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PubMed1995

A structural assignment for a stable acetaldehyde-lysine adduct.

Acetaldehyde is the first oxidation product of ethanol in vivo. Lysine residues in proteins such as hemoglobin have been implicated as target structures for acetaldehyde adducts resulting from ethanol consumption. Although the presence of both stable and unstable acetaldehyde-hemoglobin adducts has been established, the structural characterization of the adducts has received relatively little attention. As a model for such adduct formation, we studied the peptide pentalysine in vitro. Pentalysine has several potential sites for adduct formation. The amino-terminal amine group as well as the epsilon-amine groups of each lysine side chain can serve as potential sites for modification by acetaldehyde. Mass spectrometry, nuclear magnetic resonance, and Raman spectroscopy were employed to demonstrate that acetaldehyde forms a stable linkage to lysine amine groups via a Schiff base.

Acetaldehyde↗
PubMed2003

Evaluation of relationships between mainstream smoke acetaldehyde and "tar" and carbon monoxide yields in tobacco smoke and reducing sugars in tobacco blends of U.S. commercial cigarettes.

Mainstream (MS) smoke acetaldehyde (AA), carbon monoxide (CO), and "tar" yields and percentage total reducing sugars in the tobacco blends from a Philip Morris USA database of a large number of commercial U.S. cigarettes were analyzed. MS smoke acetaldehyde is significantly correlated with "tar" yield and also with MS smoke carbon monoxide. These correlations are consistent with recently available data, including the 1999 Massachusetts Benchmark Study. MS smoke acetaldehyde yield is not correlated with reducing sugar (RS) concentration in the tobacco blend. For the available data over the time period 1985-1993, the concentration of reducing sugars (mean values for the brands tested) decreased. The correlations found between MS smoke acetaldehyde yield and "tar" and MS smoke carbon monoxide, and the percentage of the variance in AA yield explained by "tar" and MS smoke CO, coupled with the lack of correlation between "tar" normalized MS smoke AA and RS, plus related pyrolysis studies, support the hypothesis that MS smoke acetaldehyde yields are affected more by cigarette design characteristics influencing total smoke production than by tobacco reducing sugars.

Acetaldehyde↗
PubMed2003

Evaluation of the developmental toxicities of ethanol, acetaldehyde, and thioacetamide using FETAX.

Potential mechanisms of the developmental toxicities of ethanol, acetaldehyde, and thioacetamide were evaluated using frog embryo teratogenesis assay-Xenopus (FETAX). Early X. laevis embryos were exposed to ethanol and thioacetamide in two separate definitive concentration-response tests with and without differentially induced exogenous metabolic activation systems (MAS) or selectively inhibited MAS. Two concentration-response tests were also performed with ethanol metabolites, acetaldehyde and acetic acid. The MAS was treated with 3,4-amino-1,2,4-triazole to modulate CYP2E1 activity, and heat to inactivate flavin containing monooxygenases (FMO) activity. Results from these studies suggested that thioacetamide may be bioactivated by both CYP2E1 and the FMO systems. Ethanol also appeared to be bioactivated by CYP2E1. Acetaldehyde was markedly more potent as a developmental toxicant than ethanol or acetic acid. Binary joint mixture studies conducted with ethanol and acetaldehyde indicated that the parent compound and metabolite acetaldehyde acted in a response additive manner. These results warrant the continued use of FETAX as a means of evaluating mechanisms of developmental toxicity in vitro.

Acetaldehyde↗
PubMed1989

Covalent interactions of acetaldehyde with the actin/microfilament system.

The covalent binding of [14C]acetaldehyde to purified rabbit skeletal muscle actin was characterized. As we have found for other cytoskeletal proteins, actin formed stable covalent adducts under reductive and non-reductive conditions. Under non-reductive conditions, individual and competition binding studies versus albumin both showed that the G-form of actin is more reactive toward acetaldehyde than the F-form. When proteins were compared on an 'equi-lysine' basis under non-reducing conditions, G-actin was found to preferentially compete with albumin for binding to acetaldehyde. Time-course dialysis studies indicated that acetaldehyde-actin adducts become more stable with prolonged incubation at 37 degrees C. These data raise the possibility that actin could be a preferential target for adduct formation in cellular systems and will serve as the basis for ongoing studies aimed at defining the role of acetaldehyde-protein adducts in ethanol-induced cell injury.

Acetaldehyde↗
PubMed2005

The role of acetaldehyde in the central effects of ethanol.

This article represents the proceedings of a symposium at the 2004 annual meeting of the Research Society on Alcoholism in Vancouver, Canada. The symposium was organized by Etienne Quertemont and chaired by Kathleen A. Grant. The presentations were (1) Behavioral stimulant effects of intracranial injections of ethanol and acetaldehyde in rats, by Mercè Correa, Maria N. Arizzi and John D. Salamone; (2) Behavioral characterization of acetaldehyde in mice, by Etienne Quertemont and Sophie Tambour; (3) Role of brain catalase and central formed acetaldehyde in ethanol's behavioral effects, by Carlos M.G. Aragon; (4) Contrasting the reinforcing actions of acetaldehyde and ethanol within the ventral tegmental area (VTA) of alcohol-preferring (P) rats, by William J. McBride, Zachary A. Rodd, Avram Goldstein, Alejandro Zaffaroni and Ting-Kai Li; and (5) Acetaldehyde increases dopaminergic transmission in the limbic system, by Milena Pisano and Marco Diana.

Acetaldehyde↗
PubMed1980

The effects of acetaldehyde and disulfiram on albumin synthesis in the isolated perfused rabbit liver.

Acetaldehyde infusions inhibit albumin synthesis in the liver from fed donors but not in the livers from fasted donors. The inhibition of acetaldehyde metabolism with 4-MP and disulfiram reverses this finding, suggesting that acetaldehyde per se is not the toxic agent. Disulfiram stimulates albumin synthesis in livers from fasted donors, and the presence of acetaldehyde does not prevent this process. The effects of ethanol infusions cannot be explained as due to the presence of acetaldehyde; some intermediate metabolic step may be the basis of the inhibition of albumin production and polysome disaggregation in the presence of ethanol.

Acetaldehyde↗
PubMedDate not supplied

Liquid/air partition coefficients of acetaldehyde: values and limitations in estimating blood concentrations from analysis of breath.

We report liquid/air partition coefficients for dilute solutions of acetaldehyde in water, saline (0.9% wt/vol NaCl), human plasma, and corn oil. Equilibrium was studied at 34 degrees C and 37 degrees C with various concentrations of acetaldehyde in the liquid phases. At 37 degrees C, the liquid/air partition ratios for water, saline, plasma, and oil were 143 +/- 7.1, 132 +/- 6.6, 183 +/- 3.6, and 64 +/- 9.9 (mean +/- SE), respectively. At 34 degrees C, all the values were higher and the temperature coefficients of solubility were 3.7%, 3.3%, and 4.0% per 1 degree C for water, saline, and plasma solutions of acetaldehyde, respectively. The partition coefficients were independent of the concentration of acetaldehyde in the liquids, and the solubility was higher in water than in oil. The results are discussed with emphasis on the usefulness of expired breath as a biological specimen for the quantitative determination of acetaldehyde.

Acetaldehyde↗
PubMed1988

Mitochondria as the primary site of acetaldehyde metabolism in beef and pig liver slices.

Aldehyde dehydrogenase (ALDH) is the major enzyme involved in the oxidation of acetaldehyde. It has been shown that the liver enzyme is located in both cytosol and mitochondria. It has not been established where the subcellular oxidation of acetaldehyde occurs in species other than rat. Using slices isolated from beef and pig livers and selectively inhibiting the mitochondria enzyme with cyanamide or the cytosolic enzyme with disulfiram, it was possible to address this question. It was found that with both beef and pig liver slices 60% of the oxidation was catalyzed by the mitochondrial ALDH and 20% by the higher Km cytosolic enzyme. The remainder of the metabolism was the result of non-ALDH involvement. Furthermore, any decrease in the level of the low Km mitochondrial aldehyde dehydrogenase activity resulted in a decreased rate of acetaldehyde oxidation showing that its activity governed the rate of acetaldehyde oxidation. These were the same conclusions previously reached using rat liver tissue slices. Thus, it appears that for all mammalian tissue, mitochondria is the primary location of acetaldehyde oxidation.

Acetaldehyde↗
PubMed1988

Investigation of an acetaldehyde-hemoglobin adduct in alcoholics.

It has been proposed that an ethanol-related adduct is formed with hemoglobin in chronic alcoholics. This proposal is based on the observation that alcoholics were found to have an elevation of minor hemoglobins but normal amounts of glycosylated hemoglobin (HbA1c). Since acetaldehyde is believed to be the primary candidate involved in adduct formation, investigation was focused on this particular compound. This study describes the attempt to isolate and purify an acetaldehyde-hemoglobin adduct in alcoholics by cation-exchange chromatography and m-aminophenylboronic acid affinity chromatography for the purpose of characterization. Using acetaldehyde concentrations of 5 and 10 mM, an acetaldehyde adduct with hemoglobin was formed in vitro, isolated, and characterized. However, a similar adduct could not be isolated in vitro using a pharmacological concentration of 100 microM acetaldehyde nor could this adduct be isolated in human alcoholic subjects.

Acetaldehyde↗
PubMed1989

Methionine lowers circulating levels of acetaldehyde after ethanol ingestion.

Methionine, administered to ethanol treated mice and rats, significantly reduced circulating acetaldehyde levels without altering circulating levels of ethanol. Hepatic levels of acetaldehyde were also lowered by methionine. Methionine was effective when given prior to or after the administration of ethanol, but the time course of the action of methionine suggested the necessity for metabolic transformation of this amino acid in order for the acetaldehyde-lowering effect to be evidenced. Studies with humans, given methionine doses of approximately one-tenth of those used with mice, indicated that methionine can also lower acetaldehyde in humans ingesting ethanol. Given the toxic characteristics of acetaldehyde, methionine may prove effective in reducing the damaging effects of ethanol ingestion.

Acetaldehyde↗
PubMed1990

Cutaneous vasomotor sensitivity to ethanol and acetaldehyde: subtypes of alcohol-flushing response among Chinese.

A cutaneous test has been applied in examination of the flushing response to ethanol and acetaldehyde in 402 Chinese of Han ethnicity. Using this noninvasive method, five response subtypes have been observed: (A) fast flushing to both ethanol and acetaldehyde; (B) fast flushing only to ethanol but not to acetaldehyde; (C) slow flushing to ethanol only; (D) no response either to ethanol or to acetaldehyde; (E) vasoconstriction to ethanol, or to both ethanol and acetaldehyde. A total of 94% in subtype (A) are reported to be flushers, while only 25% was reported in subtype (D). Other physiological responses, such as tachycardia, dizziness, headache, drowsiness, and nausea are less frequent after alcohol ingestion. The recent history of consumption of alcohol of the subjects in different subtypes was also obtained. Although alcohol-induced flushing is thought to be a deterrent factor to heavy consumption of alcohol, the frequency of drinking of alcoholic beverages was not found to be different between flushers and nonflushers.

Acetaldehyde↗
PubMed1993

Production of antibodies that recognize the heterogeneity of immunoreactive sites in human hemoglobin chemically modified by acetaldehyde.

Human hemoglobin (Hgb) was incubated with acetaldehyde under two different conditions: (a) in the presence of 250 mM acetaldehyde for 1 hr then reduced with 100 mM NaCNBH3 for an additional 4 hr at room temperature; and (b) in the presence of 500 mM acetaldehyde for 10 days at room temperature and then reduced with 1 mM NaBH4 for 1 hr. It was found that 44% and 27% of free amino groups in Hgb-acetaldehyde adduct (AA) remained unmodified when Hgb was treated under conditions (a) and (b), respectively. SDS-PAGE analysis revealed that the molecular weight of Hgb-AA(a) [Hgb modified under condition (a)] was slightly greater than that of unmodified Hgb and extensive protein cross-linking had occurred in Hgb-AA(b) [Hgb modified under condition (b)]. Electrophoresis on agarose gel showed the order of negative charge was Hgb-AA(b) > Hgb-AA(a) > unmodified Hgb. Polyclonal antibody raised in rabbits using keyhole limpet hemocyanin as the carrier protein modified by acetaldehyde under condition (a) [i.e., KLH-AA(a)] preferentially recognized Hgb-AA(a), whereas antibody raised using KLH-AA(b) as the immunogen recognized only Hgb-AA(b). In conclusion, antibodies raised with protein-AA antigens produced under different conditions recognize different epitopes.

Acetaldehyde↗
PubMed1993

Effect of alcohol, acetaldehyde, and salsolinol on beta-endorphin secretion from the hypothalamic neurons in primary cultures.

The effect of ethanol, acetaldehyde, and salsolinol on hypothalamic beta-endorphin secreting neurons is studied by using rat fetal hypothalamic neurons in primary culture. Exposure of these neuronal cells to different concentrations of ethanol (12.5-50 mM) and acetaldehyde (12.5-50 microM) caused a concentration-dependent increase in the secretion of beta-endorphin. Salsolinol (12.5-50 microM) did not cause any significant change in the secretion of beta-endorphin. Ethanol's effect was short-lasting (2 hr). Acetaldehyde's effect on beta-endorphin secretion was greater and longer lasting, as compared with ethanol. Ethanol and salsolinol do not have any effect on cell viability, whereas higher concentrations of acetaldehyde appear to reduce the number of viable cells after 6 hr of treatment. None of the above treatments has any effect on cellular DNA content. These results suggest that ethanol is a potent stimulator of hypothalamic beta-endorphin. These results also show for the first time that ethanol's metabolite acetaldehyde is more potent in stimulating beta-endorphin secretion and may be significant in the ethanol regulated beta-endorphin secretion.

Acetaldehyde↗
PubMed1994

Acetaldehyde exposure causes growth inhibition in a Chinese hamster ovary cell line that expresses alcohol dehydrogenase.

Chronic ethanol exposure causes many pathophysiological changes in cellular function due to ethanol itself and/or the effects of its metabolism (i.e., generation of acetaldehyde and redox equivalents). However, the role of each of these effects remains controversial. To address these questions, we have developed a cell line that expresses alcohol dehydrogenase. This cell line permits separate examination of the effects of ethanol and its metabolite acetaldehyde on cell function. An expression vector for the mouse liver alcohol dehydrogenase was constructed and transfected into Chinese hamster ovary cells. Cells expressing alcohol dehydrogenase were identified by screening with allyl alcohol, which is metabolized by alcohol dehydrogenase to the toxic aldehyde acrolein. A number of cell lines were identified that expressed alcohol dehydrogenase. A-10 cells were selected for further study because of their high sensitivity to allyl alcohol, suggesting a high level of alcohol dehydrogenase expression. These cells expressed a mRNA that hybridizes with the alcohol dehydrogenase cDNA and had an alcohol dehydrogenase activity comparable to murine liver. When cultures of these cells were exposed to ethanol, acetaldehyde was detected in both the medium and cells. The acetaldehyde concentration in the medium remained constant for at least 1 week in culture and was a function of the added ethanol concentration. Chronic exposure of A-10 cells to ethanol resulted in a dose-dependent reduction in the number of cells that accumulated over 7 days. Ethanol-treated cells remained viable, and growth inhibition was reversible. Growth inhibition was blocked by the alcohol dehydrogenase inhibitor 4-methylpyrazole, suggesting that acetaldehyde and not ethanol was responsible for growth inhibition in these cells.

Acetaldehyde↗
PubMed1995

Effect of ethanol, propanol, butanol, and catalase enzyme blockers on beta-endorphin secretion from primary cultures of hypothalamic neurons: evidence for a mediatory role of acetaldehyde in ethanol stimulation of beta-endorphin release.

Previously, we have shown that low doses of ethanol (12.5-100 mM) and acetaldehyde (12.5-50 microM), but not salsolinol, enhanced immunoreactive beta-endorphin (IR-beta-EP) secretion from fetal hypothalamic neurons in primary culture. In this study, the effects of ethanol, propanol, and butanol, as well as the effect of catalase inhibitors on IR-beta-EP secretion were studied in vitro to determine the role of membrane fluidization and ethanol metabolism on ethanol-induced IR-beta-EP secretion. The primary cultures of fetal hypothalamic neurons were maintained for 8-9 days in chemically defined medium and treated for 5 hr with ethanol (50 mM), propanol (25 and 50 mM), and butanol (25 and 50 mM). Determination of hourly secretion of IR-beta-EP from the cultures revealed that only 50 mM ethanol caused stimulation of IR-beta-EP secretion, whereas propanol and butanol did not alter IR-beta-EP response at any given concentration. Pretreatment of these cultures with the catalase inhibitors, 3-amino-1,2,4-triazole (3-AT; 1, 5, and 10 mM), caused a dose-dependent inhibition of ethanol-stimulated IR-beta-EP secretion, but did not inhibit dibutyryl cAMP (dcAMP)-stimulated IR-beta-EP secretion. Another catalase inhibitor, sodium azide (5 mM), also inhibited ethanol-stimulated IR-beta-EP secretion. Measurement of acetaldehyde production in cultured cells and media after ethanol or dcAMP treatments revealed that cultured cells produce acetaldehyde only after ethanol treatment and at levels of acetaldehyde (8-24 microM) that are known to evoke IR-beta-EP release. The catalase inhibitor 3-AT (10 mM) treatment reduced ethanol-evoked acetaldehyde production.(ABSTRACT TRUNCATED AT 250 WORDS)

1-Butanol↗
PubMed1996

Inhibitory mechanism of intestinal ethanol absorption induced by high acetaldehyde concentrations: effect of intestinal blood flow and substance specificity.

This study describes the effects of high blood acetaldehyde concentrations on the intestinal absorption of ethanol and 2-butanone using an in situ single-pass perfusion technique on the rat intestine and the colored microsphere method to measure intestinal blood flow. We found that high blood acetaldehyde concentrations inhibit intestinal ethanol absorption in an inverse proportion to peak acetaldehyde concentrations, decrease intestinal blood flow, and inhibit intestinal absorption of 2-butanone. The decrease of the intestinal blood flow, induced by high blood acetaldehyde concentrations, is a major mechanism inhibiting intestinal ethanol absorption, but other mechanisms are also thought to inhibit absorption. Therefore, inhibition by high acetaldehyde concentrations is not the only factor affecting ethanol absorption.

Acetaldehyde↗
PubMed1996

Estrogen-related acetaldehyde elevation in women during alcohol intoxication.

Alcohol is more often unpleasant and causes tissue damage more rapidly in women than men. The present study was designed to find out whether acetaldehyde, the primary metabolite of alcohol, could play a crucial role in these actions. Special emphasis was focused on the appropriate determination of blood acetaldehyde and hormonal factors. Occurrence of elevated blood acetaldehyde levels during alcohol oxidation was established in both normally cycling women and ones taking oral contraceptives, but not in men. An association between elevated acetaldehyde levels and high estrogen phases was observed in both groups of women. Estrogen-related acetaldehyde elevation is suggested to be the key factor explaining the gender differences of the adverse effects of alcohol.

Acetaldehyde↗
PubMed1994

Acetaldehyde production in Saccharomyces cerevisiae wine yeasts.

Eighty-six strains of Saccharomyces cerevisiae were investigated for their ability to produce acetaldehyde in synthetic medium and in grape must. Acetaldehyde production did not differ significantly between the two media, ranging from a few mg/l to about 60 mg/l, and was found to be a strain characteristic. The fermentation temperature of 30 degrees C considerably increased the acetaldehyde produced. This study allowed us to assign the strains to different phenotypes: low, medium and high acetaldehyde producers. The low and high phenotypes differed considerably also in the production of acetic acid, acetoin and higher alcohols and can be useful for studying acetaldehyde production in S. cerevisiae, both from the technological and genetic point of view.

Acetaldehyde↗