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)

Increases in transepithelial solute permeability were elicited in the frog skin with external hypertonic urea, theophylline, and vasopressin (ADH). In external hypertonic urea, which is known to increase the permeability of the extracellular (paracellular) pathway, the unidirectional transepithelial fluxes of Na (passive), K, Cl, and urea increased substantially while preserving a linear relationship to each other. The same linear relationship was also observed for the passive Na and urea fluxes in regular Ringer and under stimulation with ADH or 10 mM theophylline, indicating that their permeation pathway was extracellular. A linear relationship between Cl and urea fluxes could be demonstrated if the skins were separated according to their open circuit potentials; parallel lines were obtained with increasing intercepts on the Cl axis as the open circuit potential decreased. The slopes of the Cl vs. urea lines were not different from that obtained in external hypertonic urea, indicating that this relationship described the extracellular movement of Cl. The intercept on the ordinate was interpreted as the contribution from the transcellular Cl movement. In the presence of 0.5 mM theophylline or 10 mU/ml of ADH, mainly the transcellular movement of Cl increased, whereas 10 mM theophylline caused increases in both transcellular and extracellular Cl fluxes. These and other data were interpreted in terms of a possible intracellular control of the theophylline-induced increase in extracellular fluxes. The changes in passive solute permeability were shown to be independent of active transport. The responses of the active transport system, the transcellular and paracellular pathways to theophylline and ADH could be explained in terms of the different resulting concentrations of cyclic 3'-5'-AMP produced by each of these substances in the tissue.
J Gen Physiol 1975 May
PMID:Actions of external hypertonic urea, ADH, and theophylline on transcellular and extracellular solute permeabilities in frog skin. 108 Jul 96

Two unlinked loci controlling the glucose-repressible alcohol dehydrogenase (ADH II) in Saccharomyces cerevisiae were investigated. One locus (AD R2) was characterized by electrophoretically slow and fast alleles and by inactive adr2 mutant alleles. The ADH II pattern of heteroallelic slow X fast diploids indicates a tetrameric structure of the enzyme. AD R2 was considered as the structural gene, which codes for the ADH II subunits. Allelic adr2-f mutants could be classified by their response to the slow wild type allele (AD RS-S) in heterozygous diploids. In most cases, only the slow band appeared. In three adr2-f/ADR2-S crosses hybrid enzymes between inactive fast and active slow enzymes were formed. It was demonstrated, that allelic interactions at the protein level are not restricted to electrophoretical behaviour of hybrid enzymes. They also influence specific activities and substrate affinities. The other locus investigated, AD R1, was characterized by ADH II negative mutants (adr1) and by allelic mutants which generate only very low activity (ADR1-L). ADR1 does not influence the electrophoretic properties of slow and fast ADH II proteins. adr1 mutants have an intact structural gene, which is not expressed. The gene has probably a regulatory function with respect to ADH II synthesis.
Mol Gen Genet 1975
PMID:Genetics of alcohol dehydrogenase in Saccharomyces cerevisiae. II. Two loci controlling synthesis of the glucose-repressible ADH II. 110 50

Twenty transformed lines have been isolated as a result of the germ line insertion of a 3.2 kb alcohol dehydrogenase (Adh) gene fragment into an Adh negative strain of Drosophila melanogaster by P element-mediated transformation. More than half of these lines exhibited abnormal ADH expression. The level of ADH expression ranges from zero in some lines to near normal levels in others, and the pattern of ADH expression in the larval gut is also abnormal in many of these lines. Each of the abnormal tissue-specific patterns is stable and characterized by the absence or reduction of ADH expression in certain tissues. High levels of ectopic expression were not observed. In two of these lines, the pattern of ADH staining is highly restricted: it is limited to the medial midgut in line MM-50, and to the gastric caecae and the proventriculus in line GC-1. In heterozygotes between these two lines ADH is expressed in both of these tissues. To test the hypothesis that this abnormal expression is due to position effects, inserts were mobilized to new locations. The mobilized inserts exhibited new patterns of tissue-specific expression associated with new cytological insert locations, showing that the abnormal expression in lines MM-50 and GC-1 is due to tissue-specific position effects and not to mutations. The results are discussed in the context of chromatin structure as a possible cause of these position effects.
Mol Gen Genet 1992 Mar
PMID:Tissue-specific position effects on alcohol dehydrogenase expression in Drosophila melanogaster. 131 45

1. Gossypol, an antifertility ingredient of the cotton plant, altered specific activity of mouse liver alcohol dehydrogenase (L-ADH) and subcellular aldehyde dehydrogenase (L-ALDH) in mice of both sexes. 2. Intraperitoneal injection of a single gossypol dose, 50 mg/kg, inhibited both male and female L-ADH and cytoplasmic L-ALDH from saline controls 21 hr after drug treatment. 3. Gossypol inhibited female but not male mouse mitochondrial L-ALDH isoenzymes. 4. Gossypol-produced enzyme inhibition was determined as noncompetitive. 5. The results suggest gender-dependent sensitivity of mitochondrial L-ALDH to the gossypol inhibition. A toxic metabolic interaction between ethanol and gossypol has been indicated which suggests the contraindication of alcoholic beverages during gossypol use.
Gen Pharmacol 1991
PMID:Effect of gossypol on kinetics of mouse liver alcohol and aldehyde dehydrogenase. 193 90

Treatment of tomato seeds with ethyl methanesulphonate (EMS) followed by allyl alcohol selection of M2 seeds has led to the identification of one plant (B15-1) heterozygous for an alcohol dehydrogenase (Adh) null mutation. Genetic analysis and expression studies indicated that the mutation corresponded to the structural gene of the Adh-1 locus on chromosome 4. Homozygous Adh-1 null mutants lacked ADH-1 activity in both pollen and seeds. Using an antiserum directed against ADH from Arabidopsis thaliana, which cross-reacts with ADH-1 and ADH-2 proteins from tomato, no ADH-1 protein was detected in seeds of the null mutant. Northern blot analysis showed that Adh-1 mRNA was synthesized at wild-type levels in immature seeds of the null mutant, but dropped to 25% in mature seeds. Expression of the Adh-2 gene on chromosome 6 was unaffected. The potential use of the Adh-1 null mutant in selecting rare transposon insertion mutations in a cross with "mutable" Adh-1+ tomato lines is discussed.
Mol Gen Genet 1991 Apr
PMID:Genetic and molecular characterization of an Adh-1 null mutant in tomato. 203 10

The roles of the TATA element and sequences near the mRNA initiation site in specifying the location of initiation sites in Saccharomyces cerevisiae were examined, using the Schizosaccharomyces pombe ADH gene. The importance of spacing was demonstrated by analysis of a series of deletions that removed from 8-50 bp between the TATA element and ATG translation initiation site of this gene. Primer extension mapping showed that increasing deletion length is associated with a progressive shift downstream in the location of the initiation sites. The distance of a given site from the promoter affected the relative ability of the site to be utilized for initiation. For this gene, a permissive region for transcription initiation exists between 55 and 125 bases downstream of the TATA element, and a zone of 75-115 bases allows maximal usage of an initiation site. The presence of a TATA sequence was shown to be necessary in S. cerevisiae for maintaining the location of this "window" of initiation. The TATA sequence is essential for function of the gene in S. pombe. This gene, as well as the majority of the 63 S. cerevisiae genes surveyed, uses initiation sites which fit a PyAA/T(Pu) consensus. Cis-acting mutations were recovered which restored ADH activity to a deletion allele that initiates its mRNAs downstream of the ATG. DNA sequence and transcript analysis with these mutants confirmed the requirement of proper spacing and conformity of initiation sites to the PyAA/T(Pu) consensus for efficient transcript initiation.
Mol Gen Genet 1990 Sep
PMID:DNA sequence elements required for transcription initiation of the Schizosaccharomyces pombe ADH gene in Saccharomyces cerevisiae. 227 81

Six independent mutant lines of Nicotiana plumbaginifolia resistant to ethanol, designated E3, E8, E101, E112, E144 and E251, were isolated as germinating seedlings on selective medium. In all cases, resistance to ethanol was conferred by a single recessive nuclear mutation at the same locus. Mutant seeds and pollen lacked detectable ADH activity, with the exception of E251 where a residual activity was detected. An antiserum directed against Arabidopsis thaliana ADH detected an ADH-related polypeptide of 44 kDa present in wild-type seeds and, to a lesser extent, in the seeds of the leaky mutant E251. No ADH-related polypeptide could be detected in seeds of the other mutants. However, all of them had a nearly normal level of ADH mRNA except one which did not synthesize any mRNA. These results suggest that these ethanol-resistant mutants are impaired in one of the structural genes coding for alcohol dehydrogenase. The corresponding locus has been designated Adh1.
Mol Gen Genet 1990 Jul
PMID:Ethanol-resistant mutants of Nicotiana plumbaginifolia are deficient in the expression of pollen and seed alcohol dehydrogenase activity. 227 39

Data presented in this paper deal with a further molecular characterization of 2 out of 32 EMS-induced Arabidopsis ADH null mutants that we isolated previously. In order to localize and characterize each mutation at the molecular level, we have cloned and completely sequenced the R002 and R006 null mutant alleles. For mutant R002, which does not contain any detectable levels of ADH protein and mRNA, we have found that the mutation is due to a single C to T base pair substitution in the reading frame; this leads to the incorporation of a TAG stop codon (amber nonsense mutation). For mutant R006, which contains normal levels of inactive protein and mRNA levels, we found a G to A base pair transition. This gives rise to a Cys to Tyr amino acid substitution in the active site of the ADH enzyme.
Mol Gen Genet 1990 Nov
PMID:Sequence analysis of two null-mutant alleles of the single Arabidopsis Adh locus. 227 48

1. Values of the sodium potential (ENa), active conductance (GNa) and passive conductance (Gsh) were measured in the isolated skin of the toad Pleurodema thaul placed in an Ussing chamber, and Isaacson's test was performed with 2,4,6-trieminopyrimidine (TAP) and with amiloride. 2. The numerical estimates obtained in the presence of TAP were ENa 122.85 +/- 15.17 mV, GNa 0.493 +/- 0.09 mS/cm2 and Gsh 1.145 +/- 0.23 mS/cm2. 3. After exposure to ADH these values were as follows: ENa 85.76 +/- 12.17 mV, GNa 1.191 +/- 0.20 mS/cm2 and Gsh 0.935 +/- 0.14 mS/cm2. 4. Addition of 0.5 x 10(2-) TAP produced a 53.90 +/- 5.10% decrease in transepithelial potential and a 37.90 +/- 4.90% fall in short-circuit current. 5. Exposure to ADH increased the transepithelial potential difference 34.20 +/- 13.20% and the short-circuit current to 78.00 +/- 20.50% above the control values. 6. Comparison of the efficiency and mechanism of action of TAP and amiloride in the determination of electrical parameters shows that both agents induce a similar decrease in Gsh, a finding which could indicate that TAP blocks toad skin apical membrane Na+ channels without affecting tight junction conductance.
Gen Pharmacol 1987
PMID:Determination of the driving force for the sodium pump (ENa) and of active and passive conductances (GNa and Gsh) in isolated toad skin: influence of antidiuretic hormone. 244 89

Phenothiazines and W7, calmodulin antagonists, inhibit the water flow response produced by ADH, exogenous cyclic AMP, phosphodiesterase inhibition and serosal hypertonicity. Calmodulin antagonists had no effect on osmotic water movement in the absence of hormone. Calmodulin was isolated and localized by immunofluorescence in bladder epithelial cells. Phenothiazines inhibited toad bladder calmodulin activation of phosphodiesterase and prevented fluorescent antibody recognition. The results suggest that the calcium-calmodulin process plays a role in the hydro-osmotic response to ADH and that produced by serosal hypertonicity. The calmodulin common site occurs subsequent to cyclic AMP formation, perhaps on the microtubule-microfilament system.
Gen Pharmacol 1985
PMID:Inhibition of the hydro-osmotic response to vasopressin and hypertonicity by phenothiazines and W7, calmodulin antagonists. 299 93


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