Biomedical subjects

L Lumeng

Publications and source records attributed to L Lumeng.

At least 145 records · Page 8Linked to original sources

PubMed1990

Flexible sigmoidoscopy plus air contrast barium enema versus colonoscopy for suspected lower gastrointestinal bleeding.

A randomized, controlled trial was performed to compare the diagnostic yields and cost-effectiveness of two strategies for the evaluation of nonemergent lower gastrointestinal bleeding. Three hundred eighty patients aged greater than or equal to 40 yr were randomized to undergo initial flexible sigmoidoscopy plus air contrast barium enema or colonoscopy; 332 completed the initial studies. Initial colonoscopy detected more cases of polyps less than 9 mm in size, adenomas, and arteriovenous malformations but fewer cases of diverticulosis. No significant difference was found between strategies in the number of patients detected with cancers or polyps greater than or equal to 9 mm in size. In both strategies, cancers were more common in subjects aged greater than or equal to 55 yr (8% overall) than in those aged less than 55 yr (1%). Among patients aged less than 55 yr with suspected lower gastrointestinal bleeding, initial flexible sigmoidoscopy plus air contrast barium enema is a more cost-effective strategy for the detection of colonic neoplasms than initial colonoscopy. However, initial colonoscopy is more cost effective for those aged greater than or equal to 55 yr.

Barium Sulfate↗

PubMed1990

Higher density of serotonin-1A receptors in the hippocampus and cerebral cortex of alcohol-preferring P rats.

Saturable [3H]-8OHDPAT binding to 5HT-1A receptors in membranes prepared from hippocampus and frontal cerebral cortex of alcohol-preferring P rats and of alcohol-nonpreferring NP rats has been compared. The Bmax values or densities of recognition sites for 5HT-1A receptors in both brain areas of the P rats are 39 and 131 percent, respectively, higher than those in the NP rats. The corresponding KD values are 38 and 44 percent lower in the P rats than in the NP rats, indicating higher affinities of the recognition sites for the 5HT-1A receptors in hippocampus and cerebral cortex of the P rats. These findings indicate either an enrichment of 5HT-1A receptor density during selective breeding for alcohol preference or an upregulation of 5HT-1A receptors developed as an adaptation to lower presynaptic concentrations of 5HT found in these brain areas of P rats as compared with the NP rats.

8-Hydroxy-2-(di-n-propylamino)tetralin↗

PubMed1990

Naloxone attenuates voluntary ethanol intake in rats selectively bred for high ethanol preference.

The effect of naloxone on voluntary ethanol intake was examined in rats which were selectively bred for oral ethanol preference (High Alcohol Drinking or HAD line). Rats of the HAD line were treated with naloxone in doses of 0.05-18.0 mg/kg b.wt. before access to water alone or to a free-choice between a 10% (v/v) ethanol solution and water. Naloxone suppressed water intake when water was presented as the sole source of fluid. In contrast, naloxone produced a dose-dependent decrease in ethanol consumption, without altering water intake, when rats were given a free-choice between the ethanol solution and water. Selective suppression of ethanol consumption by naloxone was not attributable to changes in blood ethanol concentrations or ethanol elimination rates following naloxone treatment. It appears that although naloxone may attenuate the positively reinforcing properties of both ethanol and water, ethanol drinking is a subset of consummatory behaviors that is particularly sensitive to opioid receptor blockade. The results suggest that activation of the endogenous opioid system may be an important mechanism which serves to maintain continued ethanol drinking.

Alcohol Drinking↗

PubMed1990

Protein-acetaldehyde adducts in serum of alcoholic patients.

Enzyme-linked immunosorbent assay (ELISA) was used to detect the presence of protein-acetaldehyde adducts (-AAs) in human serum samples. Two methods were compared: (1) direct ELISA: samples, rabbit anti-hemocyanin-AA IgG, and beta-galactosidase (beta-gal) conjugated goat anti-rabbit serum IgG added to a 96-well ELISA plate in a stepwise manner; and (2) two-site or sandwich ELISA: serum samples added to an ELISA plate that had been precoated with anti-hemocyanin-AA IgG (the capture antibody) and incubated stepwise with biotinated anti-hemocyanin-AA IgG (the signal antibody) and avidin-beta-gal conjugates. Serum protein-AA levels were then assayed by bound beta-gal activities at OD405. When human hemoglobin (Hgb)-AA was used as a model protein-AA for the sandwich ELISA, the EC50 (estimated concentration that corresponds to 50% of the OD405 response range) was 7 ng/ml. Direct ELISA was less sensitive (EC50 of 120 ng/ml). Adding control human serum to Hgb-AA increased the EC50 of the direct ELISA more than the sandwich ELISA. Intra- and interassay coefficients of variance for sandwich ELISA were both about 8%. Detection of Hgb-AA by sandwich ELISA was highly specific. The above results with anti-hemocyanin-AA IgG were also obtained when anti-myoglobin-AA IgG was used in sandwich ELISA. Using sandwich ELISA and anti-hemocyanin-AA IgG, OD405 for sera of control subjects and alcoholic patients were 0.036 +/- 0.033 (+/- SEM, n = 28) and 0.150 +/- 0.088 (n = 28), respectively. Serum protein-AAs reacted more strongly with anti-myoglobin-AA IgG than anti-hemocyanin-AA IgG.(ABSTRACT TRUNCATED AT 250 WORDS)

Acetaldehyde↗

PubMed1990

Increased number of GABAergic terminals in the nucleus accumbens is associated with alcohol preference in rats.

Ethanol is known to be anxiolytic and this effect may be mediated through GABA transmission acting on the GABAA-benzodiazepine-Cl- ionophore complex. Recent studies from our laboratory have suggested that GABA transmission and the GABAA-benzodiazepine-Cl- ionophore complex might be involved in the rewarding action of ethanol in alcohol-preferring rats. We report here immunocytochemical and morphometric studies analyzing the GABAergic terminal density in the nucleus accumbens (NA), corpus striatum, nucleus tractus solitarius, and lateral septum of the selectively bred P (alcohol-preferring) and the NP (alcohol-nonpreferring) lines of rats, as well as of the high-alcohol-drinking (HAD) and low-alcohol-drinking (LAD) lines of rats. The NA was included for analysis because this structure has been implicated as an important component of the brain reward system. An increase of GABAergic terminal density was found in the NA of the P rats, when compared with the NP rats. Similarly, there were more GABAergic terminals in the NA of HAD rats than of the LAD rats. No differences between the lines were seen in the other brain regions examined. The results suggest that alcohol preference in P and HAD rats may be related to increased GABA terminals and enhanced GABAergic inhibition within the NA.

Alcohol Drinking↗

PubMed1990

Formation of the 37KD protein-acetaldehyde adduct in liver during alcohol treatment is dependent on alcohol dehydrogenase activity.

Protein-acetaldehyde adducts (protein-AAs) are formed in vivo during chronic alcohol ingestion. These protein-AAs reported thus far include a 37KD protein-AA in liver cytosol, cytP450IIE 1-AA in hepatic microsomes, hemoglobin-AA, and serum protein-AAs. It has been postulated that acetaldehyde or perhaps a reactive acetaldehyde radical generated by the microsomal ethanol oxidizing system (MEOS or cytP450IIE1) explains the formation of the cytP450IIE1-AA. The source of acetaldehyde responsible for the formation of the cytosolic 37KD protein-AA has not been determined. In this report, we have examined the effects of pyrazole (an ADH inhibitor) and cyanamide (an aldehyde dehydrogenase inhibitor) on the formation of the 37KD liver protein-AA in vivo and in vitro. It was found that feeding rats with an alcohol-containing liquid diet supplemented with cyanamide enhanced while a diet supplemented with pyrazole completely abolished the formation of the 37KD liver protein-AA. The liver of rats fed the pyrazole supplemented alcohol-containing diet showed significantly higher content of cytP450IIE1 than that of rats fed the diet containing alcohol alone. On the other hand, feeding the cyanamide supplemented alcohol-containing liquid diet did not further enhance the content of cytP450IIE1. Similarly, adding cyanamide to the culture medium enhanced while adding 4-methylpyrazole inhibited the production of the 37KD protein-AA by cultured hepatocytes even though the combination of alcohol and 4-methylpyrazole increased the content of cytP450IIE1 2-fold over that in control cells. These results demonstrate that the formation of the 37KD liver Protein-AA is dependent on ADH and not on MEOS.(ABSTRACT TRUNCATED AT 250 WORDS)

Acetaldehyde↗

PubMed1989

Serum high-density lipoprotein particles of alcohol-fed rats are deficient in apolipoprotein E.

Effects of chronic ethanol consumption on serum lipoproteins have been studied in the rat. The serum levels of triglycerides, cholesterol, phospholipids and apolipoproteins AI and AIV increased significantly after 1 week of ethanol feeding, and they remained elevated up to 7 weeks of alcohol drinking. By contrast, serum total apolipoprotein E decreased or, sometimes, did not change. Very-low-density lipoprotein cholesterol, triglycerides and very-low-density lipoprotein apolipoprotein E of the alcohol-fed rats increased in parallel and were about 2- to 2.5-fold over the controls. Whereas high-density lipoprotein cholesterol, phospholipids, apolipoprotein AI and AIV increased 1.2-fold by chronic alcohol feeding, the level of high-density lipoprotein apolipoprotein E decreased to 70% of that of the control rats. The rates of secretion of apolipoprotein AI, E and AIV into the culture medium by hepatocytes isolated from ethanol-fed rats were 1.8-, 1.3- and 1.1-fold higher than those from control rats. These data indicate that (i) chronic ethanol feeding increases very-low-density lipoprotein and high-density lipoprotein in the rat; (ii) serum high-density lipoprotein particles of the ethanol-fed rats are deficient in apolipoprotein E, and (iii) chronic ethanol feeding increases hepatic secretion of apolipoprotein AI, E and AIV. Since the steady-state serum level of apolipoprotein E decreases or remains unchanged in the presence of increased hepatic apolipoprotein E secretion, this imbalance suggests that alcohol feeding either accelerates the rate of degradation of serum apolipoprotein E or suppresses apolipoprotein E synthesis by nonhepatic tissues.

Albumins↗

PubMed1989

Further studies on the 37 kD liver protein-acetaldehyde adduct that forms in vivo during chronic alcohol ingestion.

We have previously reported the detection of a 37 kD liver protein-acetaldehyde adduct in rats fed alcohol chronically with the AIN'76 diet. It was surprising that only one liver protein-acetaldehyde adduct was found. In this report, we have tried to detect additional protein-acetaldehyde adducts by electroimmunotransblot with rabbit anti-hemocyanin-acetaldehyde adduct IgG and to further characterize the 37 kD liver protein-acetaldehyde adduct. Sensitivity of electroimmunotransblot increased 10- to 20-fold when alkaline phosphatase-linked antibody was used in place of horseradish peroxidase, but only one protein-acetaldehyde adduct band was detected in liver. Feeding rats the Lieber-DeCarli alcohol diet also did not produce more protein-acetaldehyde adduct bands in electroimmunotransblot. Addition of cyanamide, an aldehyde dehydrogenase inhibitor, to the AIN'76 alcohol diet greatly increased the intensity of the 37-kD protein-acetaldehyde adduct band on electroimmunotransblot but did not produce other bands. The 37 kD protein-acetaldehyde adduct decayed in vivo with a half-life of 4 days when alcohol was removed from the diet. The 37 kD protein-acetaldehyde adduct in liver is cytosolic. Its interaction with anti-hemocyanin-acetaldehyde adduct IgG was blocked by polylysine-acetaldehyde adduct and polytyrosine-acetaldehyde adduct. It could be removed by immunosorption with anti-hemocyanin-acetaldehyde adduct IgG-bound immunoresin. When immunoblotted with anti-alcohol dehydrogenase and anti-aldehyde dehydrogenase antibodies, the alcohol dehydrogenase and aldehyde dehydrogenase bands in liver of alcohol-fed rats showed identical intensities before and after immunosorption.(ABSTRACT TRUNCATED AT 250 WORDS)

Acetaldehyde↗

PubMed1989

Serotonin and ethanol preference.

This chapter brings together evidence indicating the involvement of serotonin (5-HT) in ethanol preference using data mainly obtained from selectively bred alcohol-preferring and alcohol-nonpreferring lines of rodents. Although several laboratories have established rodent lines that will consume large quantities of ethanol daily, only one line thus far has been established that satisfied all the criteria for an animal model of alcoholism and that would be suitable for studying the biological basis of ethanol preference. This is the P line of alcohol-preferring rats that: (1) freely consumes 5-9 g ethanol/kg body wt/day; (2) drinks sufficient alcohol to produce intoxicating blood alcohol concentrations; (3) works to obtain alcohol; (4) self-administers ethanol for its CNS pharmacological effects; and (5) develops chronic tolerance to and dependence on alcohol with free-choice drinking. Relative to the NP line of alcohol-nonpreferring rats, the P rat has lower 5-HT levels in several CNS regions, including some, such as the nucleus accumbens, hypothalamus, and frontal cortex, which are involved in the brain reward circuitry. Furthermore, both acute and chronic ethanol administration have effects on the 5-HT pathway from the dorsal raphe nucleus to the nucleus accumbens in the P rat. Pharmacological studies have demonstrated that fluoxetine, a serotonin uptake inhibitor, reduced the oral consumption or intragastric self-administration of alcohol in the P rats. In addition, administration of a 5-HT1B agonist also attenuated the oral intake of ethanol by P rats. It is hypothesized that the serotonergic pathway from the dorsal raphe nucleus to the nucleus accumbens is involved in the reinforcing actions of alcohol in the P line of rats.

Alcohol Drinking↗

PubMed1989

Spiroxatrine augments fluoxetine-induced reduction of ethanol intake by the P line of rats.

The present study was undertaken to determine if spiroxatrine, a reported 5-HT1A antagonist, could block the attenuating effects of fluoxetine (a 5-HT uptake inhibitor) on voluntary ethanol intake by the selectively bred alcohol-preferring P line of rats. Fluoxetine (10 mg/kg, IP) significantly reduced the intake of 10% ethanol by P rats approximately 50% during the 4-hour period of alcohol availability. Spiroxatrine (4 mg/kg, IP) was without effect on ethanol intake when given alone. However, when given 5 minutes before fluoxetine (10 mg/kg, IP), this dose of spiroxatrine augmented the reduction of ethanol intake to approximately 15% of control values after 4 hours. Similar experiments conducted with 1 mg/kg (IP) 8-hydroxy-2(di-N-propylamino) tetralin (DPAT) demonstrated that this 5-HT1A agonist also enhanced the attenuating effects of fluoxetine on ethanol intake. Likewise, spiroxatrine augmented the DPAT reduction of alcohol intake. Spiroxatrine enhanced the effect of DPAT and fluoxetine on food intake as it did on ethanol intake. The results suggest that spiroxatrine behaved as a partial agonist and/or modulator and not as an antagonist at 5-HT1A receptors under the present experimental conditions.

8-Hydroxy-2-(di-n-propylamino)tetralin↗

PubMed1989

Ethanol reinforcement in the alcohol nonpreferring rat: initiation using behavioral techniques without food restriction.

Genetic selection of rats can markedly alter their ethanol consumption. The manner in which environmental factors interact in these genetically selected animals to influence ethanol consumption has not been thoroughly investigated. Using the alcohol-nonpreferring (NP) line of rats selectively bred at the Indiana University School of Medicine, alcohol self-administration in an operant situation was initiated using either a sucrose-fading or a secondary-conditioning procedure. These initiation procedures do not require any food or fluid restriction. Initiation was successful in 10 out of 12 NP animals, with the initiated rats self-administering ethanol at concentrations as high as 40%. Following initiation, a retest of home-cage ethanol preference found increases in ethanol acceptability. When tested in a concurrent operant situation, the initiated NP rats also chose ethanol over water. However, the NP rats had lower alcohol intakes and a different pattern of drinking over time when compared to that of nonselected Long-Evans rats. While the NP rats could be initiated to lever-press for ethanol, at no time did their intake approach that of the selected line of alcohol-preferring (P) rats. Thus, while an upward shift from the genetic baseline in ethanol preference and intake can result from the environmental initiation manipulations employed in these studies, genetic factors would appear to limit the extent to which ethanol ingestion can be increased.

Alcohol Drinking↗

PubMed1988

Serotonergic and adrenergic receptors in alcohol-preferring and non-preferring rats.

Serotonergic and adrenergic receptors in brain areas of the alcohol-preferring P and alcohol-nonpreferring NP rats were compared by radioligand-binding assays. Binding of 3H-serotonin (3H-5HT) to 5HT-1 receptors in membranes of cerebral cortex and hippocampus was significantly higher in density (B max values) and affinity (Kd values) in the P than in the NP rats, whereas B max values in membranes from the brain stem of the P rats were lower than those of the NP rats. No significant difference between the P and NP lines was observed when the binding of 3H-ketanserin to 5HT-2 receptors and of 3H-WB4101, 3H-clonidine and 3H-dihydoalprenolol to alpha-1, alpha-2 and beta-adrenergic receptors was compared. The increase of 3H-5HT binding probably indicates up-regulation or supersensitivity of 5HT-1 receptors as a compensatory mechanism to the lower levels of 5HT in brain areas of the P rats (Murphy, et al., 1982).

Alcoholism↗

PubMed1988

Effects of Ro 15-4513, fluoxetine and desipramine on the intake of ethanol, water and food by the alcohol-preferring (P) and -nonpreferring (NP) lines of rats.

The effects of the IP administration of RO 15-4513 (1, 2 and 4 mg/kg), fluoxetine (5 and 10 mg/kg) and desipramine (5 and 10 mg/kg) on the intake of 10% ethanol, H2O and food were determined in the selectively bred alcohol-preferring (P) and -nonpreferring (NP) lines of rats with daily access to fluids being limited to single 2-hour sessions. The imidazobenzodiazepine Ro 15-4513 (a partial inverse benzodiazepine agonist) significantly reduced the intake of 10% ethanol by the P rats to 50-60% of control levels in the first 30 minutes without altering food or H2O intake. The attenuating actions of 2 mg/kg Ro 15-4513 on ethanol intake could be completely blocked by the central benzodiazepine receptor antagonist Ro 15-1788 (10 mg/kg). Ro 15-1788, by itself, produced no effects on alcohol and H2O consumption. The 5 mg/kg dose of fluoxetine significantly reduced 10% ethanol intake by the P rats to 20% of control values without altering either H2O or food consumption. The 10 mg/kg dose of fluoxetine further reduced ethanol intake by the P rats, but this dose also reduced daily food intake to approximately 70% of normal. Desipramine at both doses significantly (p less than 0.05) reduced both ethanol and food uptake by the P rats and had a tendency to reduce H2O consumption as well. In general, the three drugs had effects in the NP rats similar to those observed for the P group, although the effects on 10% ethanol intake were difficult to compare because of the low, variable intake of alcohol by the NP group.(ABSTRACT TRUNCATED AT 250 WORDS)

Alcohol Drinking↗

PubMed1988

Effects of acute ethanol administration on monoamine and metabolite content in forebrain regions of ethanol-tolerant and -nontolerant alcohol-preferring (P) rats.

The contents of dopamine (DA), serotonin (5-HT) and their metabolites in the frontal cortex, anterior striatum, nucleus accumbens and hypothalamus of alcohol-tolerant and -nontolerant rats of the alcohol-preferring P line were determined one hour after the IP administration of 2.5 g ethanol/kg body wt. Compared with saline-injected controls, nontolerant P-rats injected with ethanol had (a) 60% higher levels of 3,4-dihydroxyphenylacetic acid (DOPAC) and homovanillic acid (HVA) in the frontal cortex; (b) 30-60% higher levels of DOPAC and HVA in the anterior striatum and nucleus accumbens; and (c) 20% higher levels of 5-HIAA in all three forebrain regions. In the tolerant group, the effects of IP ethanol on DOPAC and HVA were markedly attenuated or completely eliminated in these three forebrain regions. However, in the case of 5-HIAA, an attenuated response was observed only in the nucleus accumbens of the tolerant group. The IP administration of ethanol had little effect on the contents of DA or 5-HT in any of these three forebrain regions, with the exception that 5-HT levels were elevated in the anterior striatum of both the tolerant and nontolerant groups. In the hypothalamus, there were no significant differences for the contents of DA, 5-HT or their metabolites between the nontolerant or tolerant P rats after IP ethanol. The data indicate that both acute ethanol administration and chronic alcohol intake by the P line of rats alters certain DA and 5-HT systems that may be involved in the brain reward circuitry and in DA pathways involved in motor functions.

3,4-Dihydroxyphenylacetic Acid↗

PubMed1988

Differences in response to the aversive properties of ethanol in rats selectively bred for oral ethanol preference.

A conditioned taste aversion (CTA) paradigm was used to determine whether aversion to the pharmacological effects of ethanol, apart from orosensory cues, can contribute to genetic differences in voluntary ethanol consumption. Four doses of ethanol, administered IP, were paired with the consumption of a 0.1% saccharin solution in rats from the alcohol-preferring (P) and alcohol-nonpreferring (NP) lines. Repeated pairing of saccharin and ethanol in a dose of 1.0 g/kg produced stronger and more prolonged aversion to saccharin in NP rats, compared with P rats, at comparable blood ethanol levels. A low dose of ethanol (0.25 g/kg) produced transient conditioned facilitation of saccharin consumption in P rats, but not in NP rats, at comparable blood ethanol levels. The results suggest that rats of the NP line find the postingestional effects of high-dose ethanol more aversive, and low-dose ethanol less reinforcing, than do rats of the P line. Genetic differences in voluntary ethanol consumption may be due, in part, to differences in aversion to the postingestional effects of ethanol.

Alcohol Drinking↗

PubMed1988

Genetic polymorphism of enzymes of alcohol metabolism and susceptibility to alcoholic liver disease.

Differences in the pharmacokinetics of alcohol absorption and elimination are, in part, genetically determined. There are polymorphic variants of the two main enzymes responsible for ethanol oxidation in liver, alcohol dehydrogenase and aldehyde dehydrogenase. The frequency of occurrence of these variants, which have been shown to display strikingly different catalytic properties, differs among different racial populations. Since the activity of alcohol dehydrogenase in liver is a rate-limiting factor for ethanol metabolism in experimental animals, it is likely that the type and content of the polymorphic isoenzyme subunit encoded at ADH2, beta-subunit, and at ADH3, the gamma-subunit, are contributing factors to the genetic variability in ethanol elimination rate. The recent development of methods for genotyping individuals at these loci using white cell DNA will allow us to test this hypothesis as well as any relationship between ADH genotype and the susceptibility to alcoholism or alcohol-related pathology. A polymorphic variant of human liver mitochondrial aldehyde dehydrogenase, ADLH2, which has little or no acetaldehyde oxidizing activity has been identified. Individuals with the deficient ALDH2 phenotype do not have altered ethanol elimination rates but they do exhibit high blood acetaldehyde levels and dysphoric symptoms such as facial flushing, nausea and tachycardia, after drinking alcohol. Because acetaldehyde is so reactive, it binds to free amino groups of proteins including a 37 kilodalton hepatic protein-acetaldehyde adduct and may elicit an antibody response. We would predict that individuals who have low ALDH2 activity because of liver disease or because they have the inactive ALDH2 variant isoenzyme might form more protein-acetaldehyde adducts and elicit a greater immune response. These adducts may represent good biological markers of alcohol abuse and may also play a role in liver injury due to chronic alcohol consumption.

Alcohol Dehydrogenase↗

PubMed1988

Effect of low dose ethanol on the EEG of alcohol-preferring and -nonpreferring rats.

Low dose ethanol has been shown to differentially affect the behavior of alcohol-preferring (P) and -nonpreferring (NP) rats. The present study was undertaken to determine if this differential effect is reflected in the EEG of these two rat lines. Frontocortical and hippocampal EEG were recorded from P and NP rats after intragastric infusions of ethanol (0.5 g/kg) and vehicle. Spectra were created from sequential 8-second epochs and power was calculated for frequency bands 0-4, 4-8, 8-16 and 16-50 Hz. Band power data was then grouped according to the rat's behavior and compared for P and NP rats. During nonREM sleep, ethanol produced a persistent increase in power in the NP rats, while power in the P rats was initially decreased, then returned to baseline. This differential effect was seen at both recording sites. The results suggest the P rats were midly aroused by low dose ethanol, while the NP rats were mildly sedated.

Alcohol Drinking↗

PubMed1988

Detection of a protein-acetaldehyde adduct in the liver of rats fed alcohol chronically.

We report here the formation in vivo of a protein-acetaldehyde adduct (protein-AA) in liver when rats were fed alcohol chronically. This chemically modified protein was demonstrated by electroimmunotransblot technique and with rabbit polyclonal antibodies that recognize acetaldehyde adduct as an epitope (i.e., both anti-hemocyanin-AA IgG and anti-myoglobin-AA IgG). It has a molecular weight of 37,000. It can be detected in the liver of rats fed the alcohol-containing American Institute of Nutrition 1976 liquid diet for only 1 wk. Since the protein profiles of soluble hepatic proteins from alcohol-fed and control rats were identical on SDS-PAGE, the peroxidase-positive band demonstrated by electroimmunotransblot was most likely not a new protein synthesized de novo. Borohydride reduction was not necessary to stabilize this protein-AA. Intraperitoneal injections of ethanol (2 g/kg body wt) at 8-h intervals to rats over a 24-h period did not produce any detectable protein-AA in the liver. Incubation of the liver homogenate from a control liver with acetaldehyde without sodium cyanoborohydride for 4 h also failed to generate any protein-AA. Therefore, the formation of the 37-kD protein-AA in vivo reported here is dependent on chronic alcohol consumption.

Acetaldehyde↗