Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0038187 (starvation)
 24,951 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Ethanol elimination rates were determined in rats using an intravenous route of ethanol administration after several experimental manipulations. Twenty-four hr food deprivation resulted in a 30% reduction to 35 mg/100ml blood/hr in elimination rate from a non-deprived rate of 50 mg/100 ml blood/hr. After 2 months of ethanol drinking (5% v/v), 24 hr starvation resulted in only a 10% reduction in elimination rate (45 mg/100 ml blood/hr), and did not increase the non-food-deprived rate (49.2 mg/100 ml blood/hr) over that obtained in the above animals' drinking water rather than 5% ethanol. Animals which chronically overdrank ethanol or water for 3 months on a schedule-induced polydipsia procedure, known to result in ethanol physical dependence, showed a decreased rate of ethanol elimination (37.9 mg/100 ml blood/hr for water drinkers) in the non-food-deprived condition. By providing 750 mg of liver powder daily as a food supplement in the ethanol overdrinking regimen, the ethanol elimination rate remained at a rate comparable to the normal animal (48.4 mg/100 ml blood/hr).
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PMID:Ethanol elimination rates in normal and ethanol dependent animals. 103 70

Cardiac: Cardiac protein synthesis is influenced by the state of nutrition with reduction of cardiac size in starvation. Ethanol per se may not affect this synthesis directly, but the metabolite of ethanol, acetaldehyde, profoundly decreases normal protein synthesis in the heart in vitro. The interference with the synthetic process may play a role in the ultimate cardiomyopathies of malnutrition and alcoholism. Hepatic: In vivo albumin synthesis is sensitive to environment, oncotic pressure, normal balance, nutrition, as well as toxins and state of health. Thus, to study the acute effects of alcohol alone, it was necessary to employ the isolated perfused liver. Fasting reduced albumin synthesis 50%, with loss of RNA and a disaggregation of the endoplasmic membrane bound polysome. Tryptophan, arginine and ornithine added to the perfusate at a final concentration of 10 mM reversed these findings. Alcohol likewise reduced albumin synthesis; disaggregates the bound polysome without a marked loss of RNA. Ornithine, arginine and tryptophan are able to reverse this loss in albumin synthesizing capacity. The combination of fasting and alcohol, while not lowering albumin synthesis below that seen with either stress alone, prevents the recovery from either stress.
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PMID:Effects of ethanol on protein synthesis. 109 51

Simultaneous treatment of rats with ethanol (EtOH) and methylmercury (MeHg) increases the frequency of lesions in the rat kidney. Therefore, it was of interest to us to study the effects of simultaneous treatment of rats with MeHg and EtOH on kidney metallothionein (MT) and mercury residues levels in kidneys of rats maintained on 70% of ad libitum diet. Treatment with MeHg alone induced kidney MT the most (twice) compared to its pair-fed control. Simultaneous treatment with MeHg and EtOH also induced kidney MT but to a lesser degree than treatment with MeHg alone (by about 30%). Ethanol by itself caused a slight increase in kidney MT although starvation resulting from pair-feeding with mercury-treated animals may have contributed to this observation. Simultaneous treatment with MeHg and 2 g/kg EtOH caused a significant reduction in inorganic mercury levels in the kidney (P less than 0.05) compared to treatment with MeHg alone or in combination with 1 g/kg EtOH. Corresponding with the decrease in kidney inorganic mercury levels was a significant increase in urine inorganic mercury levels in this group compared to treatment with 1 g/kg ethanol + MeHg.
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PMID:Combined effects of methylmercury and ethanol on renal metallothionein and mercury residues in rats fed restricted amounts of a liquid diet. 200 70

Two major forms of hepatic microsomal cytochrome P-450 were purified from starved and acetone-treated rats. On the basis of amino acid sequence analysis, they were identified as P-450j and P-450b. Ethanol or acetone treatment of rats caused a 9-fold increase in the amount of P-450j in liver microsomes accompanied by similar increases in the rate of NADPH-dependent metabolism of carbon tetrachloride, acetone, and benzene. Immunological experiments indicated that P-450j constitutes the major catalyst of the microsomal metabolism of the latter agents and contributes by about 50% to microsomal P-450-dependent ethanol oxidation under the conditions used. The P-450j-dependent catalytic activities had a high rate of turnover. In contrast, this was not the case for the immunodetectable P-450j, indicating the occurrence of inactive forms of this protein in microsomes. Starvation or ethanol or acetone treatment caused 10-30-fold increases in the amount of both mRNA and apoprotein of P-450b,e compared to control. Run-on experiments and the concomitant increases of the P-450b,e gene products at the mRNA and protein levels indicated the appearance of mainly a transcriptional activation by acetone, ethanol, or starvation. Fasting exerted, in addition, a pronounced synergistic effect on acetone-dependent induction of P-450b,e mRNA (3-fold), apo-P-450b,e (4.3-fold), P-450j mRNA (2-fold), and apo-P-450j (2-fold). No increase of mRNA coding for P-450j, compared to control, was seen after acetone or ethanol treatment alone. The results indicate that effects of ethanol, acetone, and/or starvation on drug and xenobiotic metabolism are caused by the induction of P-450 forms belonging to at least two gene subfamilies.
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PMID:Ethanol-, fasting-, and acetone-inducible cytochromes P-450 in rat liver: regulation and characteristics of enzymes belonging to the IIB and IIE gene subfamilies. 337 38

Rats preferring ethanol differ from those preferring water in a lowered blood serum IRI level in the presence of the same level of glycemia. Ethanol preferring animals are characterized by raised function of the adrenal cortex revealed in an elevated II-oxycordicosteroid content in these glands and a lowered cholesterol level. The glucose tolerance test (4 g/kg by intragastric administration) shows a faster depletion of beta-cells of langerhans islets in ethanol preferring animals which is suggestive of a prediabetic state. A different sensitivity of the insular apparatus to glucose is noted in the study group, too. As for glycemia, rats preferring ethanol demonstrate greater resistance to 48-hour starvation as compared to rats preferring water.
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PMID:[Characteristics of the hormonal regulation of glycemia in rats with varying alcoholic motivation]. 351 59

Ethanol is constantly formed endogenously from acetaldehyde, and level of the former can be measured in both human beings and animals. Acetaldehyde can be generated in situ from the metabolism of pyruvate, threonine, deoxyribose-5-phosphate, phosphoethanolamine, alanine and presumably from other substrates. The levels of blood and tissue endogenous ethanol change as a function of various physiologic and experimental conditions such as starvation, aging, stress, cooling, adrenalectomy, etc. and are regulated by many exogenous compounds such as antimetabolites, derivatives of amino acids, lithium salts, disulfiram, cyanamide, etc. Under free choice alcohol selection situations, the levels of endogenous ethanol in rat blood and alcohol preference by the animals are negatively correlated. Similar negative correlations have been found between the levels of blood endogenous ethanol and the frequency of delirium in alcoholic patients undergoing alcohol withdrawal. Endogenous ethanol and acetaldehyde can therefore be regarded as compounds which fulfil substrate, regulatory and modulator functions.
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PMID:Endogenous ethanol--its metabolic, behavioral and biomedical significance. 353 Feb 79

The effect of ethanol on the interrelationship of lactate and glucose metabolism was investigated in eight human volunteers. Lactate and glucose kinetics and intervconversion rates were determined by the sequential administration of L-(+) lactate-U-(14)C and glucose-1-(14)C over an 8 hr period. After a 12 hr fast, the glucose turnover and recycling rates were 94.0 +/-3.8 (SEM) and 13.7 +/-1.1 mg/kg per hr, respectively. Approximately 50% of the glucose turnover or 40.7 +/-2.1 mg/kg per hr was converted to lactate, accounting for 50% of the lactate turnover rate. Lactate turnover and lactate conversion to glucose were 81.8 +/-6.2 and 16.7 +/-1.1 mg/kg per hr, respectively. Approximately 20% of the glucose turnover was derived from lactate under these conditions. During the administration of ethanol, the blood lactate concentration doubled and the lactate turnover rate declined slightly. Lactate conversion to glucose was markedly inhibited, decreasing from 16 to 5 mg/kg per hr, and the per cent of the glucose turnover derived from lactate decreased from 18 to 6. Despite the marked inhibition of lactate conversion to glucose, neither the blood glucose concentration nor the glucose turnover rate changed. Both glucose recycling and glucose conversion to lactate were decreased, indicating that ethanol inhibited peripheral glucose utilization. There was no difference in the degree of inhibition of lactate incorporation into glucose produced by ethanol when nonfasted subjects were compared with two subjects who had fasted for 48-72 hr despite the presence of hypoglycemia in the latter. These results indicate that starvation is not a prerequisite for ethanol inhibition of gluconeogenesis from lactate in humans but is necessary for the development of hypoglycemia. Inhibition of lactate incorporation into glucose in nonfasted subjects is probably masked by a concomitant increase in glycogenolysis which prevents hypoglycemia. Ethanol decreases glucose conversion to lactate as well as lactate conversion to glucose, thus inhibiting the Cori cycle.
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PMID:Glucose-lactate interrelationships: effect of ethanol. 510 Dec 94

Rats preferring ethanol were distinct from water-consuming animals in a decreased level of immunoreactive insulin im blood serum as well as in glucokinase activity of liver tissue. Per oral loading with glucose, 4 g/kg of body mass, enabled to detect a difference in the sugar phosphorylation via hexokinase and glucokinase reactions as well as the dissimilar sensitivity of the insulin system to glucose in the ethanol-, water-consuming and intermediate animals. Ethanol-consuming rats were more resistant to the effect of starvation during 48 hrs. The data obtained suggest that the characteristic properties of glucose metabolism in ethanol-consuming rats appear to be responsible for increased consumption of ethanol, which is used as optimal energy source, metabolized via pathways which did not involve the glycolytic pathway.
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PMID:[Characteristics of glucose metabolism in rats with different preferences for alcohol]. 609 27

Ethanol-inducible cytochrome P450 (CYP) 2E1 (CYP2E1) is responsible for the metabolism of many xenobiotics which exert toxic effects in humans. Specific inhibitors might constitute valuable tools in the elucidation of the pharmacological and toxicological roles of this isozyme in vivo. In the present investigation we have evaluated the effects of a drug used for treatment of ethanol withdrawal states, chloromethiazole (CMZ), on CYP2E1 expression in rat liver. A 4-fold induction of CYP2E1 was observed after 3 days of starvation, accompanied by a similar increase in the level of the corresponding mRNA. CMZ specifically inhibited the elevation of CYP2E1 mRNA and protein, but did not prevent CYP2B1 and CYP3A1 or CYP1A1 induction caused by treatment with phenobarbital or beta-naphthoflavone, respectively. From nuclear run-off experiments it was apparent that the rate of the CYP2E1 gene transcription was inhibited greatly by CMZ treatment. Rats treated with ethanol in a total enteral nutrition model had higher CYP2E1-dependent hepatic microsomal activities of p-nitrophenol hydroxylase and carbon tetrachloride-induced lipid peroxidation than controls, and simultaneous CMZ treatment abolished the ethanol-dependent induction. In vitro experiments with rat liver microsomes showed that CMZ did not act as an inhibitor of CYP2E1-dependent catalytic activities or as an inhibitor of microsomal NADPH and CYP2E1-dependent lipid peroxidation. In conclusion, we suggest that CMZ might constitute an efficient and specific inhibitor of CYP2E1 expression suitable for in vivo experiments.
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PMID:Chlormethiazole as an efficient inhibitor of cytochrome P450 2E1 expression in rat liver. 801 72

The freeze-thaw tolerance of Saccharomyces cerevisiae was examined throughout growth in aerobic batch culture. Minimum tolerance to rapid freezing (immersion in liquid nitrogen; cooling rate, approximately 200 degrees C min-1) was associated with respirofermentative (exponential) growth on glucose. However, maximum tolerance occurred not during the stationary phase but during active respiratory growth on ethanol accumulated during respirofermentative growth on glucose. The peak in tolerance occurred several hours after entry into the respiratory growth phase and did not correspond to a transient accumulation of trehalose which occurred at the point of glucose exhaustion. Substitution of ethanol with other carbon sources which permit high levels of respiration (acetate and galactose) also induced high freeze-thaw tolerance, and the peak did not occur in cells shifted directly from fermentative growth to starvation conditions or in two respiratorily incompetent mutants. These results imply a direct link with respiration, rather than exhaustion of glucose. The role of ethanol as a cryoprotectant per se was also investigated, and under conditions of rapid freezing (cooling rate, approximately 200 degrees C min-1), ethanol demonstrated a significant cryoprotective effect. Under the same freezing conditions, glycerol had little effect at high concentrations and acted as a cryosensitizer at low concentrations. Conversely, under slow-freezing conditions (step freezing at -20, -70, and then -196 degrees C; initial cooling rate, approximately 3 degrees C min-1), glycerol acted as a cryoprotectant while ethanol lost this ability. Ethanol may thus have two effects on the cryotolerance of baker's yeast, as a respirable carbon source and as a cryoprotectant under rapid-freezing conditions.
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PMID:Role of growth phase and ethanol in freeze-thaw stress resistance of Saccharomyces cerevisiae. 847 82


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