scholarly journals Deficiency in alcohol dehydrogenase 2 reduces arsenic in rice grains by suppressing silicate transporters

2021 ◽  
Author(s):  
Shimpei Hayashi ◽  
Masato Kuramata ◽  
Tadashi Abe ◽  
Noriko Yamaguchi ◽  
Hiroki Takagi ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Intracellular Ph ◽  
Reproductive Stage ◽  
Valuable Insight ◽  
Anaerobic Conditions ◽  
Rice Grains ◽  
Important Challenge ◽  
Ph Decrease ◽  
Alcohol Dehydrogenase 2 ◽  
Adh Activity

Abstract Paddy fields are anaerobic and facilitate arsenite (As(III)) elution from the soil. Paddy-field rice accumulates arsenic (As) in its grains because silicate transporters actively assimilate As(III) during the reproductive stage. Reducing the As level in rice grains is an important challenge for agriculture. Using a forward genetic approach, we isolated a rice (Oryza sativa) mutant, low arsenic line 3 (las3), whose As levels were decreased in aerial tissues, including grains. The low-As phenotype was not observed in young plants before heading (emergence of the panicle). Genetic analyses revealed that a deficiency in alcohol dehydrogenase (ADH) 2 by mutation is responsible for the phenotype. Among the three rice ADH paralogues, ADH2 was the most efficiently produced in root tissue under anaerobic conditions. In wild-type (WT), silicon and As concentrations in aerial tissues increased with growth. However, the increase was suppressed in las3 during the reproductive stage. Accordingly, the gene expression of two silicate transporters, Lsi1 and Lsi2, was increased in WT around the time of heading, whereas the increase was suppressed in las3. These results indicate that the low-As phenotype in las3 is due to silicate transporter suppression. Measurement of intracellular pH by 31P-nuclear magnetic resonance revealed intracellular acidification of las3 roots under hypoxia, suggesting that silicate transporter suppression in las3 might arise from an intracellular pH decrease, which is known to be facilitated by a deficiency in ADH activity under anaerobic conditions. This study provides valuable insight into reducing As levels in rice grains.

scholarly journals GENETIC AND BIOCHEMICAL BASIS OF ENZYME ACTIVITY VARIATION IN NATURAL POPULATIONS. I. ALCOHOL DEHYDROGENASE IN DROSOPHILA MELANOGASTER

Genetics ◽  
1978 ◽  
Vol 89 (2) ◽  
pp. 371-388
Author(s):  
John F McDonald ◽  
Francisco J Ayala
Keyword(s):  
Gene Regulation ◽  
Drosophila Melanogaster ◽  
Alcohol Dehydrogenase ◽  
Natural Populations ◽  
Difficult Problem ◽  
Regulatory Genes ◽  
Biochemical Basis ◽  
Evolutionary Consequence ◽  
The Third ◽  
Adh Activity

ABSTRACT Recent studies by various authors suggest that variation in gene regulation may be common in nature, and might be of great evolutionary consequence; but the ascertainment of variation in gene regulation has proven to be a difficult problem. In this study, we explore this problem by measuring alcohol dehydrogenase (ADH) activity in Drosophila melanogaster strains homozygous for various combinations of given second and third chromosomes sampled from a natural population. The structural locus (Adh) coding for ADH is on the second chromosome. The results show that: (1) there are genes, other than Adh, that affect the levels of ADH activity; (2) at least some of these "regulatory" genes are located on the third chromosome, and thus are not adjacent to the Adh locus; (3) variation exists in natural populations for such regulatory genes; (4) the effect of these regulatory genes varies as they interact with different second chromosomes; (5) third chromosomes with high-activity genes are either partially or completely dominant over chromosomes with low-activity genes; (6) the effects of the regulatory genes are pervasive throughout development; and (7) the third chromosome genes regulate the levels of ADH activity by affecting the number of ADH molecules in the flies. The results are consistent with the view that the evolution of regulatory genes may play an important role in adaptation.

Intracellular acidification induces apoptosis by stimulating ICE-like protease activity

1997 ◽  
Vol 110 (5) ◽  
pp. 653-661 ◽  
Author(s):  
I.J. Furlong ◽  
R. Ascaso ◽  
A. Lopez Rivas ◽  
M.K. Collins
Keyword(s):  
Cell Line ◽  
Dna Fragmentation ◽  
Intracellular Ph ◽  
Protease Activity ◽  
Intracellular Acidification ◽  
Over Expression ◽  
Protease Activation ◽  
Dependent Cell ◽  
A Cell ◽  
Ph Decrease

ICE-like protease activation and DNA fragmentation are preceded by a decrease in intracellular pH (pHi) during apoptosis in the IL-3 dependent cell line BAF3. Acidification occurs after 7 hours in cells deprived of IL-3 and after 4 hours when cells are treated with etoposide, close to the time of detection of ICE-like protease activity. Increasing extracellular pH reduces ICE-like protease activation and DNA fragmentation. Bcl-2 over-expression both delays acidification and inhibits ICE-like protease activation. Generation of a rapid intracellular pH decrease, using the ionophore nigericin, induces ICE-like protease activation and apoptosis. ZVAD, a cell permeable inhibitor of ICE-like proteases, does not affect acidification but inhibits apoptosis induced by IL-3 removal or nigericin treatment. These data suggest that intracellular acidification triggers apoptosis by directly or indirectly activating ICE-like proteases.

Alcohol and aldehyde dehydrogenase activity in the stomach and small intestine of rats poisoned with methanol

2001 ◽  
Vol 20 (5) ◽  
pp. 255-258
Author(s):  
L Chrostek ◽  
D Szczepura ◽  
M Szmitkowski ◽  
W Jelski ◽  
J Wierzchowski
Keyword(s):  
Small Intestine ◽  
Alcohol Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Aldehyde Dehydrogenase ◽  
Protein Denaturation ◽  
Cell Damage ◽  
Sublethal Dose ◽  
Adh Activity ◽  
Aldehyde Dehydrogenase Activity

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.

scholarly journals The Identification and Characterization of ADR6, a Gene Required for Sporulation and for Expression of the Alcohol Dehydrogenase II Isozyme From Saccharomyces cerevisiae

Genetics ◽  
1987 ◽  
Vol 116 (4) ◽  
pp. 523-530
Author(s):  
Aileen K W Taguchi ◽  
Elton T Young
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Alcohol Dehydrogenase ◽  
Isocitrate Lyase ◽  
Carbon Sources ◽  
Recessive Mutation ◽  
Yeast Saccharomyces Cerevisiae ◽  
Upstream Activating Sequence ◽  
Adh Activity ◽  
Identification And Characterization

ABSTRACT The alcohol dehydrogenase II isozyme (enzyme, ADHII; structural gene, ADH2) of the yeast, Saccharomyces cerevisiae, is under stringent carbon catabolite control. This cytoplasmic isozyme exhibits negligible activity during growth in media containing fermentable carbon sources such as glucose and is maximal during growth on nonfermentable carbon sources. A recessive mutation, adr6-1, and possibly two other alleles at this locus, were selected for their ability to decrease Ty-activated ADH2-6 c expression. The adr6-1 mutation led to decreased ADHII activity in both ADH2-6c and ADH2+ strains, and to decreased levels of ADH2 mRNA. Ty transcription and the expression of two other carbon catabolite regulated enzymes, isocitrate lyase and malate dehydrogenase, were unaffected by the adr6-1 mutation. adr6-1/adr6-1strains were defective for sporulation, indicating that adr6 mutations may have pleiotropic effects. The sporulation defect was not a consequence of decreased ADH activity. Since the ADH2-6c mutation is due to insertion of a 5.6-kb Ty element at the TATAA box, it appears that the ADR6+-dependent ADHII activity required ADH2 sequences 3′ to or including the TATAA box. The ADH2 upstream activating sequence (UAS) was probably not required. The ADR6 locus was unlinked to the ADR1 gene which encodes another trans-acting element required for ADH2 expression.

scholarly journals The comparison of total bile acid concentration and alcohol dehydrogenase activity as markers of intrahepatic cholestasis of pregnancy

2021 ◽  
Author(s):  
Wojciech Jelski ◽  
Joanna Piechota ◽  
Karolina Orywal ◽  
Barbara Mroczko
Keyword(s):  
Bile Acid ◽  
Alcohol Dehydrogenase ◽  
Bile Acids ◽  
Intrahepatic Cholestasis ◽  
Total Bile Acid ◽  
Intrahepatic Cholestasis Of Pregnancy ◽  
Third Trimester ◽  
Total Bile Acids ◽  
Adh Activity ◽  
Cholestasis Of Pregnancy

Introduction: Intrahepatic cholestasis of pregnancy (ICP) is the liver disorder in the second or early third trimester of pregnancy. It is characterized by pruritus with increased serum bile acids concentration and other liver function tests. ICP  is connected with increased risk of fetal mortality, but is unfortunately detected quite late. Therefore, it is important to recognize the disease in its early stages. We aimed to investigate the serum alcohol dehydrogenase (ADH) activity and compare it with the concentration of total bile acid (TBA) in women with ICP. Methods: Serum samples were taken for routine investigation from 80 pregnancies with ICP in the second or third trimester of pregnancy and from 80 healthy pregnant women in the same time of pregnancy. For measurement of class I activity we used the spectrofluorometric methods. The total ADH activitiy was measured by the photometric method. Results: The analysis of results shows a statistically significant increase in the activity of ADH I and ADH total (about 60% and 41.3%, respectively). Activity of ADH I well correlated with aminotransferases (alanine ALT and aspartate AST) and total bile acids (TBA) concentration. The total ADH activity was also positively correlated with ALT, AST and total bile acids. Conclusion: We can state that the activity of class I alcohol dehydrogenase isoenzyme in the sera of patients with ICP is increased and seems to be a good indicator of liver cell destruction during this disease and is comparable with the value of other markers.

scholarly journals MOLECULAR POPULATION GENETICS OF THE ALCOHOL DEHYDROGENASE GENE REGION OF DROSOPHILA MELANOGASTER

Genetics ◽  
1986 ◽  
Vol 114 (4) ◽  
pp. 1165-1190
Author(s):  
Charles F Aquadro ◽  
Susan F Desse ◽  
Molly M Bland ◽  
Charles H Langley ◽  
Cathy C Laurie-Ahlberg
Keyword(s):  
Drosophila Melanogaster ◽  
Alcohol Dehydrogenase ◽  
Sequence Variation ◽  
Natural Populations ◽  
Restriction Map ◽  
Length Variation ◽  
Eastern United States ◽  
Chromosome Inversion ◽  
Frequency Spectra ◽  
Adh Activity

ABSTRACT Variation in the DNA restriction map of a 13-kb region of chromosome ll including the alcohol dehydrogenase structural gene (Adh) was examined in Drosophila melanogaster from natural populations. Detailed analysis of 48 D. melanogaster lines representing four eastern United States populations revealed extensive DNA sequence variation due to base substitutions, insertions and deletions. Cloning of this region from several lines allowed characterization of length variation as due to unique sequence insertions or deletions [nine sizes; 21-200 base pairs (bp)] or transposable element insertions (several sizes, 340 bp to 10.2 kb, representing four different elements). Despite this extensive variation in sequences flanking the Adh gene, only one length polymorphism is clearly associated with altered Adh expression (a copia element approximately 250 bp 5′ to the distal transcript start site). Nonetheless, the frequency spectra of transposable elements within and between Drosophila species suggests they are slightly deleterious. Strong nonrandom associations are observed among Adh region sequence variants, ADH allozyme (Fast vs. Slow), ADH enzyme activity and the chromosome inversion ln(2L)t. Phylogenetic analysis of restriction map haplotypes suggest that the major twofold component of ADH activity variation (high vs. low, typical of Fast and Slow allozymes, respectively) is due to sequence variation tightly linked to and possibly distinct from that underlying the allozyme difference. The patterns of nucleotide and haplotype variation for Fast and Slow allozyme lines are consistent with the recent increase in frequency and spread of the Fast haplotype associated with high ADH activity. These data emphasize the important role of evolutionary history and strong nonrandom associations among tightly linked sequence variation as determinants of the patterns of variation observed in natural populations.

A FRET-based two-photon probe for in vivo tracking of pH during a traumatic brain injury process

2019 ◽  
Vol 43 (43) ◽  
pp. 17018-17022
Author(s):  
Baoping Zhai ◽  
Shuyang Zhai ◽  
Ruilin Hao ◽  
Jianjun Xu ◽  
Zhihong Liu
Keyword(s):  
Traumatic Brain Injury ◽  
Brain Injury ◽  
Neurodegenerative Diseases ◽  
Intracellular Ph ◽  
Ph Change ◽  
Ph Probe ◽  
Two Photon ◽  
Ph Decrease

Traumatic brain injury (TBI) is a cause of neurodegenerative diseases accompanied by intracellular pH decrease. Herein, a FRET-based ratiometric two-photon fluorescent pH probe is designed to monitor pH change and understand TBI process.

scholarly journals Adaptedness of Variants at an Alcohol Dehydrogenase Locus in Bromus mollis L. (Soft Bromegrass)

1976 ◽  
Vol 29 (4) ◽  
pp. 389 ◽  
Author(s):  
ADH Brown ◽  
DR Marshall ◽  
J Munday
Keyword(s):  
Alcohol Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Dry Matter ◽  
Animal Species ◽  
Natural Populations ◽  
Continuous Flooding ◽  
Naturally Occurring ◽  
Alcohol Dehydrogenase Activity ◽  
Adh Activity ◽  
Bromus Mollis

Alcohol dehydrogenase is highly polymorphic in many plant and animal species. Here we report evidence that the naturally occurring, electrophoretically detectable allozyme variants of the AdhlB locus in B. mollis can respond differentially to environmental stresses. It is argued that alcohol dehydrogenase activity is specifically involved in response to these stresses. Crude extracts of predominantly selfed seeds sampled from plants of known Adh1B genotype were assayed for their ADH activity in the forward and backward reactions. The seeds from Adh~B Adh~B plants produced extracts about 12 % less active in both directions than seeds from their Adh~BAdh~B counterparts. Such Adh~BAdh~B plants were also shown to produce about 13% more dry matter when grown under continuous flooding in the greenhouse whereas no difference between genotypes was detected in control pots. The seeds of Adh~B Adh~B plants showed an advantage over the alternative homozygotes in more rapid germination at 2�C, but no difference was found at 15�C. Thus the variants are differentially adapted, and this is likely to playa role in the maintenance of the polymorphism in natural populations.

Effects of manipulation of pyruvate decarboxylase and alcohol dehydrogenase levels on the submergence tolerance of rice

2001 ◽  
Vol 28 (12) ◽  
pp. 1231 ◽  
Author(s):  
Musrur Rahman ◽  
Anil Grover ◽  
W. James Peacock ◽  
Elizabeth S. Dennis ◽  
Marc H. Ellis
Keyword(s):  
Alcohol Dehydrogenase ◽  
Ethanol Production ◽  
Rice Variety ◽  
Pyruvate Decarboxylase ◽  
Inducible Promoter ◽  
Moderate Increase ◽  
Sense Orientation ◽  
Transgenic Lines ◽  
Hybrid Lines ◽  
Adh Activity

A transgenic approach was taken to manipulate the levels of pyruvate decarboxylase (PDC) and alcohol dehydrogenase (ADH) in rice, in order to investigate whether alteration of ethanol fermentation can affect anaerobic tolerance. A line transformed with an antisense Adh1 construct had only 4–8% of the ADH activity of untransformed plants. This line showed reduced ethanol production and coleoptile growth under anoxia. Mature plants had reduced survival when submerged in water and exposed to anoxia, suggesting that ADH plays an essential role in seed germination and plant survival in the absence of O2. A transgenic line transformed with a cotton Adh2 cDNA in the sense orientation relative to a constitutive promoter, showed 3–4-fold more ADH activity than either untransformed controls, or a flooding-tolerant rice variety (FR13A), both in air and under hypoxia. However, ethanol production by this line was only slightly higher than that of untransformed controls, and there was no increase in survival following anoxia treatments. Three independent transgenic lines containing the ricePdc1 cDNA driven by an anaerobically-inducible promoter (6XARE) showed an increase in PDC1 polypeptide in shoots, but not in roots or endosperm. A moderate increase in PDC activity and ethanol production was observed in shoots of these lines under anaerobic conditions, as well as decreased survival of shoots when submerged and exposed to anoxia. F1 plants containing both the PDC and ADH constructs showed levels of anoxia-tolerance similar to those of untransformed plants. These results suggest that over-production of PDC may be toxic to rice plants because of increased acetaldehyde. Consistent with this view, acetaldehyde levels were appreciably higher in plants over-producing PDC, compared with untransformed plants, or hybrid lines containing both the PDC and ADH constructs.

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