Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C1332347 (ADH)
 2,230 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effects of the various naturally occurring amino acids on ethanol oxidation in hepatocytes from 18-hrs starved and fed rats were studied. In order to minimize the non-ADH pathways and to avoid interference with the liver amino acid uptake the ethanol concentration used was 4 mM, the amino acids being added at the same concentration. In hepatocytes from starved rats, asparagine, serine, ornithine, hydroxyproline, histidine, cysteine, alanine, glycine, glutamate, glutamine, aspartate and arginine significantly increase ethanol consumption. The stimulatory effect of glutamine being much less pronounced than the asparagine one and proline being devoid of action, the influence of ammonium chloride addition on ethanol consumption in the presence of these amino acids was studied. Ammonium chloride determines an enhancement of ethanol oxidation, the results showing, contrarily to previous data, no apparent correlation between intracellular glutamate concentration and ethanol oxidation rate but rather a relation with aspartate concentration. In hepatocytes from fed rats alanine, asparagine, cysteine, glycine, hydroxyproline, ornithine and serine still increase ethanol oxidation, although to a lesser extent than in cells from starved rats. It appears that only amino acids which are precursors of either pyruvate or aspartate or glutamate are able to activate the ethanol oxidation. Pyruvate, aspartate and glutamate supply malate-aspartate shuttle components especially in cells from starved rats, pyruvate allowing direct cytosolic reoxidation of NADH in cells from fed rats as well as from starved rats. The relative strengths of the stimulatory effect could be roughly dependent on energy demand for glucose synthesis in starved rats and for urea synthesis in fed rats.
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PMID:Comparative study of the effect of amino acids on ethanol oxidation in isolated hepatocytes from starved and fed rats. 742 19

A chimeric gene, consisting of 428 bp of the promoter sequences of the alpha-amylase gene of Drosophila melanogaster, fused to the transcribed region of the alcohol dehydrogenase (Adh) gene, was introduced into the genome of an Adhnull stock of Drosophila via P element mediated transformation. DNA analysis (Southern blotting) of three transformant strains confirmed the insertion of either one or two copies of the chimeric gene per strain. A histochemical study of ADH enzyme activity in dissected tissues of the transgenic larvae revealed that the chimeric Amy-Adh gene was expressed only in the posterior larval midgut and that this expression was repressed by dietary glucose, thus representing an expression pattern characteristic of the Amy gene. This indicates that the Amy upstream promoter sequences contain signals mediating both tissue specificity and glucose repression of the Adh structural gene in the transgenic larvae. The level of ADH activity expressed in transgenic flies was relatively low. This was paralleled by a low level of Adh mRNA, indicating a reduction in the transcriptional rate of the chimeric gene.
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PMID:Expression of an amylase--alcohol dehydrogenase chimeric gene in transgenic strains of Drosophila melanogaster. 750 62

Entamoeba histolytica ferments glucose to ethanol under the anaerobic conditions of the human colon. There is special interest in this metabolic pathway because it provides an opportunity for parasite-specific chemotherapy. Peptide sequences from a 97-kDa E. histolytica protein, which was originally isolated because of extracellular matrix binding properties, were used to clone and sequence a gene that was found to encode an E. histolytica alcohol dehydrogenase and acetaldehyde dehydrogenase (EhADH2). The EhADH2 cDNA clone had an open reading frame encoding 870 amino acids with a predicted molecular weight of 95,758. The EhADH2 cDNA clone was identical in 48% of its amino acids to the multifunctional enzyme (alcohol dehydrogenase, acetyl-CoA reductase, and pyruvate-formate-lyase-deactivase) encoded by the Escherichia coli adhE gene. The isolation of the EhADH2 protein helps define a new family of ADH enzymes that may be specific to anaerobic and facultatively anaerobic organisms.
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PMID:Entamoeba histolytica has an alcohol dehydrogenase homologous to the multifunctional adhE gene product of Escherichia coli. 793 3

Changes in the concentrations of serum electrolytes and those of water and electrolyte regulating hormones were studied in mongrel dogs undergoing a sham operation (gastrectomy) under general anesthesia. Six dogs (L-group) were infused regular lactated Ringer's solution containing 1% glucose, and other six dogs (KL-group) were infused lactated Ringer's solution containing 1% glucose and potassium 10 mEq.l-1. The serum potassium concentration decreased significantly during the surgery in the L-group, but it remained unchanged in the KL-group. Blood sugar level increased during and after the surgery in the L-group. On the other hand, the blood sugar level changed in a similar way as that of the L-group during the surgery, but it decreased after the surgery in the KL-group. NEFA level also decreased after the surgery in the KL-group. Aldosterone secretion was increased after the surgery in the L-group. On the other hand, the aldosterone secretion increased during the surgery in the KL-group. The differences of the aldosterone secretion between the groups may be due to the direct influence of potassium on the adrenal cortex. Serum concentration of ADH increased in both groups during the surgery. In the L-group, it remained later, but it recovered toward the initial level after the surgery in the KL-group. The above data indicate that no peculiar change occurred in hormonal homeostasis of subjects receiving operations under general anesthesia following the infusion of lactated Ringer's solution with high potassium concentration.
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PMID:[Changes in the intraoperative hormonal homeostasis following infusion of lactated Ringer's solution with high potassium concentration]. 801 59

The effect of mannitol and glucose on antidiuretic and natriuretic actions of ADH was investigated in water-loaded, male Sprague-Dawley rats anesthetized with sodium pentobarbital (5 mg/100g). Water diuresis was induced and sustained by continuous intravenous perfusion of hypotonic solution containing 0.3% NaCl, 1.67% glucose, 1.2% ethanol and sufficient inulin at a constant rate 150 microliters/min. Arginine vasopressin at a single dose 0.1 ng/100g was tested twice in the phase of water diuresis and in the phase of water diuresis plus mannitol osmotic diuresis. Urine samples were collected at ten-minute intervals. Three doses of mannitol (5.18, 3.63, 1.81 mumol/min/100g) were given into the right renal artery in three groups of experimental rats, respectively. Administration of mannitol did not alter renal inulin clearance but increased urine flow and excretion of sodium from experimental kidney. Our findings show that mannitol reduced antidiuretic response to ADH in the experimental kidney. This reduction was related to intraarterial mannitol doses. Local administration of mannitol increased natriuretic action of ADH in the experimental kidney. However, a small dose (1.81 mumol/min/100g) of mannitol did not increase natriuretic action of ADH. Saline and glucose (5.23 mumol/min/100g) were also infused intra-arterially to replace mannitol. The effect of saline on antidiuretic and natriuretic responses to ADH was found to be insignificant. Glucose reduced antidiuretic response to ADH as mannitol did but failed to alter natriuretic response to ADH as saline did. We conclude that mannitol does positively affect antidiuretic and natriuretic actions of ADH. Glucose has similar effect but much less than mannitol.
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PMID:The effect of mannitol on antidiuretic and natriuretic actions of ADH in rats. 819 94

The present case was a 44-year-old man who had been diagnosed as having noninsulin-dependent diabetes mellitus 2 years before admission. He gradually showed severe neuropathy and emaciation because of poor control of his blood glucose levels. He was admitted to our hospital because of disturbance of consciousness with hyponatremia. The endocrinological findings including thyroid and adrenal functions revealed no abnormalities. Insufficiency of water diuresis was noted in the water loading test. Severe orthostatic hypotension was noted during the standing up test, and an excessive response in the plasma ADH level was also noted. These findings demonstrated that excessive ADH secretion occurred to compensate for the fall in blood pressure because of the breakdown of homeostatic regulation in blood pressure due to diabetic neuropathy. It is suggested that hyponatremia seemed to be subsequently induced by hypersecretion of ADH.
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PMID:Possible involvement of hypersecretion of ADH in hyponatremia in a diabetic patient complicated with severe neuropathy. 831 11

Expression of the alpha-amylase gene is highly repressed by dietary glucose in Drosophila melanogaster larvae. Here, we show that glucose repression is controlled by DNA sequences that are located upstream of the transcribed region. Recombinant gene constructions, in which the amylase promoter sequences were fused with the transcribed region of the Adh gene, were expressed in transgenic Drosophila larvae. The expression of ADH from the recombinant gene was shown to be subject to glucose repression. The function of potential regulatory cis-acting elements within the glucose responsive upstream region was examined by deletion analysis and by site-directed mutagenesis, coupled with expression assays in transformed larvae. The upstream deletion analysis showed that essential elements, both for overall activity and for glucose repression of the amylase gene, are located within a 109-bp region upstream of the transcription start site. Site-directed mutagenesis of these upstream sequences showed that the TATA motif, at position -31, and a novel 36-bp element, at position -109, were necessary for full activity of the amylase promoter. None of the introduced mutations resulted in loss of glucose responsiveness. These results indicate that glucose repression, in Drosophila, is mediated by transcriptional mechanisms that involve multiple, functionally redundant DNA elements.
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PMID:A short 5'-flanking region mediates glucose repression of amylase gene expression in Drosophila melanogaster. 832 86

Using a Saccharomyces cerevisiae ADH1 probe, a gene coding for a cytoplasmic alcohol dehydrogenase from Kluyveromyces marxianus ATCC 12424 (formerly K. fragilis) has been cloned. This gene is able to restore alcoholic fermentation in an ADH-null strain of S. cerevisiae and its encoded protein shows strong similarity with other yeast alcohol dehydrogenases (from S. cerevisiae, Schizosaccharomyces pombe and its close relative K. lactis). The product of the gene expressed in S. cerevisiae co-migrates on native gel with a K. marxianus ADH isozyme which is more active in cells growing on non-fermentable carbon sources than on glucose. This behaviour is in contrast with that of the two cytoplasmic ADH isozymes of K. lactis which are both more active in glucose-growing than in ethanol-growing cells.
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PMID:Sequence of a gene coding for a cytoplasmic alcohol dehydrogenase from Kluyveromyces marxianus ATCC 12424. 848 63

To investigate pancreatic endocrine function in brain-dead patients, an intravenous glucose tolerance test (i.v. GTT) was performed in 8 brain-dead subjects maintained using the combined administration of vasopressin (ADH) and catecholamines during the first 3 days following the onset of brain death. Ten healthy adults served as control subjects. Although plasma glucose concentrations markedly increased and exceeded 300 mg/dl in most subjects just after the onset of brain death, they decreased to less than 200 mg/dl in most subjects after 24 h. The early insulin release also was significantly lower in brain dead subjects compared to controls (p < 0.01). The late insulin release was not decreased compared to controls but rather increased, which was accompanied by decreased glucose disappearance rate. The early insulin release recovered rapidly during the first 3 days following brain death without significant changes in the plasma hormone concentrations such as epinephrine, human growth hormone, thyroid-stimulating hormone, triiodothyronine, thyroxine, cortisol, and glucagon. The early insulin release and the plasma glucose concentration just before i.v. GTT was negatively correlated (R = -0.55, p < 0.05). We suggest awaiting recovery from hyperglycemia and early insulin release provides a reasonable approach to transplantation of the pancreas.
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PMID:Transient suppression of pancreatic endocrine function in patients following brain death. 865 94

The Candida albicans ADH1 gene encodes an alcohol dehydrogenase which is immunogenic during infections in humans. The ADH1 gene was isolated and sequenced, and the 5'- and 3'-ends of its mRNA were mapped. The gene encodes a 350 amino acid polypeptide with strong homology (70.5-85.2% identity) to alcohol dehydrogenases from Saccharomyces cerevisiae, Kluyveromyces lactis and Schizosaccharomyces pombe. The cloned C. albicans ADH1 gene was shown to be functional through complementation of adh mutations and efficient production of active alcohol dehydrogenase in S. cerevisiae. Northern analysis of C. albicans RNA revealed that ADH1 mRNA levels were regulated in response to carbon source and during batch growth. During growth on glucose, ADH1 mRNA levels rose to maximum levels during late exponential growth phase and declined to low levels in stationary phase. The ADH1 mRNA was relatively abundant during growth on galactose, glycerol, pyruvate, lactate or succinate, and less abundant during growth on glucose or ethanol. Alcohol dehydrogenase levels did not correlate closely with ADH1 mRNA levels under the growth conditions studied, suggesting either that this locus is controlled at both transcriptional and post-transcriptional levels, or that other differentially regulated ADH loci exist in C. albicans.
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PMID:Structure and regulation of the Candida albicans ADH1 gene encoding an immunogenic alcohol dehydrogenase. 868 75


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