by human fibroblasts.

The mechanisms responsible for the increased hepatic collagen deposition in alcoholic cirrhosis remain unknown. The question of whether ethanol or acetaldehyde has a direct effect on collagen and noncollagen protein production was investigated in human fibroblasts with no detectable activity of alcohol dehydrogenase to distinguish the effects of these metabolites. To eliminate environmental factors, protein production by confluent human skin, fetal and hepatic fibroblasts was studied after three passages. Cells were labeled with [5-3H]proline for 4 hr in the presence of 0.2 mM ascorbate alone or with addition of either ethanol (50 mM) or acetaldehyde (0 to 300 microM). Rates of protein production were calculated from the radioactivities of collagenase-sensitive and collagenase-resistant proteins. Skin fibroblasts from alcoholic individual either with cirrhosis or without liver disease have comparable rates of collagen and noncollagen protein production. Acetaldehyde, in a concentration found in the liver during ethanol abuse, significantly increased collagen production by human skin fibroblasts (up to 140%), fetal fibroblasts (up to 240%) and hepatic fibroblasts (up to 70%) but the addition of ethanol had no significant effect on basal collagen production. The effect of acetaldehyde was dose-related and affected noncollagen protein production in a similar manner. Acetaldehyde did not cause changes in either proline transport or the specific activity of the proline precursor pool. This newly recognized stimulation of collagen production by acetaldehyde may be a possible mechanism of fibrogenesis in alcoholic individuals.

Acetaldehyde↗
PubMedDate not supplied

Antibodies against acetaldehyde-modified protein epitopes in human alcoholics.

Acetaldehyde, the primary metabolite of ethanol, binds covalently to proteins forming condensation products which have been recently shown to be immunogenic. To assess whether an antibody response against acetaldehyde-modified protein epitopes is associated with alcoholic liver disease, the serum immunoreactivity against proteins modified in vitro by acetaldehyde and against the corresponding unmodified proteins was measured by an enzyme-linked immunosorbent assay in 58 alcoholics with varying degrees of liver damage. Alcoholics showed significantly higher titers against protein-acetaldehyde conjugates than against the unmodified protein, independent of the nature of the carrier protein. The highest titers occurred in alcoholic hepatitis patients. Sera of patients with chronic hepatitis of nonalcoholic origin and of healthy controls also reacted with acetaldehyde conjugates, but their titers were significantly lower than those in alcoholic hepatitis patients. Our data support the idea that binding of acetaldehyde to proteins in humans generates antigenic determinants which trigger a corresponding immune response against such epitopes and suggest that this humoral immune response may be implicated in autoantibody formation and liver damage associated with excessive alcohol consumption.

Acetaldehyde↗
PubMed1992

Polyunsaturated lecithin prevents acetaldehyde-mediated hepatic collagen accumulation by stimulating collagenase activity in cultured lipocytes.

We recently found that polyunsaturated lecithin prevents ethanol from causing cirrhosis in the baboon. Because transformation of lipocytes to transitional cells plays a key role in hepatic fibrogenesis in vivo, and because this process in alcohol-fed baboons was found to be attenuated by polyunsaturated lecithin, we focused on lipocytes to study the mechanism of the protective effect. Rat lipocytes cultured on plastic undergo spontaneous activation, accompanied by expression of alpha-smooth muscle actin isoform and production of substantial amounts of type I collagen. The latter was further increased on incubation with acetaldehyde. This in vitro model was used here to study how acetaldehyde-mediated collagen production and accumulation can be turned off. Addition of polyunsaturated lecithin (10 mumols/L) was found to prevent the acetaldehyde-induced increase in collagen accumulation by 83% (p less than 0.001). By contrast, a saturated phospholipid (10 mumols/L dilauroyl phosphatidylcholine), a monounsaturated one (10 mumols/L linoleoyl-palmitoyl phosphatidylcholine) or linoleic acid (20 mumols/L bound to albumin) had no such effect. Incorporation of [3H]proline into collagen and the expression of alpha-1 (I) procollagen mRNA were increased by acetaldehyde; the latter was not significantly affected by polyunsaturated lecithin. Polyunsaturated lecithin increased lipocyte collagenase activity by 100% (p less than 0.001), whereas dilauroyl phosphatidylcholine, linoleoyl-palmitoyl phosphatidylcholine and linoleic acid had no such action. We concluded that (a) polyunsaturated lecithin selectively prevents the acetaldehyde-induced increase in collagen accumulation in lipocyte cultures, whereas other phospholipids or linoleate have no such effect; and (b) polyunsaturated lecithin does not modify the acetaldehyde-mediated increase in alpha-1 (I) procollagen mRNA, but it increases collagenase activity, suggesting that the protective effect exerted by polyunsaturated lecithin against alcohol induced fibrosis in vivo is due at least in part to stimulation of collagenase activity, which may prevent excess collagen accumulation by offsetting increased collagen production.

Acetaldehyde↗
PubMed1997

Acetaldehyde-modified and 4-hydroxynonenal-modified proteins in the livers of rats with alcoholic liver disease.

Liver proteins form adducts with acetaldehyde and are modified by products of lipid peroxidation in alcohol-fed animals. It has been hypothesized that the formation of these modified liver proteins may contribute to liver injury in alcoholic liver disease. The present work was performed to determine the extent of protein modification in rats with experimental alcoholic liver disease. Rats were fed ethanol intragastrically with medium chain triglycerides (MCTs), palm oil, corn oil, or fish oil. The group fed MCTs and ethanol showed no liver injury, rats fed palm oil and ethanol showed only fatty liver, rats fed corn oil and ethanol showed fatty liver with moderate necrosis and inflammation, and rats fed fish oil and ethanol showed fatty liver with severe necrosis and inflammation. Antibodies were raised by using keyhole limpet hemocyanin modified in vitro by 4-hydroxynonenal (4-HNE) or acetaldehyde as immunogens. When liver extracts were examined by Western blot analysis, the intensities of the acetaldehyde-modified protein band (37 kd) in the alcohol-fed animals were significantly different among the ethanol-treated groups and correlated with plasma acetaldehyde concentrations. It was strongest in rats fed fish oil and ethanol, followed by rats fed palm oil and ethanol and rats fed corn oil and ethanol, whereas rats fed MCTs and ethanol showed the weakest intensity. The 37-kd protein-adetaldehyde adduct was located mainly in the pericentral region of the liver. No acetaldehyde adduct was detected in the control rats that were pair-fed with isocaloric amounts of dextrose. Western blot analysis using the anti-4-HNE antibody showed four distinctive bands (48, 45, 40, and 38 kd) in the liver extracts of alcohol-fed rats. Control animals showed only a weak 38-kd band. Although the intensities of the 48-, 40-, and 38-kd bands were similar among the different ethanol-treated groups, the intensity of the 45-kd band decreased from MCTs and ethanol > palm oil and ethanol > or = corn oil and ethanol > fish oil and ethanol. The data indicate that the degree of liver protein modification by acetaldehyde correlates well with the severity of liver injury in ethanol-fed rats, whereas modification by the lipid peroxidation product 4-HNE shows no correlation with the severity of liver injury.

Acetaldehyde↗
PubMed1999

Differential role of ethanol and acetaldehyde in the induction of oxidative stress in HEP G2 cells: effect on transcription factors AP-1 and NF-kappaB.

The oxidative metabolism of ethanol by the cytochrome P450 2E1 (CYP2E1) has been recognized to contribute to the ethanol-induced deleterious effects through the induction of oxidative stress. This study compared the effect of ethanol and acetaldehyde in the induction of oxidative stress and activation of transcription factors nuclear factor-kappaB (NF-kappaB) and activating protein 1 (AP-1) in HepG2 cells, which do not express CYP2E1, and HepG2 cells transfected with CYP2E1 (E47 cells). Neither ethanol (80 mmol/L) nor acetaldehyde (25-200 micromol/L) caused oxidative stress in HepG2 cells, an effect that was independent of blocking reduced glutathione (GSH) synthesis with buthionine-L-sulfoximine (BSO). However, BSO preincubation caused an overproduction of peroxides and activation of NF-kappaB and AP-1 in E47 cells even in the absence of ethanol. Furthermore, the incubation of E47 cells with ethanol (80 mmol/L for up to 5 days) depleted cellular GSH stores in both cytosol and mitochondria, reflecting the induction of oxidative stress. Ethanol activated NF-kappaB and AP-1 in E47 cells, an effect that was prevented by 4-methylpyrazole, potentiated by cyanamide, and attenuated by trolox C. Interestingly, however, despite the inability of acetaldehyde to induce oxidative stress in HepG2, acetaldehyde activated NF-kappaB and AP-1; in contrast, ethanol failed to activate these transcription factors in HepG2. Thus, our findings indicate that activation of NF-kappaB and AP-1 by ethanol and acetaldehyde occurs through distinct mechanisms. CYP2E1 is indispensable in the induction of oxidative stress from ethanol, whereas the activation of NF-kappaB and AP-1 by acetaldehyde is independent of oxidative stress.

Acetaldehyde↗
PubMed1983

Urinary excretion products after the administration of 14C-acetaldehyde to rats.

Rats were injected with 120 micro Ci of 14C-acetaldehyde containing carrier acetaldehyde, and the urinary excretion products were assayed by cation exchange chromatography, resolving five main peaks of radioactivity. Urine contained 6% of the dose of 14C-acetaldehyde administered. The main urinary product of acetaldehyde, fraction 5, was produced via acetate. Acetate was also identified in the urine. Two cysteine adducts, probably isomeric metabolites of 2-methylthiazolidine-4-carboxylic acid, were detected. They constituted about 2% of the radioactivity in the urine collected 48 h after the administration of 14C-acetaldehyde. They appeared to retain a carboxylic group. When the reaction mixture of 14C-cysteine and acetaldehyde was injected into a rat, the half-lives of the two tiazolidine derivatives was 10 h. Only 13.6% of the radioactivity was detected in the urine suggesting ready metabolism of 2-methylthiazolidine-4-carboxylic acid.

Acetaldehyde↗
PubMed2002

Kinetics and isotope patterns of ethanol and acetaldehyde emissions from yeast fermentations of glucose and glucose-6,6-d2 using selected ion flow tube mass spectrometry: a case study.

As a prelude to investigations of the emission of metabolites from human cell lines in vitro, we have conducted a study using selected ion flow tube mass spectrometry (SIFT-MS) of the acetaldehyde and ethanol that appear in the headspace above a fermenting yeast/glucose/water mixture in sealed glass bottles at a temperature of 30 degrees C. A fixed quantity of yeast (10 mg) and varying amounts (2, 4, 8 and 16 mg) of both non-deuterated glucose and glucose-6,6-d2 in 5 mL of water were used and the emission of the acetaldehyde and the ethanol were observed as a function of time. The ethanol and acetaldehyde concentrations in the headspace were obtained from the magnitudes of their characteristic ions on the accumulated SIFT mass spectra and, when the deuterated glucose was used, characteristic singly and doubly deuterated ions were obvious. This study indicates, as expected, that ethanol is the major species generated and that acetaldehyde is a relatively minor component of the headspace and a very minor component of the liquid phase. We estimate that about 10(8) ethanol molecules are produced per minute per cell in this yeast fermentation process. The distribution of the non-deuterated and partially deuterated ethanol under these fermentation conditions is observed to be C2H5OH (66 +/- 4)%, C2H4DOH(6 +/- 1)%, C2H3D2OH(28 +/- 4)%, and the analogous distribution for the acetaldehyde is the same, within error. These results indicate that the D atoms in the glucose-6,6-d2 are mostly retained by the 6-C atom, but the appearance of the singly deuterated ethanol and acetaldehyde indicates that some D/H mixing must be occurring in the enzymatic reactions. The results of this study illustrate the potential and power of on-line SIFT-MS analysis in this area of research.

Acetaldehyde↗
PubMed1996

Activation by acetaldehyde of the promoter of the mouse alpha2(I) collagen gene when transfected into rat activated stellate cells.

The effect of acetaldehyde in activating the mouse alpha2(I) collagen promoter in transiently transfected rat activated stellate cells and the possible mediating effect of transforming growth factor beta1 (TGFbeta1) on type I collagen gene expression were determined. Acetaldehyde and TGFbeta1, each had a similar effect in activating the wild-type promoter, but failed to activate the promoter with a -352 to -104 deletion, or the promoter containing a 3-bp substitution between -305 and -303 in the putative nuclear factor I (NF-I) binding site. The effects of acetaldehyde and TGFbeta1 are therefore mediated by a similar factor or factors that bind to the NF-I consensus sequence within the region -352 to -104. Additional factors may also play a role in the effects of acetaldehyde and TGFbeta1, which have similar effects on the wild-type promoter, but become additive in activating the promoter with a more distal deletion containing a cis-repressor element. Pretreatment of activated stellate cells with antibodies to TGFbeta1 suppressed the effect of acetaldehyde in increasing the alpha1(I) collagen message, indicating that TGFbeta1 mediates the effect of the acetaldehyde-induced increase in the expression of the alpha1(I) collagen gene which also contains NF-I binding sites.

Acetaldehyde↗
PubMed1997

Effect of acetaldehyde on Sp1 binding and activation of the mouse alpha 2(I) collagen promoter.

Acetaldehyde activates the mouse alpha 2(I) collagen promoter and this effect is mediated in part by increased binding of nuclear factor I (NF-I). Additional mechanisms may exist since deletions in the promoter upstream to the NF-I binding site prevented enhancement by acetaldehyde. Three adjacent areas of binding by nuclear proteins from activated hepatic stellate cells were identified at -568 to -554 (region 1), -542 to -518 (region 2), and -473 to -453 (region 3) of the promoter using DNase I protection analyses. Multiple DNA-protein complexes were formed in electrophoretic mobility shift assays with oligonucleotide probes specifying the three regions. Sp1 and NF-1 bound to all three regions, while Sp3 bound to region 2. Acetaldehyde decreased nuclear protein binding to all three regions. Mutations of regions 1, 2, and 3 reduced basal activity of the promoter and inhibited acetaldehyde stimulation in transfected stellate cells. Acetaldehyde inhibited the stimulatory effect of the Sp1 vector pPacSp1 on the promoter in transfected Drosophila cells. In conclusion, three regions of Sp1 binding were identified and are required for optimal activity of the alpha 2(I) collagen promoter. Sp1 is required for basal activity of the alpha 2(I) collagen promoter; however, the enhancing effect of acetaldehyde on the promoter is not mediated by Sp1.

Acetaldehyde↗
PubMed2000

Effect of retinoic acid on the enhancing effect of acetaldehyde on mouse type I collagen expression.

Acetaldehyde alone and retinoic acid alone have been shown to increase and decrease, respectively, collagen production by stellate cells in culture. In this study the effects of retinoic acid on alpha(1)(I) and alpha(2)(I) collagen expression and its influence on the enhancing effects of acetaldehyde were determined. Retinoic acid decreased the activation of the alpha(2)(I) collagen promoter and decreased the message of alpha(2)(I) collagen in cultured stellate cells, but had no effect on either the activation of the alpha(1)(I) collagen promoter or on the alpha(1)(I) collagen message. This depressant effect of retinoic acid was also evident in the transfected alpha(2)(I) collagen promoter mutated at the retinoic acid response element (RARE). The activation of the alpha(2)(I) collagen promoter by acetaldehyde was not decreased significantly by retinoic acid, but was suppressed by the retinoic acid receptor (RAR) selective retinoid SRI-6751-84. Retinoic acid, however, decreased the acetaldehyde-induced enhancement of the alpha(1)(I) and alpha(2)(I) collagen messages. Acetaldehyde also resulted in a decrease in RAR beta message and RARbeta protein. This study shows that retinoic acid depresses alpha(2)(I) collagen gene expression but that this effect is less pronounced when the expression of this collagen is enhanced by acetaldehyde, which also decreases RARbeta message and protein. Furthermore, the action of retinoic acid in inhibiting alpha(2)(I) collagen gene expression occurs at sites other than the RARE site.

Acetaldehyde↗
PubMed1980

Acetaldehyde directly inhibits the conversion of androstenedione to testosterone in the testes.

The effects of ethanol and acetaldehyde on testicular steroidogenesis were examined in enzymatically dispersed cells of the rodent testes. We found that both compounds significantly inhibited the gonadotropin-stimulated biosynthesis of testosterone. Acetaldehyde was approximately 4000 times more potent than its parent compound, however. Moreover, in contrast to the effects of ethanol, acetaldehyde was effective at concentrations compatible with those found under in vivo conditions after acute ethanol administration. These data indicate that acetaldehyde is, at the least, probably an extremely important factor in the well-documented ethanol-induced inhibition of testicular steroidogenesis in vivo and further suggest that ethanol may be converted to acetaldehyde to produce its testicular toxicity. Finally, we have found that acetaldehyde blocks testicular steroidogenesis by selectively and specifically inhibiting the conversion of androstenedione to testosterone.

Acetaldehyde↗
PubMed1995

Static headspace gas chromatography of acetaldehyde in aqueous foods and polythene terephthalate.

Polythene terephthalate (PET) is frequently used as a packaging material for mineral water and other non-alcoholic beverages. PET contains detectable amounts of acetaldehyde, which is able to migrate to its packed product. An automated headspace gas chromatographic method for the determination of acetaldehyde has been developed and was used for the quantification of acetaldehyde in aqueous food products and their PET packages. A cold trap, mounted in the GC oven, between the auto sampler and analytical column was introduced as a new application. The detection limit of acetaldehyde was found to be 3 ng/ml with a standard deviation of 3%. The contents of acetaldehyde found in carbonated mineral water and lemonade ranged between 11 ng/ml and 7447 ng/ml, while the contents of acetaldehyde in the PET packages ranged from 1.1 microgram/g to 3.8 micrograms/g.

Acetaldehyde↗
PubMed1987

Effect of acetaldehyde on rat platelet aggregation in vivo and in vitro.

The effect of acetaldehyde on primary hemostasis and platelet aggregation was studied in vivo and in vitro in the rat. Acetaldehyde was found in circulation following ethanol intoxication or was present after direct i.v. injection. In vitro, acetaldehyde was added to whole blood or platelet plasma suspension. Bleeding time and blood loss were increased upon ethanol intoxication and immediately after i.v. infusion of acetaldehyde. The intrinsic coagulation system, assayed by APT-time, was unaffected. In vivo, ADP and collagen-induced platelet aggregation was inhibited upon the presence of acetaldehyde. In vitro, inhibition of platelet aggregation was observed when acetaldehyde was added to blood, while the addition of the compound to plasma did not affect platelet function.

Acetaldehyde↗
PubMed1994

Acetaldehyde alters coagulation protein function.

Acetaldehyde is the first metabolite of ethanol and has the potential to react with proteins and alter their function. This study evaluated the function of clotting proteins that had been preincubated with acetaldehyde as compared to those incubated with buffer or ethanol as controls. Thrombin, fibrinogen, thromboplastin, or whole plasma were preincubated with 1.8-447 mM acetaldehyde, 1.7-429 mM ethanol, or buffer for varying time periods prior to use in a clotting assay. Clot formation was measured with an automatic fibrometer. Acetaldehyde prolonged the clotting time but ethanol did not. These experiments indicate that circulating acetaldehyde would have the potential to react with proteins of the clotting system and alter their function. Therefore, it is possible that not all of the abnormalities in coagulation in alcohol abusers result from inadequate hepatic synthesis. Perhaps some of the deranged coagulation may be the result of the interaction of acetaldehyde with coagulation proteins.

Acetaldehyde↗
PubMed2004

Oxidation of ethanol to acetaldehyde and free radicals by rat testicular microsomes.

A large number of epidemiological studies evidencing that excessive alcohol consumption is associated with impaired testosterone production and testicular atrophy are available in the literature. One hypothesis to explain the deleterious action of alcohol involves the in situ biotransformation to acetaldehyde, but it strongly suggests the need to learn more about the enzymatic processes governing alcohol metabolism to acetaldehyde in different cellular fractions since limited information is available in the literature. In this article we report studies on the metabolic conversion of alcohol to acetaldehyde and to 1-hydroxyethyl radicals in rat testicular microsomal fractions. The oxidation of ethanol to acetaldehyde in rat testes microsomal fraction was mostly of enzymatic nature and strongly dependent on the presence of NADPH and oxygen. Several compounds were able to significantly decrease the production of acetaldehyde: SKF 525A; diethyldithiocarbamate; esculetin; gossypol; curcumin; quercetin; dapsone; and diphenyleneiodonium. Microsomal preparations in the presence of NADPH were also able to produce both hydroxyl and 1-hydroxyethyl free radicals. Their generation was modulated by the presence of diphenyleneiodonium, gossypol, and deferoxamine. Results show that rat microsomal fractions are able to metabolize alcohol to deleterious chemicals, such as acetaldehyde and free radicals, that may be involved in ethanol toxic effects. Enzymes involved could include CYP2E1, P450 reductase, and other enzymes having lipoxygenase- /peroxidase-like behavior.

Acetaldehyde↗