Journal articles on the topic 'ADH-1'
To see the other types of publications on this topic, follow the link: ADH-1.
Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles
Consult the top 50 journal articles for your research on the topic 'ADH-1.'
Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.
You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.
Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.
1
Lin, Guang-Huey, Ming-Chuan Hsieh, and Hung-Yu Shu. "Role of Iron-Containing Alcohol Dehydrogenases in Acinetobacter baumannii ATCC 19606 Stress Resistance and Virulence." International Journal of Molecular Sciences 22, no. 18 (September 14, 2021): 9921. http://dx.doi.org/10.3390/ijms22189921.
Full textAbstract:
Most bacteria possess alcohol dehydrogenase (ADH) genes (Adh genes) to mitigate alcohol toxicity, but these genes have functions beyond alcohol degradation. Previous research has shown that ADH can modulate quorum sensing in Acinetobacter baumannii, a rising opportunistic pathogen. However, the number and nature of Adh genes in A. baumannii have not yet been fully characterized. We identified seven alcohol dehydrogenases (NAD+-ADHs) from A. baumannii ATCC 19606, and examined the roles of three iron-containing ADHs, ADH3, ADH4, and ADH6. Marker-less mutation was used to generate Adh3, Adh4, and Adh6 single, double, and triple mutants. Disrupted Adh4 mutants failed to grow in ethanol-, 1-butanol-, or 1-propanol-containing mediums, and recombinant ADH4 exhibited strongest activity against ethanol. Stress resistance assays with inorganic and organic hydroperoxides showed that Adh3 and Adh6 were key to oxidative stress resistance. Virulence assays performed on the Galleria mellonella model organism revealed that Adh4 mutants had comparable virulence to wild-type, while Adh3 and Adh6 mutants had reduced virulence. The results suggest that ADH4 is primarily involved in alcohol metabolism, while ADH3 and ADH6 are key to stress resistance and virulence. Further investigation into the roles of other ADHs in A. baumannii is warranted.
2
&NA;. "ADH 1." Reactions Weekly &NA;, no. 1389 (February 2012): 7. http://dx.doi.org/10.2165/00128415-201213890-00018.
Full text
3
van Ooij, C., R. C. Snyder, B. W. Paeper, and G. Duester. "Temporal expression of the human alcohol dehydrogenase gene family during liver development correlates with differential promoter activation by hepatocyte nuclear factor 1, CCAAT/enhancer-binding protein alpha, liver activator protein, and D-element-binding protein." Molecular and Cellular Biology 12, no. 7 (July 1992): 3023–31. http://dx.doi.org/10.1128/mcb.12.7.3023-3031.1992.
Full textAbstract:
The human class I alcohol dehydrogenase (ADH) gene family consists of ADH1, ADH2, and ADH3, which are sequentially activated in early fetal, late fetal, and postnatal liver, respectively. Analysis of ADH promoters revealed differential activation by several factors previously shown to control liver transcription. In cotransfection assays, the ADH1 promoter, but not the ADH2 or ADH3 promoter, was shown to respond to hepatocyte nuclear factor 1 (HNF-1), which has previously been shown to regulate transcription in early liver development. The ADH2 promoter, but not the ADH1 or ADH3 promoter, was shown to respond to CCAAT/enhancer-binding protein alpha (C/EBP alpha), a transcription factor particularly active during late fetal liver and early postnatal liver development. The ADH1, ADH2, and ADH3 promoters all responded to the liver transcription factors liver activator protein (LAP) and D-element-binding protein (DBP), which are most active in postnatal liver. For all three promoters, the activation by LAP or DBP was higher than that seen by HNF-1 or C/EBP alpha, and a significant synergism between C/EBP alpha and LAP was noticed for the ADH2 and ADH3 promoters when both factors were simultaneously cotransfected. A hierarchy of ADH promoter responsiveness to C/EBP alpha and LAP homo- and heterodimers is suggested. In all three ADH genes, LAP bound to the same four sites previously reported for C/EBP alpha (i.e., -160, -120, -40, and -20 bp), but DBP bound strongly only to the site located at -40 bp relative to the transcriptional start. Mutational analysis of ADH2 indicated that the -40 bp element accounts for most of the promoter regulation by the bZIP factors analyzed. These studies suggest that HNF-1 and C/EBP alpha help establish ADH gene family transcription in fetal liver and that LAP and DBP help maintain high-level ADH gene family transcription in postnatal liver.
4
van Ooij, C., R. C. Snyder, B. W. Paeper, and G. Duester. "Temporal expression of the human alcohol dehydrogenase gene family during liver development correlates with differential promoter activation by hepatocyte nuclear factor 1, CCAAT/enhancer-binding protein alpha, liver activator protein, and D-element-binding protein." Molecular and Cellular Biology 12, no. 7 (July 1992): 3023–31. http://dx.doi.org/10.1128/mcb.12.7.3023.
Full textAbstract:
The human class I alcohol dehydrogenase (ADH) gene family consists of ADH1, ADH2, and ADH3, which are sequentially activated in early fetal, late fetal, and postnatal liver, respectively. Analysis of ADH promoters revealed differential activation by several factors previously shown to control liver transcription. In cotransfection assays, the ADH1 promoter, but not the ADH2 or ADH3 promoter, was shown to respond to hepatocyte nuclear factor 1 (HNF-1), which has previously been shown to regulate transcription in early liver development. The ADH2 promoter, but not the ADH1 or ADH3 promoter, was shown to respond to CCAAT/enhancer-binding protein alpha (C/EBP alpha), a transcription factor particularly active during late fetal liver and early postnatal liver development. The ADH1, ADH2, and ADH3 promoters all responded to the liver transcription factors liver activator protein (LAP) and D-element-binding protein (DBP), which are most active in postnatal liver. For all three promoters, the activation by LAP or DBP was higher than that seen by HNF-1 or C/EBP alpha, and a significant synergism between C/EBP alpha and LAP was noticed for the ADH2 and ADH3 promoters when both factors were simultaneously cotransfected. A hierarchy of ADH promoter responsiveness to C/EBP alpha and LAP homo- and heterodimers is suggested. In all three ADH genes, LAP bound to the same four sites previously reported for C/EBP alpha (i.e., -160, -120, -40, and -20 bp), but DBP bound strongly only to the site located at -40 bp relative to the transcriptional start. Mutational analysis of ADH2 indicated that the -40 bp element accounts for most of the promoter regulation by the bZIP factors analyzed. These studies suggest that HNF-1 and C/EBP alpha help establish ADH gene family transcription in fetal liver and that LAP and DBP help maintain high-level ADH gene family transcription in postnatal liver.
5
Liu, Xueqian, Yanpeng Dong, Jing Zhang, Aixiang Zhang, Lei Wang, and Lu Feng. "Two novel metal-independent long-chain alkyl alcohol dehydrogenases from Geobacillus thermodenitrificans NG80-2." Microbiology 155, no. 6 (June 1, 2009): 2078–85. http://dx.doi.org/10.1099/mic.0.027201-0.
Full textAbstract:
Two alkyl alcohol dehydrogenase (ADH) genes from the long-chain alkane-degrading strain Geobacillus thermodenitrificans NG80-2 were characterized in vitro. ADH1 and ADH2 were prepared heterologously in Escherichia coli as a homooctameric and a homodimeric protein, respectively. Both ADHs can oxidize a broad range of alkyl alcohols up to at least C30, as well as 1,3-propanediol and acetaldehyde. ADH1 also oxidizes glycerol, and ADH2 oxidizes isopropyl alcohol, isoamylol, acetone, octanal and decanal. The best substrate is ethanol for ADH1 and 1-octanol for ADH2. For both ADHs, the optimum assay condition is at 60 °C and pH 8.0, and both NAD and NADP can be used as the cofactor. Sequence analysis reveals that ADH1 and ADH2 belong to the Fe-containing/activated long-chain ADHs. However, the two enzymes contain neither Fe nor other metals, and Fe is not required for the activity, suggesting a new type of ADH. The ADHs characterized here are potentially useful in crude oil bioremediation and other bioconversion processes.
6
Mangum, Paul D., and Ellen B. Peffley. "INHERITANCE OF PGM-1, ADH-1, AND 6-PGDH-1 in ALLIUM FISTULOSUM L." HortScience 27, no. 6 (June 1992): 644d—644. http://dx.doi.org/10.21273/hortsci.27.6.644d.
Full textAbstract:
The inheritance and linkage relationships among PGM-1, ADH-1, and 6-PGDH-1 were determined for Allium fistulosum (Japanese bunching onion) individuals. Individuals expressing Pgm-11/Pgm-12, Adh-13/Adh-14, Adh-13/Adh-15, or 6-Pgdh-11/6-Pgdh-12 were selfed seperately. These backcrosses and their reciprocals were made: Pgm-11/Pgm-12 to Pgm-11/Pgm-11 or Pgm-12/Pgm-12; Adh-13/Adh-14 to Adh-13/Adh-13 or Adh-14/Adh-14, 6-Pgdh-11/6-Pgdh-12 to 6-Pgdh-11/6-Pgdh-11 or 6-Pgdh-12/6-Pgdh-12. Progeny segregations were tested for Mendelian inheritance using a chi-square goodness of fit test. Expression of 6-Pgdh has not been previously reported in onion. Two zones of activity were detected and were designated as 6-PGDH-1 and 6-PGDH-2. 6-PGDH-2 was monomorphic for all individuals tested. Progeny segregation of 6-PGDH-1 fit a model for a dimeric enzyme encoded by one disomic locus with two alleles, expressed as fast (1) and slow (2), in a dimeric enzyme pattern in heterozygous individuals.
7
Haseba, Takeshi, Kouji Kameyama, Keiko Mashimo, and Youkichi Ohno. "Dose-Dependent Change in Elimination Kinetics of Ethanol due to Shift of Dominant Metabolizing Enzyme from ADH 1 (Class I) to ADH 3 (Class III) in Mouse." International Journal of Hepatology 2012 (2012): 1–8. http://dx.doi.org/10.1155/2012/408190.
Full textAbstract:
ADH 1 and ADH 3 are major two ADH isozymes in the liver, which participate in systemic alcohol metabolism, mainly distributing in parenchymal and in sinusoidal endothelial cells of the liver, respectively. We investigated how these two ADHs contribute to the elimination kinetics of blood ethanol by administering ethanol to mice at various doses, and by measuring liver ADH activity and liver contents of both ADHs. The normalized AUC (AUC/dose) showed a concave increase with an increase in ethanol dose, inversely correlating with β.CLT(dose/AUC) linearly correlated with liver ADH activity and also with both the ADH-1 and -3 contents (mg/kg B.W.). When ADH-1 activity was calculated by multiplying ADH-1 content by itsVmax/mg (4.0) and normalized by the ratio of liver ADH activity of each ethanol dose to that of the control, the theoretical ADH-1 activity decreased dose-dependently, correlating with β. On the other hand, the theoretical ADH-3 activity, which was calculated by subtracting ADH-1 activity from liver ADH activity and normalized, increased dose-dependently, correlating with the normalized AUC. These results suggested that the elimination kinetics of blood ethanol in mice was dose-dependently changed, accompanied by a shift of the dominant metabolizing enzyme from ADH 1 to ADH 3.
8
Haseba, Takeshi, Takahisa Okuda, Motoyo Maruyama, Toshio Akimoto, Gregg Duester, and Youkichi Ohno. "Roles of Two Major Alcohol Dehydrogenases, ADH1 (Class I) and ADH3 (Class III), in the Adaptive Enhancement of Alcohol Metabolism Induced by Chronic Alcohol Consumption in Mice." Alcohol and Alcoholism 55, no. 1 (December 11, 2019): 11–19. http://dx.doi.org/10.1093/alcalc/agz091.
Full textAbstract:
Abstract Aims It is still unclear which enzymes contribute to the adaptive enhancement of alcohol metabolism by chronic alcohol consumption (CAC). ADH1 (Class I) has the lowest Km for ethanol and the highest sensitivity for 4-methylpyrazole (4MP) among ADH isozymes, while ADH3 (Class III) has the highest Km and the lowest sensitivity. We investigated how these two major ADHs relate to the adaptive enhancement of alcohol metabolism. Methods Male mice with different ADH genotypes (WT, Adh1−/− and Adh3−/−) were subjected to CAC experiment using a 10% ethanol solution for 1 month. Alcohol elimination rate (AER) was measured after ethanol injection at a 4.0 g/kg dose. 4MP-sensitive and -insensitive AERs were measured by the simultaneous administration of 4MP at a dose of 0.5 mmol/kg in order to estimate ADH1 and non-ADH1 pathways. Results AER was enhanced by CAC in all ADH genotypes, especially more than twofold in Adh1−/− mice, with increasing ADH1 and/or ADH3 liver contents, but not CYP2E1 content. 4MP-sensitive AER was also increased by CAC in WT and Adh3−/− strains, which was greater in Adh3−/− than in WT mice. The sensitive AER was increased even in Adh1−/− mice probably due to the increase in ADH3, which is semi-sensitive for 4MP. 4MP-insensitive AER was also increased in WT and Adh1−/− by CAC, but not in Adh3−/− mice. Conclusion ADH1 contributes to the enhancement of alcohol metabolism by CAC, particularly in the absence of ADH3. ADH3 also contributes to the enhancement as a non-ADH1 pathway, especially in the absence of ADH1.
9
Mitchell, L. E., E. S. Dennis, and W. J. Peacock. "Molecular analysis of an alcohol dehydrogenase (Adh) gene from chromosome 1 of wheat." Genome 32, no. 3 (June 1, 1989): 349–58. http://dx.doi.org/10.1139/g89-454.
Full textAbstract:
We have cloned and determined the nucleotide sequence of a gene encoding alcohol dehydrogenase (Adh) from Triticum aestivum cv. Millewa. Southern analysis using cv. Chinese Spring nullisomic–tetrasomic and ditelosomic lines established that the cloned gene mapped to the long arm of chromosome 1A and does not correspond to any previously identified wheat Adh locus. Southern analysis also provided evidence for triplicate copies of this Adh gene on the homoeologous group 1 chromosomes, while Northern blots indicated that the homoeologous group 1 Adh genes, like several other plant Adh genes, are transcribed under anaerobic conditions. Sequence analysis indicates that the cloned gene has a structure similar to both monocot and dicot Adh genes with an open reading frame encoding a polypeptide of 379 amino acids. Sequences important for eucaryotic gene expression such as the TATA box, polyadenylation signal, and intron splice sites were found in the expected positions. The open reading frame is interrupted by 8 introns which are in identical positions with 8 of the 9 introns in maize and pea Adh genes, suggesting that during evolution there are processes occurring that result in the loss of introns. Sequence analysis also revealed that the cloned wheat Adh gene shared extensive homology with the barley Adh3 gene not only in the coding region but also in the noncoding regions. However, this homology is discontinuous as a result of a 1.8-kbp insertion (TLM), which is present in the cloned wheat Adh gene and absent in the barley Adh3 gene. Sequence analysis of this insertion reveals features characteristic of the short terminal inverted repeat class of eucaryotic transposable elements. We have no evidence for the transposition of the TLM element. However, Southern blots reveal multiple copies of sequences related to TLM in the wheat genome and in other closely related species, suggesting that transposition may once have played an important role in the evolution of the Gramineae family.Key words: Triticum aestivum, alcohol dehydrogenase, Adh, chromosome 1, anaerobic induction, insertion element, transposable element.
10
Ayer, S., and C. Benyajati. "Conserved enhancer and silencer elements responsible for differential Adh transcription in Drosophila cell lines." Molecular and Cellular Biology 10, no. 7 (July 1990): 3512–23. http://dx.doi.org/10.1128/mcb.10.7.3512-3523.1990.
Full textAbstract:
The distal promoter of Adh is differentially expressed in Drosophila tissue culture cell lines. After transfection with an exogenous Adh gene, there was a specific increase in distal alcohol dehydrogenase (ADH) transcripts in ADH-expressing (ADH+) cells above the levels observed in transfected ADH-nonexpressing (ADH-) cells. We used deletion mutations and a comparative transient-expression assay to identify the cis-acting elements responsible for enhanced Adh distal transcription in ADH+ cells. DNA sequences controlling high levels of distal transcription were localized to a 15-base-pair (bp) region nearly 500 bp upstream of the distal RNA start site. In addition, a 61-bp negative cis-acting element was found upstream from and adjacent to the enhancer. When this silencer element was deleted, distal transcription increased only in the ADH+ cell line. These distant upstream elements must interact with the promoter elements, the Adf-1-binding site and the TATA box, as they only influenced transcription when at least one of these two positive distal promoter elements was present. Internal deletions targeted to the Adf-1-binding site or the TATA box reduced transcription in both cell types but did not affect the transcription initiation site. Distal transcription in transfected ADH- cells appears to be controlled primarily through these promoter elements and does not involve the upstream regulatory elements. Evolutionary conservation in distantly related Drosophila species suggests the importance of these upstream elements in correct developmental and tissue-specific expression of ADH.
11
Ayer, S., and C. Benyajati. "Conserved enhancer and silencer elements responsible for differential Adh transcription in Drosophila cell lines." Molecular and Cellular Biology 10, no. 7 (July 1990): 3512–23. http://dx.doi.org/10.1128/mcb.10.7.3512.
Full textAbstract:
The distal promoter of Adh is differentially expressed in Drosophila tissue culture cell lines. After transfection with an exogenous Adh gene, there was a specific increase in distal alcohol dehydrogenase (ADH) transcripts in ADH-expressing (ADH+) cells above the levels observed in transfected ADH-nonexpressing (ADH-) cells. We used deletion mutations and a comparative transient-expression assay to identify the cis-acting elements responsible for enhanced Adh distal transcription in ADH+ cells. DNA sequences controlling high levels of distal transcription were localized to a 15-base-pair (bp) region nearly 500 bp upstream of the distal RNA start site. In addition, a 61-bp negative cis-acting element was found upstream from and adjacent to the enhancer. When this silencer element was deleted, distal transcription increased only in the ADH+ cell line. These distant upstream elements must interact with the promoter elements, the Adf-1-binding site and the TATA box, as they only influenced transcription when at least one of these two positive distal promoter elements was present. Internal deletions targeted to the Adf-1-binding site or the TATA box reduced transcription in both cell types but did not affect the transcription initiation site. Distal transcription in transfected ADH- cells appears to be controlled primarily through these promoter elements and does not involve the upstream regulatory elements. Evolutionary conservation in distantly related Drosophila species suggests the importance of these upstream elements in correct developmental and tissue-specific expression of ADH.
12
Bayer, C. A., S. W. Curtiss, J. A. Weaver, and D. T. Sullivan. "Delineation of cis-acting sequences required for expression of Drosophila mojavensis Adh-1." Genetics 131, no. 1 (May 1, 1992): 143–53. http://dx.doi.org/10.1093/genetics/131.1.143.
Full textAbstract:
Abstract The control of expression of the Adh-1 gene of Drosophila mojavensis has been analyzed by transforming ADH null Drosophila melanogaster hosts with P element constructs which contain D. mojavensis Adh-1 having deletions of different extent in the 5' and 3' ends. Adh-1 expression in the D. melanogaster hosts is qualitatively similar to expression in D. mojavensis, although expression is quantitatively lower in transformants. Deletions of the 5' end indicate that information required for normal temporal and tissue expression in larvae is contained within 70 bp of the transcription start site. However, deletion constructs to -70 are deficient in ovarian nurse cell expression, whereas the additional upstream sequences present in constructs containing deletions to -257 do support expression in the ovary. Comparison of the nucleotide sequence in the -257 to -70 region of Adh-1 of four species: D. mojavensis and Drosophila arizona, which express Adh-1 in the ovary, and Drosophila mulleri and Drosophila navojoa, which do not, has led to the identification of regions of sequence similarity that correlate with ovary expression. One of these bears a striking similarity to a conserved sequence located upstream of the three heat shock genes that have constitutive ovarian expression and may be an ovarian control element. We have identified an aberrant aspect of Adh-1 expression. In transformants which carry an Adh-1 gene without a functional upstream Adh-2 gene Adh-1 expression continues into the adult stage instead of ceasing at the onset of metamorphosis. In transformants with a functional Adh-2 gene, Adh-1 expression ceases in the third larval instar stage and aberrant expression in the adult stage does not occur.
13
Menotti-Raymond, M., W. T. Starmer, and D. T. Sullivan. "Characterization of the structure and evolution of the Adh region of Drosophila hydei." Genetics 127, no. 2 (February 1, 1991): 355–66. http://dx.doi.org/10.1093/genetics/127.2.355.
Full textAbstract:
Abstract Drosophila of the repleta group have a duplication of the gene which encodes alcohol dehydrogenase (ADH). We report the nucleotide sequence of an 8.4-kb region of genomic DNA of Drosophila hydei which includes the entire Adh region. Analysis of this sequence reveals similarity in organization to the Adh region of Drosophila mojavensis and Drosophila mulleri of the mulleri subgroup, with three genes ordered 5' to 3', Adh-psi, Adh-2, Adh-1. Deletion of a nucleotide in the second codon of each pseudogene suggests that the first Adh duplication occurred before the divergence of the hydei and mulleri subgroups. However, Adh-1 and Adh-2 of D. hydei are significantly more alike than Adh-1 and Adh-2 of D. mojavensis. Models to account for the difference in similarity between the coding genes were tested by orthologous and paralogous comparisons of the extent of sequence divergence. A model which proposes that independent duplication events generated Adh-1 and Adh-2 in the two lineages is supported by these data. The D. hydei pseudogene is transcribed and the transcript is processed in a complex manner. An intron of greater than 6.2 kb exists between the first "coding" exon and an upstream exon which is approximately 250 nucleotides in length.
14
Shintani, Yasushi, Yuri Fukumoto, Nina Chaika, Paul M. Grandgenett, Michael A. Hollingsworth, Margaret J. Wheelock, and Keith R. Johnson. "ADH-1 suppresses N-cadherin-dependent pancreatic cancer progression." International Journal of Cancer 122, no. 1 (2007): 71–77. http://dx.doi.org/10.1002/ijc.23027.
Full text
15
Sheehan, M. C., C. J. Bailey, B. C. A. Dowds, and D. J. McConnell. "A new alcohol dehydrogenase, reactive towards methanol, from Bacillus stearothermophilus." Biochemical Journal 252, no. 3 (June 15, 1988): 661–66. http://dx.doi.org/10.1042/bj2520661.
Full textAbstract:
An NAD+-dependent alcohol dehydrogenase (ADH) was purified to homogeneity from an aerobic strain of Bacillus stearothermophilus, DSM 2334 (ADH 2334), and compared with the ADH from B. stearothermophilus NCA 1503 (ADH 1503). When an antibody raised against ADH 2334 was used, no cross-reactivity with ADH 1503 was observed on Western blots; by means of an enzyme-linked-immunoabsorbent-assay (‘e.l.i.s.a.’) procedure, it was found that ADH 1503 had less than 6% of the antigenic activity of ADH 2334. Amino acid analyses detected very small differences in composition, equivalent to about 40 sequence changes, between the two enzymes. The new enzyme has the same six-amino-acid N-terminal sequence as ADH 1503. ADH 2334, but not ADH 1503, is reactive towards methanol; both enzymes can oxidize ethanol, propan-1-ol, butan-1-ol and butan-2-ol. The new enzyme has a distinctive pH optimum at pH 5.5-6 and has significantly lower KEthanolm and kEthanolcat. values than those of ADH 1503. From steady-state kinetic parameters of the reaction with ethanol, propan-1-ol and butan-1-ol, it was shown that ADH 2334 has an ordered mechanism in both directions, with NAD+ being the compulsory first substrate in alcohol oxidation and NADH release being the rate-limiting step. ADH 1503 has an ordered addition of NAD+ and alcohol, but NADH release is not rate-limiting.
16
Aaren*, Vedangi, Godi Sudhakar, and Girinadh L.R.S. "Polymorphisms in alcohol metabolizing genes ADH2 and ADH3 and susceptibility to pancreatitis in alcoholics." International Journal of Bioassays 6, no. 03 (February 28, 2017): 5297. http://dx.doi.org/10.21746/ijbio.2017.03.002.
Full textAbstract:
In both developed and developing countries, overuse of alcohol is a considered as the major cause of acute and chronic pancreatitis. Prolonged overconsumption of alcohol for 5–10 years typically precedes the initial attack of acute alcoholic pancreatitis. It is observed that only a minority (around 5%) of alcoholics develop pancreatitis. It is now established that the pancreas has the capacity to metabolize ethanol. Previous studies have shown that there are two major pathways of ethanol metabolism, oxidative and non-oxidative. Oxidative ethanol metabolism involves the conversion of ethanol to acetaldehyde, a reaction that is catalysed by aldehyde dehydrogenase (ADH) with contributions from cytochrome P450 enzyme (CYP2E1) and possibly also catalase. Genetic factors regulating alcohol metabolism could predispose in developing alcoholic pancreatitis (AP). We investigated the association of polymorphisms in ADH enzymes with the alcoholic pancreatitis in North coastal Andhra Pradesh. Patients with alcoholic pancreatitis (AP; n = 100), alcoholic controls (AC; n = 100), and healthy controls (HC; n = 100) were included in the study. Blood samples were collected from the subjects in EDTA coated vials. DNA was extracted and genotyping for ADH2 and ADH3 was done by PCR-RFLP (polymerase chain reaction restriction fragment length polymorphism). The products were analysed by gel electrophoresis. The frequency distribution of ADH3*1/*1 genotype was significantly higher in AP group (54%) compared with AC (35%), and HC (42%), and was found to be associated with increased risk of alcoholic pancreatitis. There was no statistically significant difference between the frequency distribution of ADH3*1/*1, ADH3*1/*2, and ADH3*2/*2 genotypes between AC and HC. There was no statistically significant difference between the frequency distribution of ADH2*1/*1, ADH2*1/*2, and ADH2*2/*2 genotypes in AP compared with AC and HC. This study shows that carriers of ADH3*1/*1 individuals consuming alcohol are at higher risk for alcoholic pancreatitis than those with other genotypes such as ADH3*1/*2 and ADH3*2/*2.
17
Starmer, William T., and J. S. F. Barker. "Ecological genetics of the Adh-1 locus of Drosophila buzzatii." Biological Journal of the Linnean Society 28, no. 4 (August 1986): 373–85. http://dx.doi.org/10.1111/j.1095-8312.1986.tb01765.x.
Full text
18
Gupta, M., D. Barnes, J. Losos, G. Spehar, M. Bednarcik, and W. P. Peters. "Anti-tumor activity of ADH-1 in vitro and in vivo in combination with paclitaxel in ovarian cancer cell lines." Journal of Clinical Oncology 25, no. 18_suppl (June 20, 2007): 16050. http://dx.doi.org/10.1200/jco.2007.25.18_suppl.16050.
Full textAbstract:
16050 Background: ADH-1 is a novel N-cadherin (Ncad) antagonist. Ncad is a protein present on certain tumor cells and established tumor blood vessels. Its expression on tumor cells increases as they become more aggressive, invasive and metastatic, making it an important target for anti-cancer therapy. ADH-1 was well tolerated in phase I studies and demonstrated evidence of anti-tumor activity in 7 patients whose tumors expressed Ncad. Patient enrollment in two phase II single agent trials concluded at the end of 2006. We report on the anti-tumor activity of ADH-1 in combination with paclitaxel in cancer cell lines in vitro and in the A2780 (Ncad positive) ovarian xenograft model in vivo. Methods: In vitro cytotoxicity of SKOV-3 (ovarian) cells exposed to a fixed ratio of ADH-1 and paclitaxel simultaneously was evaluated by the WST-1 cell proliferation assay. In vivo anti-tumor activity of ADH-1, paclitaxel, and the combination was evaluated in the A2780 xenograft model. ADH-1 100 mg/kg was administered bid IP for 21 days and paclitaxel was administered qod IV for 5 days. Results: In vitro cytotoxicity assays evaluated for combination effects using CalcuSyn software indicated a strong synergistic effect of ADH-1 in combination with paclitaxel (CI <1). In vivo paclitaxel treatment produced a median Time to Endpoint (TTE) (tumor volume >2gm or study end at 60 day) of 32.1 days and 73% Tumor Growth Delay (TGD), compared to control (p=0.028). For the paclitaxel group, there was only one Tumor Free Survivor (TFS) and one transient Complete Responder (CR). ADH-1 produced a TTE of 16.1 and a -13% TGD (p>0.05). The combination of ADH-1 and paclitaxel produced a median TTE of 48.6 days, corresponding to 161% TGD (p<0.0016 compared to untreated controls, p<0.003 for vehicle treated, and p<0.005 compared to paclitaxel alone). The combination therapy generated durable CR in 5 animals, 1 transient CR and 2 PR. The combination therapy had similar toxicity to paclitaxel alone. Conclusions: In this ovarian cancer model, the combination of ADH-1 with paclitaxel produced a synergistic anti-tumor effect. Based in part on these encouraging pre-clinical results, a clinical program of ADH-1 in combination with chemotherapeutic agents has been initiated. No significant financial relationships to disclose.
19
Burdette, D., and J. G. Zeikus. "Purification of acetaldehyde dehydrogenase and alcohol dehydrogenases from Thermoanaerobacter ethanolicus 39E and characterization of the secondary-alcohol dehydrogenase (2° Adh) as a bifunctional alcohol dehydrogenase-acetyl-CoA reductive thioesterase." Biochemical Journal 302, no. 1 (August 15, 1994): 163–70. http://dx.doi.org/10.1042/bj3020163.
Full textAbstract:
The purification and characterization of three enzymes involved in ethanol formation from acetyl-CoA in Thermoanaerobacter ethanolicus 39E (formerly Clostridium thermohydrosulfuricum 39E) is described. The secondary-alcohol dehydrogenase (2 degrees Adh) was determined to be a homotetramer of 40 kDa subunits (SDS/PAGE) with a molecular mass of 160 kDa. The 2 degrees Adh had a lower catalytic efficiency for the oxidation of 1 degree alcohols, including ethanol, than for the oxidation of secondary (2 degrees) alcohols or the reduction of ketones or aldehydes. This enzyme possesses a significant acetyl-CoA reductive thioesterase activity as determined by NADPH oxidation, thiol formation and ethanol production. The primary-alcohol dehydrogenase (1 degree Adh) was determined to be a homotetramer of 41.5 kDa (SDS/PAGE) subunits with a molecular mass of 170 kDa. The 1 degree Adh used both NAD(H) and NADP(H) and displayed higher catalytic efficiencies for NADP(+)-dependent ethanol oxidation and NADH-dependent acetaldehyde (identical to ethanal) reduction than for NADPH-dependent acetaldehyde reduction or NAD(+)-dependent ethanol oxidation. The NAD(H)-linked acetaldehyde dehydrogenase was a homotetramer (360 kDa) of identical subunits (100 kDa) that readily catalysed thioester cleavage and condensation. The 1 degree Adh was expressed at 5-20% of the level of the 2 degrees Adh throughout the growth cycle on glucose. The results suggest that the 2 degrees Adh primarily functions in ethanol production from acetyl-CoA and acetaldehyde, whereas the 1 degree Adh functions in ethanol consumption for nicotinamide-cofactor recycling.
20
Garcia, N. H., S. I. Pomposiello, and J. L. Garvin. "Nitric oxide inhibits ADH-stimulated osmotic water permeability in cortical collecting ducts." American Journal of Physiology-Renal Physiology 270, no. 1 (January 1, 1996): F206—F210. http://dx.doi.org/10.1152/ajprenal.1996.270.1.f206.
Full textAbstract:
Nitric oxide (NO) reduces blood pressure in vivo by two mechanisms, vasodilation and increasing urinary volume: however, the exact mechanism by which it increases urinary volume is not clear. We hypothesized that NO inhibits antidiuretic hormone (ADH)-stimulated fluid reabsorption (J(r)) by the isolated rat cortical collecting duct (CCD) by decreasing water permeability (Pf) and sodium reabsorption (Jna). In the presence of 10(-11) MADH, Jv was 0.15 +/- 0.04 nl.min-1.mm-1; after 10(-6) M spermine nonoate (SPM) was added to the bath. Jv decreased to 0.06 +/- 0.03 nl.min-1.mm-1 (P < 0.03). To investigate whether the inhibition of Jv was the result of decreased Pf and/or Jna, we first tested the effect of SPM on ADH-stimulated Pf. Basal Pf was stimulated to 289.2 +/- 77.3 microns/s after 10(-11) M ADH was added to the bath (P < 0.01). SPM decreased Pf to 159.8 +/- 45.0 microns/s (P < 0.05). To ensure that this effect on Pf was due to NO release, we used another NO donor, nitroglycerin (NTG). Pf was initially -25.8 +/- 18.3 microns/s and increased to 133.9 +/- 30.5 microns/s after addition of 10(-11) M ADH (P < 0.002). NTG, 20 microM, lowered Pf to 92.4 +/- 18.4 microns/s (P < 0.02). In the presence of 10(-9) M ADH, NTG also decreased Pf(P < 0.04). Next we investigated the effect of SPM on ADH-stimulated JNa. In the presence of ADH, JNa was 37.8 +/- 7.3 pmol.min-1.mm-1. After SPM was added, it dropped to 24.3 +/- 5.1 pmol.min-1.mm-1 (P < 0.05). Time controls exhibited no change in ADH-stimulated Jv, Pf, or Jna. We concluded that 1) NO decreases ADH-stimulated water and sodium transport in the isolate CCD, and 2) water reabsorption is inhibited by a primary effect on Pf. A direct effect of NO on the CCD may explain its natriuretic and diuretic effects observed in vivo.
21
Srinivasan, Mukund, Kamlesh Bhopale, Samir Amer, Jie Wan, Lata Kaphalia, Ghulam Ansari, and Bhupendra Kaphalia. "Linking Dysregulated AMPK Signaling and ER Stress in Ethanol-Induced Liver Injury in Hepatic Alcohol Dehydrogenase Deficient Deer Mice." Biomolecules 9, no. 10 (October 2, 2019): 560. http://dx.doi.org/10.3390/biom9100560.
Full textAbstract:
Ethanol (EtOH) metabolism itself can be a predisposing factor for initiation of alcoholic liver disease (ALD). Therefore, a dose dependent study to evaluate liver injury was conducted in hepatic alcohol dehydrogenase (ADH) deficient (ADH−) and ADH normal (ADH+) deer mice fed 1%, 2% or 3.5% EtOH in the liquid diet daily for 2 months. Blood alcohol concentration (BAC), liver injury marker (alanine amino transferase (ALT)), hepatic lipids and cytochrome P450 2E1 (CYP2E1) activity were measured. Liver histology, endoplasmic reticulum (ER) stress, AMP-activated protein kinase (AMPK) signaling and cell death proteins were evaluated. Significantly increased BAC, plasma ALT, hepatic lipids and steatosis were found only in ADH− deer mice fed 3.5% EtOH. Further, a significant ER stress and increased un-spliced X-box binding protein 1 were evident only in ADH− deer mice fed 3.5% EtOH. Both strains fed 3.5% EtOH showed deactivation of AMPK, but increased acetyl Co-A carboxylase 1 and decreased carnitine palmitoyltransferase 1A favoring lipogenesis were found only in ADH− deer mice fed 3.5% EtOH. Therefore, irrespective of CYP2E1 overexpression; EtOH dose and hepatic ADH deficiency contribute to EtOH-induced steatosis and liver injury, suggesting a linkage between ER stress, dysregulated hepatic lipid metabolism and AMPK signaling.
22
England, B. P., U. Heberlein, and R. Tjian. "Purified Drosophila transcription factor, Adh distal factor-1 (Adf-1), binds to sites in several Drosophila promoters and activates transcription." Journal of Biological Chemistry 265, no. 9 (March 1990): 5086–94. http://dx.doi.org/10.1016/s0021-9258(19)34088-8.
Full text
23
Ellzey, J. T., D. Borunda, and B. P. Stewart. "An Ultrastructural Comparison of Hepatocytes from ADH+ and ADH−Peromyscus Maniculatus." Proceedings, annual meeting, Electron Microscopy Society of America 54 (August 11, 1996): 30–31. http://dx.doi.org/10.1017/s0424820100162612.
Full textAbstract:
Genetically alcohol deficient deer mice (ADHN/ADHN) (obtained from the Peromyscus Genetic Stock Center, Univ. of South Carolina) lack hepatic cytosolic alcohol dehydrogenase. In order to determine if these deer mice would provide a model system for an ultrastructural study of the effects of ethanol on hepatocyte organelles, 75 micrographs of ADH+ adult male deer mice (n=5) were compared with 75 micrographs of ADH− adult male deer mice (n=5). A morphometric analysis of mitochondrial and peroxisomal parameters was undertaken.The livers were perfused with 0.1M HEPES buffer followed by 0.25% glutaraldehyde and 2% sucrose in 0.1M HEPES buffer (4C), removed, weighed and fixed by immersion in 2.5% glutaraldehyde in 0.1M HEPES buffer, pH 7.4, followed by a 3,3’ diaminobenzidine (DAB) incubation, postfixation with 2% OsO4, en bloc staining with 1% uranyl acetate in 0.025M maleate-NaOH buffer, dehydrated, embedded in Poly/Bed 812-BDMA epon resin, sectioned and poststained with uranyl acetate and lead citrate. Photographs were taken on a Zeiss EM-10 transmission electron microscope, scanned with a Howtek personal color scanner, analyzed with OPTIMAS 4.02 software on a Gateway2000 4DX2-66V personal computer and stored in Excel 4.0.
24
Yamaguchi, K., M. Koike, and H. Hama. "Plasma vasopressin response to peripheral administration of angiotensin in conscious rats." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 248, no. 2 (February 1, 1985): R249—R256. http://dx.doi.org/10.1152/ajpregu.1985.248.2.r249.
Full textAbstract:
To assess a role for peripherally administered angiotensin II (ANG II) in regulating vasopressin (antidiuretic hormone, ADH) release, the effects on plasma ANG II and ADH of intraperitoneal injections of ANG II dissolved in various solutions were examined in conscious rats. Plasma ANG II and ADH were determined by radioimmunoassay using the trunk blood collected after decapitation. Injections of 150 mM NaCl containing ANG II (6, 12, or 24 micrograms X 2 ml-1 X 100 g body wt-1) caused dose-related increases in plasma ANG II 15 and 30 min after, but plasma ADH remained unchanged. The lack of effect on plasma ADH of the ANG II dissolved in isotonic saline was also confirmed in another series of experiments in which the solution with a higher ANG II concentration was loaded by much smaller injection volume (14.3 micrograms X 0.1 ml-1 X 100 g-1). However, when given together with 600 mM NaCl, ANG II (8 micrograms X 2 ml-1 X 100 g-1) significantly potentiated the plasma ADH response to the vehicle at 15, 30, and 60 min, without affecting those of plasma osmolality, sodium, and hematocrit. The elevations of plasma ANG II and osmolality brought about by the treatment were comparable with those previously observed in rats deprived of water for 46 h. ANG II was without effect on the plasma ADH responses to the intraperitoneal injections of hypertonic sucrose or mannitol solution that did not alter plasma sodium, although these solutions were equipotent to 600 mM NaCl in augmenting plasma ADH and osmolality.(ABSTRACT TRUNCATED AT 250 WORDS)
25
Nadler, S. P., S. C. Hebert, and B. M. Brenner. "PGE2, forskolin, and cholera toxin interactions in rabbit cortical collecting tubule." American Journal of Physiology-Renal Physiology 250, no. 1 (January 1, 1986): F127—F135. http://dx.doi.org/10.1152/ajprenal.1986.250.1.f127.
Full textAbstract:
To define further the mechanism whereby prostaglandin (PG) E2 inhibits the hydroosmotic response to ADH, we studied the interactions of PGE2 with ADH and two nonhormonal activators of adenylate cyclase, forskolin and cholera toxin, in the isolated perfused rabbit cortical collecting tubule. Forskolin increased hydraulic conductivity (LP) in a dose-dependent fashion and to a degree comparable with ADH-stimulated LP. Forskolin also augmented maximal ADH-stimulated LP, from 135 +/- 15 (SE) to 174 +/- 7 . 10(-7) cm . s-1 . atm-1. Following a 45-min lag phase, 10(-9) M cholera toxin at 37 degrees C increased LP to 107 +/- 12 . 10(-7) cm . s-1 . atm-1, a response that was stable with time. In paired studies at both 25 and 37 degrees C, PGE2 reversibly inhibited ADH-stimulated LP by 45 and 47%, respectively. However, the same protocols with PGE2 and forskolin failed to reveal any inhibitory effect of PGE2 on forskolin-stimulated LP. PGE2 reversibly inhibited cholera toxin-stimulated LP, from 124 +/- 15 to 100 +/- 15 . 10(-7) cm . s-1 . atm-1. These results support the view that PGE2 inhibits ADH-stimulated LP by inhibiting the synthesis of cAMP and suggest that this inhibition occurs at a functional site at or distal to the nucleotide regulatory protein of adenylate cyclase.
26
Laurie, C. C., J. T. Bridgham, and M. Choudhary. "Associations between DNA sequence variation and variation in expression of the Adh gene in natural populations of Drosophila melanogaster." Genetics 129, no. 2 (October 1, 1991): 489–99. http://dx.doi.org/10.1093/genetics/129.2.489.
Full textAbstract:
Abstract A large part of the genetic variation in alcohol dehydrogenase (ADH) activity level in natural populations of Drosophila melanogaster is associated with segregation of an amino acid replacement polymorphism at nucleotide 1490, which generates a difference in electrophoretic mobility. Part of the allozymic difference in activity level is due to a catalytic efficiency difference, which is also caused by the amino acid replacement, and part is due to a difference in the concentration of ADH protein. A previous site-directed in vitro mutagenesis experiment clearly demonstrated that the amino acid replacement has no effect on the concentration of ADH protein, nor does a strongly associated silent polymorphism at nucleotide 1443. Here we analyze associations between polymorphisms within the Adh gene and variation in ADH protein level for a number of chromosomes derived from natural populations. A sequence length polymorphism within the first intron of the distal (adult) transcript, 1, is in strong linkage disequilibrium with the amino acid replacement. Among a sample of 46 isochromosomal lines analyzed, all but one of the 14 Fast lines have 1 and all but one of the 32 Slow lines lack 1. The exceptional Fast line has an unusually low level of ADH protein (typical of Slow lines) and the exceptional Slow line has an unusually high level (typical of Fast lines). These results suggest that the 1 polymorphism may be responsible for the average difference in ADH protein between the allozymic classes. A previous experiment localized the effect on ADH protein to a 2.3-kb restriction fragment. DNA sequences of this fragment from several alleles of each allozymic type indicate that no other polymorphisms within this region are as closely associated with the ADH protein level difference as the 1 polymorphism.
27
Selvarajan, Reena Sri, Ruslinda A. Rahim, Burhanuddin Yeop Majlis, Subash C. B. Gopinath, and Azrul Azlan Hamzah. "Ultrasensitive and Highly Selective Graphene-Based Field-Effect Transistor Biosensor for Anti-Diuretic Hormone Detection." Sensors 20, no. 9 (May 6, 2020): 2642. http://dx.doi.org/10.3390/s20092642.
Full textAbstract:
Nephrogenic diabetes insipidus (NDI), which can be congenital or acquired, results from the failure of the kidney to respond to the anti-diuretic hormone (ADH). This will lead to excessive water loss from the body in the form of urine. The kidney, therefore, has a crucial role in maintaining water balance and it is vital to restore this function in an artificial kidney. Herein, an ultrasensitive and highly selective aptameric graphene-based field-effect transistor (GFET) sensor for ADH detection was developed by directly immobilizing ADH-specific aptamer on a surface-modified suspended graphene channel. This direct immobilization of aptamer on the graphene surface is an attempt to mimic the functionality of collecting tube V 2 receptors in the ADH biosensor. This aptamer was then used as a probe to capture ADH peptide at the sensing area which leads to changes in the concentration of charge carriers in the graphene channel. The biosensor shows a significant increment in the relative change of current ratio from 5.76 to 22.60 with the increase of ADH concentration ranging from 10 ag/mL to 1 pg/mL. The ADH biosensor thus exhibits a sensitivity of 50.00 µA· ( g / mL ) − 1 with a limit of detection as low as 3.55 ag/mL. In specificity analysis, the ADH biosensor demonstrated a higher current value which is 338.64 µA for ADH-spiked in phosphate-buffered saline (PBS) and 557.89 µA for ADH-spiked in human serum in comparison with other biomolecules tested. This experimental evidence shows that the ADH biosensor is ultrasensitive and highly selective towards ADH in PBS buffer and ADH-spiked in human serum.
28
Durr, Jacques A., Johannes Hensen, Tobias Ehnis, and Mary S. Blankenship. "Chlorpropamide upregulates antidiuretic hormone receptors and unmasks constitutive receptor signaling." American Journal of Physiology-Renal Physiology 278, no. 5 (May 1, 2000): F799—F808. http://dx.doi.org/10.1152/ajprenal.2000.278.5.f799.
Full textAbstract:
The mechanism by which chlorpropamide (CP) treatment promotes antidiuresis is unknown. CP competitively inhibited antidiuretic hormone (ADH) binding and adenylyl cyclase (AC) stimulation (inhibition constants K i and K′i of 2.8 mM and 250 μM, respectively) in the LLC-PK1 cell line. CP (333 μM) increased the apparent K a of ADH for AC activation (0.31 vs. 0.08 nM) without affecting a maximal response, suggesting competitive antagonism. Because CP lowers “basal” AC activity and the AC activation-ADH receptor occupancy relationship (A-O plots), it is an ADH inverse agonist. Twenty-four-hour CP exposure (100 μM) upregulated the ADH receptors without affecting affinity. This lowered K a and increased basal AC activity and maximal response (1.86 vs. 1.35 and 14.9 vs. 10.6 fmol cAMP ⋅ min− 1 ⋅ 103cells− 1, n = 6, P < 0.05). NaCl, which potentiates ADH stimulation, also increased basal AC activity. This, together with the CP-ADH inverse agonism and increased basal AC activity at higher receptor density, unmasks constitutive receptor signaling. The CP-ADH inverse agonism explains receptor upregulation and predicts the need for residual ADH with functional isoreceptors for CP-mediated antidiuresis. This could be why CP ameliorates partial central diabetes insipidus but not nephrogenic diabetes insipidus.
29
Ke, Dangyang, Elhadi Yahia, Mila Mateos, and Adel A. Kader. "Ethanolic Fermentation of `Bartlett' Pears as Influenced by Ripening Stage and Atmospheric Composition." Journal of the American Society for Horticultural Science 119, no. 5 (September 1994): 976–82. http://dx.doi.org/10.21273/jashs.119.5.976.
Full textAbstract:
Changes in fermentation volatiles and enzymes were studied in preclimacteric and postclimacteric `Bartlett' pears (Pyrus communis L.) kept in air, 0.25% O2, 20% O2 + 80% CO2, or 0.25% O2 + 80% CO2 at 20C for 1, 2, or 3 days. All three atmospheres resulted in accumulation of acetaldehyde, ethanol, and ethyl acetate. The postclimacteric pears had higher activity of pyruvate decarboxylase (PDC) and higher concentrations of fermentation volatiles than those of the preclimacteric fruit. For the preclimacteric pears, the 0.25% O2 treatment dramatically increased alcohol dehydrogenase (ADH) activity, which was largely due to the enhancement of one ADH isozyme. Exposure to 20% O2 + 80% CO2 slightly increased ADH activity, but the combination of 0.25% O2 + 80% CO2 resulted in lower ADH activity than 0.25% O2 alone. For the postclimacteric pears, the three atmospheres resulted in higher PDC and ADH activities than those of air control fruit. Ethanolic fermentation in `Bartlett' pears could be induced by low O2 and/or high CO2 via 1) increased amounts of PDC and ADH; 2) PDC and ADH activation caused by decreased cytoplasmic pH; or 3) PDC and ADH activation or more rapid fermentation due to increased concentrations of their substrates (pyruvate, acetaldehyde, or NADH).
30
Wang, Linsong, Tingting Zhang, Zhengsong Pan, Lulu Lin, Guoqing Dong, Min Wang, and Ronggui Li. "The alcohol dehydrogenase with a broad range of substrate specificity regulates vitality and reproduction of the plant-parasitic nematodeBursaphelenchus xylophilus." Parasitology 146, no. 4 (October 15, 2018): 497–505. http://dx.doi.org/10.1017/s0031182018001695.
Full textAbstract:
AbstractPine wilt disease, which is caused by the pine wood nematode (PWN),Bursaphelenchus xylophilus, has caused huge damage to pine forests around the world. In this study, we analysed the PWN transcriptome to investigate the expression of genes related to the associated bacterial speciesPseudomonas fluorescensand found that the geneadh-1 encoding alcohol dehydrogenase (ADH) was upregulated. The open reading frame ofadh-1, which encoded a protein of 352 amino acid residues, was cloned fromB. xylophilus. Recombinant ADH with a relative molecular weight of 39 kDa, was present mainly in inclusion bodies and was overexpressed inEscherichia coliBL21 (DE3) and purified after refolding. The biochemical assay revealed that recombinant ADH could catalyse the dehydrogen reaction of eight tested alcohols including ethanol in the presence of NAD+. Quantitative real-time RT-PCR analysis indicated that ethanol upregulatedadh-1 expression in PWN. Results of RNA interference and inhibition of ADH treatment indicated that downregulating expression ofadh-1 or inhibition of ADH could reduce ethanol tolerance and the vitality and reproduction ability ofB. xylophilus, suggesting thatadh-1 is involved in pathogenicity of PWN.
31
Han, Bing, Ye Du, Ton Fu, Zhimin Fan, Shuping Xu, Chengxu Hu, Lirong Bi, Ting Gao, Haipeng Zhang, and Weiqing Xu. "Differences and Relationships Between Normal and Atypical Ductal Hyperplasia, Ductal Carcinoma In Situ, and Invasive Ductal Carcinoma Tissues in the Breast Based on Raman Spectroscopy." Applied Spectroscopy 71, no. 2 (December 20, 2016): 300–307. http://dx.doi.org/10.1177/0003702816681009.
Full textAbstract:
The aim of this study was to find the differences and relationships between normal, atypical ductal hyperplasia (ADH), ductal carcinoma in situ (DCIS), and invasive ductal carcinoma (IDC) lesions of the breast based on biochemical characteristics determined by Raman spectroscopy (RS). After collecting 39 frozen sections from patients who underwent surgical resection or mammotome biopsy, nine normal tissues, seven ADH, eight DCIS, and 15 IDC lesions were detected using confocal RS. We then used leave-one-out cross-validation (LOOCV) and radial basis function (RBF) to build a support vector machine (SVM) diagnosis model. Pronounced mean Raman spectra differences were observed between normal tissues, ADH, DCIS, and IDC tissues. Most noticeable was the increased protein and reduced lipid levels of ADH tissues compared to normal tissues. The major spectra differences in ADH, DCIS, and IDC spectrograms were evidenced by a red shift with a broad peak of CH2 (1301 cm−1), the intensity of the stretching vibration peak of carotenoids (1526 cm−1), a relatively strong band of amide-I (1656 cm−1), and the nuclear (882 cm−1) acid peak. Atypical ductal hyperplasia tissues had the largest constituent variations between subjects. During the disease progression, IDC tissues have smaller inter-subject constituent variations than DCIS and ADH tissues. The overall accuracy of SVM model is 74.39%. The sensitivities of normal tissue, ADH, DCIS, and IDC are 62.5%, 50%, 90%, and 66.7%, respectively. The specificities of normal tissue, ADH, DCIS, and IDC are 100%, 100%, 66.7%, and 89.06%, respectively. Atypical ductal hyperplasia shows significant differences and the relationship between normal tissue and malignant disease. Further study to explain the biochemical relationships between these differences will shed more light into a better understanding of the mechanism by which ADH converts to DCIS and to IDC.
32
Eslami, Mahboobeh, Navid Nezafat, Sahar Khajeh, Zohreh Mostafavi-Pour, Samaneh Bagheri Novir, Manica Negahdaripour, Younes Ghasemi, and Vahid Razban. "Deep analysis of N-cadherin/ADH-1 interaction: a computational survey." Journal of Biomolecular Structure and Dynamics 37, no. 1 (January 19, 2018): 210–28. http://dx.doi.org/10.1080/07391102.2018.1424035.
Full text
33
Quintanilla, María Elena, Lutske Tampier, Amalia Sapag, Ziomara Gerdtzen, and Yedy Israel. "Sex differences, alcohol dehydrogenase, acetaldehyde burst, and aversion to ethanol in the rat: a systems perspective." American Journal of Physiology-Endocrinology and Metabolism 293, no. 2 (August 2007): E531—E537. http://dx.doi.org/10.1152/ajpendo.00187.2007.
Full textAbstract:
Individuals who carry the most active alcohol dehydrogenase (ADH) isoforms are protected against alcoholism. This work addresses the mechanism by which a high ADH activity leads to low ethanol intake in animals. Male and female ethanol drinker rats (UChB) were allowed access to 10% ethanol for 1 h. Females showed 70% higher hepatic ADH activity and displayed 60% lower voluntary ethanol intake than males. Following ethanol administration (1 g/kg ip), females generated a transient blood acetaldehyde increase (“burst”) with levels that were 2.5-fold greater than in males ( P < 0.02). Castration of males led to 1) an increased ADH activity (+50%, P < 0.001), 2) the appearance of an acetaldehyde burst (3- to 4-fold vs. sham), and 3) a reduction of voluntary ethanol intake comparable with that of naïve females. The ADH inhibitor 4-methylpyrazole blocked the appearance of arterial acetaldehyde and increased ethanol intake. Since the release of NADH from the ADH·NADH complex constitutes the rate-limiting step of ADH (but not of ALDH2) activity, endogenous NADH oxidizing substrates present at the time of ethanol intake may contribute to the acetaldehyde burst. Sodium pyruvate given at the time of ethanol administration led to an abrupt acetaldehyde burst and a greatly reduced voluntary ethanol intake. Overall, a transient surge of arterial acetaldehyde occurs upon ethanol administration due to 1) high ADH levels and 2) available metabolites that can oxidize hepatic NADH. The acetaldehyde burst is strongly associated with a marked reduction in ethanol intake.
34
Lu, Yuan, Jinmei Wang, Haobo Xu, Chuyue Zhang, Pengpeng Cheng, Lihua Du, Lan Tang, Jinghua Li, and Zhimin Ou. "Efficient Synthesis of Key Chiral Intermediate in Painkillers (R)-1-[3,5-Bis(trifluoromethyl)phenyl]ethanamine by Bienzyme Cascade System with R-ω-Transaminase and Alcohol Dehydrogenase Functions." Molecules 27, no. 21 (October 28, 2022): 7331. http://dx.doi.org/10.3390/molecules27217331.
Full textAbstract:
(R)-1-[3,5-bis(trifluoromethyl)phenyl]ethanamine, a key chiral intermediate of selective tetrodotoxin-sensitive blockers, was efficiently synthesized by a bienzyme cascade system formed by with R-ω-transaminase (ATA117) and an alcohol dehydrogenase (ADH) co-expression system. Herein, we report that the use of ATA117 as the biocatalyst for the amination of 3,5-bistrifluoromethylacetophenone led to the highest efficiency in product performance (enantiomeric excess > 99.9%). Moreover, to further improve the product yield, ADH was introduced into the reaction system to promote an equilibrium shift. Additionally, bienzyme cascade system was constructed by five different expression systems, including two tandem expression recombinant plasmids (pETDuet-ATA117-ADH and pACYCDuet-ATA117-ADH) and three co-expressed dual-plasmids (pETDuet-ATA117/pET28a-ADH, pACYCDuet-ATA117/pET28a-ADH, and pACYCDuet-ATA117/pETDuet-ADH), utilizing recombinant engineered bacteria. Subsequent studies revealed that as compared with ATA117 single enzyme, the substrate handling capacity of BL21(DE3)/pETDuet-ATA117-ADH (0.25 g wet weight) developed for bienzyme cascade system was increased by 1.50 folds under the condition of 40 °C, 180 rpm, 0.1 M pH9 Tris-HCl for 24 h. To the best of our knowledge, ours is the first report demonstrating the production of (R)-1-[3,5-bis(trifluoromethyl)phenyl]ethanamine using a bienzyme cascade system, thus providing valuable insights into the biosynthesis of chiral amines.
35
Laurie, C. C., and L. F. Stam. "The effect of an intronic polymorphism on alcohol dehydrogenase expression in Drosophila melanogaster." Genetics 138, no. 2 (October 1, 1994): 379–85. http://dx.doi.org/10.1093/genetics/138.2.379.
Full textAbstract:
Abstract Several lines of evidence indicate that natural selection controls the frequencies of an allozyme polymorphism at the alcohol dehydrogenase (Adh) locus in Drosophila melanogaster. However, because of associations among sequence polymorphisms in the Adh region, it is not clear whether selection acts directly (or solely) on the allozymic site. This problem has been approached by using in vitro mutagenesis to distinguish among the effects on Adh expression of individual polymorphisms. This study shows that a polymorphism within the first Adh intron (delta 1) has a significant effect on the level of ADH protein. Like the allozyme, delta 1 shows a geographic cline in frequency, indicating that it may also be a target of natural selection. These results suggest that multisite selection models may be required to understand the evolutionary dynamics of individual loci.
36
Berim, Lyudmyla Derby, Beth M. Kos, Ruby Evande, Jane L. Meza, Valerie Shostrom, James K. Schwarz, and Jean L. Grem. "A phase I study of ADH-1 with cisplatin (Cisp) and gemcitabine (Gem) in patients (Pts) with unresectable or metastatic pancreatic and biliary tract cancers." Journal of Clinical Oncology 35, no. 4_suppl (February 1, 2017): 306. http://dx.doi.org/10.1200/jco.2017.35.4_suppl.306.
Full textAbstract:
306 Background: Pancreatic cancer cells in vitro undergo epithelial to mesenchymal transformation (EMT) by up-regulating mesenchymal markers, including N-cadherin. The EMT leads to increased motility & invasiveness with collagen exposure in a pancreatic cancer mouse model, which can be inhibited by N-cadherin knockdown. ADH-1 is a small, cyclic pentapeptide with inhibitory effects on stromal & endothelial cells expressing N-cadherin. Methods: Escalating doses of ADH-1 were given twice weekly for 3 wk (1,000, 2,000 & 4,000 mg) with Cisp 25 mg/m2 & Gem1000 mg/m2/100 min days 1 & 8 of a 3 wk cycle in pts with pancreaticobiliary cancers with ECOG PS 0-2 & adequate bone marrow, renal & hepatic function. Standard 3 + 3 dose escalation was used. Peripheral blood was collected for biomarkers prior to each dose of ADH-1 during cycle 1. Due to limited drug supply, ADH-1 was given for the 1st 3 cycles. Results: Between 05/2013 - 04/2015, 17 pts were enrolled, received at least 1 dose of therapy, and were evaluable for toxicity: m 13/F 4; median 60 yr (range 37-81); pancreas 9 /biliary 8. 3 pts had prior adjuvant therapy. The number pts with dose-limiting toxicity during cycle 1 of ADH-1 (mg) were 0/4 at 1,000; 1/7 at 2,000 (gr 4 ANC, platelet); 2/6 pts 4,000 mg (1 pt: gr 3 pulmonary embolus and gr 4 plt; 1: gr 4 cholangitis/sepsis/multiorgan failure). 5 of 8 pts who had ≥ 6 cycles were taken off study due to cumulative toxicities rather than PD. 14 pts had ≥ 3 cycles of therapy and were evaluable for response: SD in 9 subjects; PD in 5. The median number cycles was 5.5 (range 1-30). Median time to treatment failure (TTF) for all patients was 113 days (range 7-724). Median OS was 218 days (7-853+). Pts with biliary cancer had a longer TTF and OS vs pancreatic cancer (TTF 217 vs 93 days; OS 305 vs 180 days). 6 pts survived > 12 months (biliary 4, pancreas 2). Biomarker analysis (ICAM 1; E selectin; VEGF, Soluble VEGF-R 2 and 3, FGF basic) is ongoing. Conclusions: The phase II dose of ADH1 given with Cisp/Gem is 2,000 mg IV twice weekly. ADH-1 was relatively well tolerated. Most pts ultimately required dose delays or reductions due to cumulative toxicity with Cisp/Gem. Clinical trial information: NCT01825603.
37
Berry, A., and M. Kreitman. "Molecular analysis of an allozyme cline: alcohol dehydrogenase in Drosophila melanogaster on the east coast of North America." Genetics 134, no. 3 (July 1, 1993): 869–93. http://dx.doi.org/10.1093/genetics/134.3.869.
Full textAbstract:
Abstract Clines may either be selectively maintained or be the by-product of nonadaptive processes related to population structure and history. Drosophila melanogaster populations on the east coast of North America show a latitudinal cline in the frequencies of two common electrophoretically distinguishable alleles at the alcohol dehydrogenase locus (Adh), designated Adh-S and Adh-F. This cline may either be adaptive or an artifact of a possible recent dual founding of North American D. melanogaster populations in which frequencies of Adh alleles differed between founder populations. By means of a high resolution restriction-mapping technique, we studied the distribution of 113 haplotypes derived from 44 polymorphic DNA markers within the Adh region in 1533 individuals from 25 populations throughout the cline. We found significant clinal differentiation at the polymorphism determining the mobility-difference causing amino acid replacement between Adh-F and Adh-S alleles. Hitchhiking was limited, despite extensive linkage disequilibrium, and other sites did not vary clinally. Such a pattern of differentiation implies that selection is responsible for the cline. To investigate whether selection acts only on the Adh-F/S site, we performed a "selective equivalence" test under the assumption that all variability within the specified allelic class is selectively neutral. This revealed selective equivalence among Adh-S-bearing haplotypes, whose frequencies showed no differentiation throughout the cline, implying high levels of frequency-homogenizing gene flow. Geographical heterogeneity among Adh-F-bearing haplotypes implied the action of selection on one or more additional variants in linkage disequilibrium with Adh-F. In a further study of a subset of the data (n = 1076 from 18 populations), we found a combined insertion/deletion polymorphism, designated delta 1, located in the 5' adult intron and in linkage disequilibrium with Adh-F, to show more marked clinal variation than Adh-F/S. Although the unequivocal identification of the precise target(s) of selection requires further study, we suggest that clinal selection may be acting epistatically on the Adh-F/S and delta 1 polymorphisms.
38
Sessa, C., A. Perotti, M. Maur, A. Fasolo, D. Scaramuzza, A. Braghetti, S. Marsoni, R. K. Malik, W. P. Peters, and L. Gianni. "An enriched phase I, pharmacokinetic and pharmacodynamic study of the N-cadherin (NCAD) cyclic competitive binder exherin (ADH-1) in patients with solid tumors." Journal of Clinical Oncology 24, no. 18_suppl (June 20, 2006): 3042. http://dx.doi.org/10.1200/jco.2006.24.18_suppl.3042.
Full textAbstract:
3042 Background: N-cad is a cell adhesion molecule expressed by vascular endothelium and tumor cells of invasive tumors. ADH-1, a cyclic pentapeptide, antagonizes N-cad, causing rapid tumor vascular disruption and apoptosis in preclinical models. We report results from a Phase I study of weekly doses of intravenous ADH-1 given to patients with N-cad+ solid tumors, to evaluate safety, PK, antitumor activity, and effect of ADH-1 on tumor vasculature assessed by DCE-MRI. Methods: ADH-1 starting dose was 150 mg/m2 administered weekly for 3 W in 28 D cycles. DCE-MRI was performed to assess changes in tumor perfusion 90 mins after the first dose of ADH-1, and repeated on D 15 if no changes were noted. Following the 3rd dose level (DL 3, 600 mg/m2 ), the schedule was amended to weekly ADH-1 without interruption, in 21 D cycles. Results: 55 pts with refractory solid tumors were screened, 56% were N-cad+ [screened/N-cad+: GYN 16/21 (Ovarian 13/17), GI 5/14, breast 2/6, renal 5/5, head & neck 2/3, others 2/6]. 13 pts (5 males, median age 53 yrs.) received 20 cycles of ADH-1 by bolus injection at 150, 300 and 600 mg/m2/weekly ×3 W Q21–28 D. No DLTs have occurred to date. No pts have experienced > grade 2 study drug related AEs. One pt, with fallopian tube ca. had a mixed response. There was a 30% reduction in retroperitoneal nodal disease at the end of cycle 3, and a 37% reduction at the end of Cy 4. However, new bone lesions were also noted at the end of cycle 4 assessment. Tumor blood flow reduction of ≥40% was noted in this patient, and she also reported pain in the region of the tumor following multiple doses of ADH-1. PK parameters are available for the first 3 DLs (150, 300, and 600 mg/m2): mean Cmax 22.1, 37.0, and 50.8μg/mL, respectively; AUCinf 24.3, 60.6, and 110.3 h·μg/mL; Vss 12.6, 15.1, and 16.3 L/m2; and T1/2 1.8, 2.7, and 2.4hr. Conclusions: ADH-1 has been well tolerated in 4 dose levels tested to date, dose escalation is proceeding. No DLTs have occurred and the MTD has not been reached. Anti-tumor activity has been noted. Updated clinical, PK and PD results will be presented. [Table: see text]
39
Zorzano, Antonio, Luis Ruiz del Arbol, and Emilio Herrera. "Effect of liver disorders on ethanol elimination and alcohol and aldehyde dehydrogenase activities in liver and erythrocytes." Clinical Science 76, no. 1 (January 1, 1989): 51–57. http://dx.doi.org/10.1042/cs0760051.
Full textAbstract:
1. Liver biopsies were performed in healthy control subjects and in subjects with alcoholic and non-alcoholic liver disease in order to examine alcohol dehydrogenase (ADH; EC 1.1.1.1) and aldehyde dehydrogenase [ALDH; aldehyde dehydrogenase (NAD+); EC 1. 2. 1. 3] activities. Erythrocyte ALDH and ethanol metabolism were also investigated in the same subjects. 2. Fifteen per cent of the subjects studied (seven of 48 subjects tested) presented atypical ADH activity, characterized by elevated activity at pH 7.4 or 8.8 compared with that found in subjects with the usual ADH form. However, the ethanol elimination curves obtained in two subjects with atypical ADH were indistinguishable from the kinetics of the group with normal ADH. Subjects displaying atypical ADH activity showed normal liver and erythrocyte ALDH activities. 3. Considering only the subjects with the normal ADH form, hepatic ADH activity was unaltered in subjects with non-alcoholic liver disease (chronic hepatitis or cirrhosis) and in those with alcoholic steatosis. Subjects with alcoholic hepatitis or alcoholic cirrhosis showed a lower ADH activity compared with the healthy control group. 4. In spite of the changes detected in subjects with alcoholic liver disease, curves of blood ethanol concentration after oral administration of 0.4 g of ethanol/kg were indistinguishable between the alcoholic hepatitis group and the control group. 5. Hepatic ALDH activity, assayed at 300 μmol/l acetaldehyde, was found to be diminished in all liver pathologies investigated, regardless of their aetiology. Nevertheless, erythrocyte ALDH activity was not modified in subjects with non-alcoholic or alcoholic liver disease. As a result of these findings, no relationship was found between hepatic and erythrocyte ALDH. 6. In summary, our data demonstrate that (a) marked modifications in ADH activity, as found in patients with atypical ADH or in subjects with alcoholic liver disease, are not accompanied by parallel alterations in the kinetics of ethanol disappearance, suggesting that ADH activity per se does not limit ethanol metabolism in vivo, (b) hepatic high-Km ALDH activity is decreased in patients with liver disease independent of alcoholism, and therefore decreased ALDH activity cannot be considered as a primary defect in alcoholism but as a consequence of liver damage, and (c) erythrocyte ALDH does not reflect hepatic high-Km ALDH.
40
Chervin, Christian, Janyce K. Truett, and Jim Speirs. "Alcohol Dehydrogenase Expression and Alcohol Production during Pear Ripening." Journal of the American Society for Horticultural Science 124, no. 1 (January 1999): 71–75. http://dx.doi.org/10.21273/jashs.124.1.71.
Full textAbstract:
Regulation of alcohol dehydrogenase (ADH), activity of pyruvate decarboxylase (PDC) and accumulation of acetaldehyde and ethanol in `Packham's Triumph' pears (Pyrus communis, L.) subsequent to different storage regimes were investigated. Pears were stored for two months at -1 °C either in air (Air) or under hypoxia at 3 kPa O2 (Hyp) and subsequently warmed and allowed to ripen in air at 20 °C. One set of fruit stored in air at -1 °C was subjected to 3 days of hypoxia at -1 °C (Air+Hyp) before ripening in air. Acetaldehyde, ethanol and methanol levels increased in all fruit in a similar fashion during ripening and did not reflect differences in storage treatments. During ripening, ADH activities in posthypoxic samples were generally twice that of air samples. PDC activities increased for ≈6 days during ripening then declined slightly but did not differ significantly among treatments. Upon transfer to 20 °C in air, slightly higher levels of Adh mRNA were observed in samples treated with hypoxia than in air controls. Over the following 2 days at 20 °C, the Adh transcription was markedly induced in Air and Air+Hyp samples. Although all Adh mRNAs returned to control levels within 4 days, ADH activities remained higher in hypoxia-treated fruit than in controls for up to 18 days. These results suggest that, in ripening pears, ADH does not limit ethanol production, and that the expression of this enzyme comprises post-transcriptional regulations. GenBank accession numbers of the Adh cDNAs are AFO 31899 and AFO 31900.
41
Stiborová, Marie, and Sylva Leblová. "Mechanism of action of heavy metals, S-triazine herbicides and nitrates on alcohol dehydrogenase from rape." Collection of Czechoslovak Chemical Communications 51, no. 8 (1986): 1781–88. http://dx.doi.org/10.1135/cccc19861781.
Full textAbstract:
Heavy metals (Pb2+, Cu2+, Cd2+, and Zn2+) inhibited alcohol dehydrogenase (ADH) of rape (EC 1.1.1.1.); Pb2+ and Cd2+ ions affected the imidazole ring of histidine, Cu2+ and Zn2+ ions interacted with the sulphydryl groups of cysteine in the molecule of the enzyme. The coenzyme protected ADH from inactivation by Pb2+ and Cd2+, but did not protect it from Cu2+ and Zn2+. Ethanol in a ternary complex ADH-NAD+ -ethanol was a strong protecting agent from Pb2+ and Cd2+ ions. Nitrates inhibited rape ADH toward any substrate. Sulphates and fluorides had no effect. The S-triazine herbicides studied proved strong inhibitors of rape ADH (their Ki's corresponded to concentrations of the order 10-4 mol 1-1), occupying the binding site for the coenzyme. The herbicides interacted with the metallic component of the enzyme, to which the nicotinamide part of the coenzyme is bound.
42
Ye, Qianni, Zhenfeng Liu, Shuyi Zhang, Guolin Wang, Guanghua Wen, and Mengjie Dong. "Development of 99mTc-Hynic-Adh-1 Molecular Probe Specifically Targeting N-Cadherin and Its Preliminary Experimental Study in Monitoring Drug Resistance of Non-Small-Cell Lung Cancer." Cancers 15, no. 3 (January 26, 2023): 755. http://dx.doi.org/10.3390/cancers15030755.
Full textAbstract:
Background: N-cadherin is considered a characteristic protein of EMT and has been found to be closely related to tumor resistance. In this study, a novel molecular imaging probe, 99mTc-HYNIC-ADH-1, was developed, and its diagnostic value in monitoring drug resistance in NSCLC was preliminarily investigated. Methods: ADH-1 was labeled indirectly with 99mTc. Radiochemical purity and stability, partition coefficients and pharmacokinetics were evaluated. Additionally, the fluorescent probe of ADH-1 was synthesized to study tumor uptake in cells level and in vivo. Biodistribution analysis and small animal SPECT/CT were performed in PC9GR and PC9 tumor-bearing mice. Results: 99mTc-HYNIC-ADH-1 was highly stable (radiochemical purity ≥ 98% in PBS and serum after 24 h). A cell binding study and fluorescence imaging showed that the uptake was significantly higher in PC9GR cells (gefitinib-resistant) than in PC9 cells (nonresistant) (p < 0.05). Biodistribution analysis showed rapid blood clearance and significant uptake in the kidney and resistant tumor. Small animal SPECT/CT studies showed that uptake in PC9GR tumors (T/NT = 7.73 ± 0.54) was significantly higher than that in PC9 tumors (T/NT = 3.66 ± 0.78) at 1 h (p = 0.002). Conclusions: The 99mTc-HYNIC-ADH-1 molecular probe has a short synthesis time, high labeling rate, high radiochemical purity and good stability, does not require purification, is characterized by rapid blood clearance and is mainly excreted through the urinary system. 99mTc-HYNIC-ADH-1 is considered a promising probe for monitoring drug resistance in NSCLC.
43
Mitchell, William C., and Gojko Jelenkovic. "NAD-DEPENDENT AND NADP-DEPENDENT ALCOHOL DEHYDROGENASE ENZYMES: ANALYSIS OF THEIR FUNCTIONAL SIGNIFICANCE IN STRAWBERRY FRUITS." HortScience 27, no. 6 (June 1992): 654c—654. http://dx.doi.org/10.21273/hortsci.27.6.654c.
Full textAbstract:
Assays of enzyme activity, in vivo inhibition studies and the developmental analysis of strawberry (Fragaria × ananassa Duch.) fruit alcohol dehydrogenases (ADH) suggest that both the NAD-(E.C. 1.1.1.1) and the NADP-dependent (E.C. 1.1.1.2) forms of ADH enzymes play integral roles in the development and ripening of fruits. One role of ADH enzymes appears to be the evocation of changes in sugar, soluble solids, acidity and volatile compounds necessary for the normal organoleptic character of strawberry fruits. The data presented includes: 1.) The wide substrate specificity of both ADH enzymes for the “fragrance and flavor alcohols and aldehydes” synthesized by ripe strawberry fruits, 2.) the effect of inhibitors of ADH activity upon strawberry fruit ripening, and 3.) the comparative regulation of NAD- and NADP-ADH enzymes including 4.) the developmental control of ADH enzymes in strawberry fruits.
44
BURDETTE, Douglas S., Francesco SECUNDO, Robert S. PHILLIPS, Jun DONG, Robert A. SCOTT, and J. Gregory ZEIKUS. "Biophysical and mutagenic analysis of Thermoanaerobacter ethanolicus secondary-alcohol dehydrogenase activity and specificity." Biochemical Journal 326, no. 3 (September 15, 1997): 717–24. http://dx.doi.org/10.1042/bj3260717.
Full textAbstract:
The Thermoanaerobacter ethanolicus 39E adhB gene encoding the secondary-alcohol dehydrogenase (2° ADH) was overexpressed in Escherichia coli at more than 10% of total protein. The recombinant enzyme was purified in high yield (67%) by heat-treatment at 85 °C and (NH4)2SO4 precipitation. Site-directed mutants (C37S, H59N, D150N, D150E and D150C were analysed to test the peptide sequence comparison-based predictions of amino acids responsible for putative catalytic Zn binding. X-ray absorption spectroscopy confirmed the presence of a protein-bound Zn atom with ZnS1(imid)1(N,O)3 co-ordination sphere. Inductively coupled plasma atomic emission spectrometry measured 0.48 Zn atoms per wild-type 2° ADH subunit. The C37S, H59N and D150N mutant enzymes bound only 0.11, 0.13 and 0.33 Zn per subunit respectively, suggesting that these residues are involved in Zn liganding. The D150E and D150C mutants retained 0.47 and 1.2 Zn atoms per subunit, indicating that an anionic side-chain moiety at this position preserves the bound Zn. All five mutant enzymes had ⩽ 3% of wild-type catalytic activity, suggesting that the T. ethanolicus 2° ADH requires a properly co-ordinated catalytic Zn atom. The His-59 and Asp-150 mutations also altered 2° ADH affinity for propan-2-ol over a 140-fold range, whereas the overall change in affinity for ethanol spanned a range of only 7-fold, supporting the importance of the metal in 2° ADH substrate binding. The lack of significant changes in cofactor affinity as a result of these catalytic Zn ligand mutations suggested that 2° ADH substrate-and cofactor-binding sites are structurally distinct. Altering Gly198 to Asp reduced the enzyme specific activity 2.7-fold, increased the Km(app) for NADP+ 225-fold, and decreased the Km(app) for NAD+ 3-fold, supporting the prediction that the enzyme binds nicotinamide cofactor in a Rossmann fold. Our data indicate therefore that, unlike the liver 1° ADH, the Rossmann-fold-containing T. ethanolicus 2° ADH binds its catalytic Zn atom using a sorbitol dehydrogenase-like Cys-His-Asp motif and does not bind a structural Zn atom.
45
Na'iem, Mohammad, Yoshihiko Tsumura, Kohji Uchida, Toru Nakamura, and Kihachiro Ohba. "Linkage of allozyme loci in Japanese red pine (Pinusdensiflora)." Canadian Journal of Forest Research 23, no. 4 (April 1, 1993): 680–87. http://dx.doi.org/10.1139/x93-089.
Full textAbstract:
Linkage relationships among 29 polymorphic loci were investigated in Japanese red pine, Pinusdensiflora Sieb. et Zucc. Haploid megagametophytes from 12 highly heterozygous plus-tree clones were used. A total of 217 pairs of two-locus combinations were available for the linkage study. Chi-square and Akaike Information Criterion analyses identified 19 pairs of linkages. Close linkages (r = 0–0.10) were seen for Est-2, 3–Aap-2, 3, Dia-1–Acp, and Shd-1–Got-1. Strong linkages (r = 0.10–0.20) were seen for Est-2, 3–Dia-1, Est-2, 3–Acp, Aap-2, 3–Dia-1, Got-2–Lap-1, and Pgm–Aap-1. Moderate linkages (r = 0.20–0.30) were seen for Adh–Sod, Adh–Pgi-1, 2, Adh–Lap-1, G2d–G6p, and Dia-2–Amy pair of linkages. The remaining six pair combinations, namely 6Pg-1–Est-2, 3, 6Pg-1–Acp, Est-1–Acp, Est-2, 3–Shd-1, Sod–Pgi-1, 2, and Adh–Got-2 were weakly linked (r = 0.30–0.40). In all, 22 loci were classified into five linkage groups by means of three-point mapping methods.
46
Samokhina, L. M., and V. V. Lomako. "EFFICIENCY OF RHYTHMIC COLD EXPOSURES ON THE ACTIVITY OF PROTEINASES AND THEIR INHIBITORS IN RATS WITH ALCOHOL-DEPENDENT HYPERTENSION." Fiziolohichnyĭ zhurnal 68, no. 1 (January 18, 2022): 34–44. http://dx.doi.org/10.15407/fz68.01.034.
Full textAbstract:
The aim of the work is to study the efficiency of rhythmic cold exposures (RCEs; 5 ± 1°C, frequency 0.1 Hz, 65 min) on the activities of proteinases, nontrypsin-like proteinases (NTLP), tripsininhibitory activity (TIA) α-1-proteinase inhibitor (α-1-PI) and α-2-macroglobulin (α-2-MG) in blood serum, tissues of the brain and internal organs in male rats with alcohol-dependent hypertension (ADH) by highly sensitive (10-9 – 10-10 g) enzymatic methods. ADH was modelled by chronic (for 10 months) alcoholization of rats by the «two-bottle» method. It was noted that ADH decreases the proteinases activity in tissues, maximally in the lungs, kidneys and heart (by 6, 7 and 10 times, respectively). RCEs promotes the proteinases activation, it is most pronounced in blood serum, kidneys and liver (20, 8 and 5 times, respectively), in intact rats – in the lungs (5 times). ADH decrease the NTLP activity in the liver by 10 times and less in the kidneys, which may be due to a violation of protein biosynthesis, and in the blood serum and brain tissues it increases, in the cerebral cortex by 10 times. RCEs promotes the NTLP activation, at ADH by 2-4 times, in the intact rats by 10 or more times. The ADH decreased the α-2-MG activity, it is most pronounced in the hypothalamus, lungs, kidneys by 100 times and less in the heart. RCEs promotes the α-2-MG activation: at ADH below the control level, in the intact rats – in the brain tissues and kidneys, which may be due to the participation of syn- and catatoxical adaptive mechanisms. The α-1-PI activity decreases at ADH and the background of RCEs, which is associated with a shift in the balance in the proteinase-proteinase inhibitor system. Thus, RCEs lead to reverse changes caused by ADH in rats, promote activation of proteinases, NTLP, α-2-MG, which is associated with the functioning of regulatory systems of the body, the development of hormesis, the formation of high resistance to external and internal stressors, expanding adaptive capabilities. At the same time, low TIA α-1-IP promotes activation of proteinases, NTLP.
47
Chen, Wei J., E. W. Loh, Yun-Pung P. Hsu, Chiao-Chicy Chen, Jeng-Ming Yu, and Andrew T. A. Cheng. "Alcohol-Metabolising Genes and Alcoholism Among Taiwanese Han Men: Independent Effect of ADH2, ADH3 and ALDH2." British Journal of Psychiatry 168, no. 6 (June 1996): 762–67. http://dx.doi.org/10.1192/bjp.168.6.762.
Full textAbstract:
BackgroundPrevious population association studies have indicated that certain alleles of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) may reduce the risk of alcoholism in Asian populations. The association of ALDH2 and ADH2 with the development of alcoholism was found to be independent of each other and has been replicated in different Asian populations, while the effect of ADH3 is less studied.MethodWe genotyped the alcohol metabolism genes among Han men with alcohol dependence (n=46) and their ethnically matched normal controls (n=63) in Taiwan. Multiple logistic regression was then applied to assess the contribution of ADH3 to alcoholism by controlling the effect of ALDH2 and ADH2.ResultsThe results of multivariate analyses demonstrated that the odds ratios for an increment of one allele of ADH2∗1, ADH3∗2 and ALDH2∗1 in the development of alcoholism were 4.18, 3.82, and 6.89, respectively.ConclusionsThese findings clearly indicate that all three alcohol-metabolising genes contribute to susceptibility to alcoholism.
48
Chrostek, L., D. Szczepura, M. Szmitkowski, W. Jelski, and J. Wierzchowski. "Alcohol and aldehyde dehydrogenase activity in the stomach and small intestine of rats poisoned with methanol." Human & Experimental Toxicology 20, no. 5 (May 2001): 255–58. http://dx.doi.org/10.1191/096032701678227703.
Full textAbstract:
The activities of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) were measured with fluorogenic naphthaldehydes in the stomach and small intestine homogenates of rats dosed with 6 g methanol/kg bw after 6, 12, 24 h and 2, 5, 7 days. After intoxication with a sublethal dose, the ADH activity measured with these naphthaldehydes andALDH activities in the stomach and small intestine were significantly decreased. This inhibition is stronger in the stomach and probably depends on cell damage and protein denaturation. We conclude that the activity measured with 6-methoxy-2-naphthaldehyde (MONAL-62) may be due to the activity of rat ADH-1 isoenzyme, and the activity detected with 4-methoxy-1-naphthaldehyde (MONAL-41) to the activity of rat ADH-2 isoenzyme.
49
Liu, Liangliang, Miao Chen, and Xiaoqing Chen. "Analysis of alcohol dehydrogenase inhibitors from Desmodium styracifolium using centrifugal ultrafiltration coupled with HPLC-MS." Journal of the Serbian Chemical Society 80, no. 8 (2015): 1051–59. http://dx.doi.org/10.2298/jsc140919023l.
Full textAbstract:
Alcohol dehydrogenase (ADH) inhibitors play an important role in the treatment of human methanol or ethylene glycol poisoning and the suppression of acetaldehyde accumulation in alcoholics. In this study, centrifugal ultrafiltration coupled with high performance liquid chromatography-mass spectrometry (HPLC-MS) was utilized to screen and identify ADH inhibitors from ethyl acetate extract of Desmosium styracifolium (Osb.) Merr. The experiment conditions of centrifugal ultrafiltration were optimized. At the optimum conditions (ADH concentration: 37.5 ?g mL-1, incubation time: 90 min, pH: 7.0 and temperature: 15?C), formononetin and aromadendrin were successfully screened and identified from ethyl acetate extract of Desmodium styracifolium. The screening result was verified by ADH inhibition assays. The IC50 values of formononetin and aromadendrin were 70.8 and 84.7 ?g mL-1, which were accorded with the binding degrees of them. Aromadendrin was first reported to have inhibitory activity on ADH. This method provided an effective way to screen active compounds from natural products.
50
Schuster, V. L. "Mechanism of bradykinin, ADH, and cAMP interaction in rabbit cortical collecting duct." American Journal of Physiology-Renal Physiology 249, no. 5 (November 1, 1985): F645—F653. http://dx.doi.org/10.1152/ajprenal.1985.249.5.f645.
Full textAbstract:
Vasopressin (ADH) and bradykinin (BK) have been shown to stimulate prostaglandin synthesis in rabbit cortical collecting tubules. We studied ADH and BK effects on osmotic water flow (Lp), Na transport (JNa), and transepithelial voltage (VT). Bath BK but not lumen BK blunted subsequent ADH hydroosmotic responses. This BK effect was prevented by ibuprofen or pertussigen pretreatment and was overcome with exogenous cAMP, suggesting that BK, via prostaglandins, interferes with ADH action on Lp at the cAMP generation step. In contrast, bath BK had no effect on bath-to-lumen (Jb-1Na) or lumen-to-bath (Jl-bNa) Na flux or on VT. As reported by others, ADH lowered Jl-bNa and depolarized VT; however, prostaglandin synthesis inhibitors neither prevented nor reversed these ADH effects. Together, these BK and ADH data do not support regulation of JNa by peptide-stimulated prostaglandins. Moreover, cAMP alone depolarized VT but had no effect on Jl-bNa. Therefore, ADH-induced depolarization of VT may at least partly owe to cAMP effects on VT independent of accompanying changes in JNa. As with Lp, bath BK blunted subsequent ADH effects on VT and, to a lesser extent, Jl-bNa; these BK effects on ADH action were also prevented by ibuprofen or pertussigen pretreatment. The data are consistent with the following model: 1) ADH depolarizes VT and increases Lp via cAMP; 2) ADH decreases JNa via neither cAMP nor prostaglandins; and 3) BK, via prostaglandins, inhibits the actions of ADH on Lp and VT at the inhibitory guanyl-nucleotide regulatory subunit of adenylate cyclase.