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The Failure of Two Major Formaldehyde Catabolism Enzymes (ADH5 and ALDH2) Leads to Partial Synthetic Lethality in C57BL/ 6 Mice Jun Nakamura1,2*, Darcy W

Nakamura et al. Genes and Environment (2020) 42:21 https://doi.org/10.1186/s41021-020-00160-4 SHORT REPORT Open Access The failure of two major formaldehyde catabolism enzymes (ADH5 and ALDH2) leads to partial synthetic lethality in C57BL/ 6 mice Jun Nakamura1,2*, Darcy W. Holley3, Toshihiro Kawamoto4 and Scott J. Bultman3 Abstract Background: Exogenous formaldehyde is classified by the IARC as a Category 1 known human carcinogen. Meanwhile, a significant amount of endogenous formaldehyde is produced in the human body; as such, formaldehyde-derived DNA and protein adducts have been detected in animals and humans in the absence of major exogenous formaldehyde exposure. However, the toxicological effects of endogenous formaldehyde on individuals with normal DNA damage repair functions are not well understood. In this study, we attempted to generate C57BL/6 mice deficient in both Adh5 and Aldh2, which encode two major enzymes that metabolize endogenous formaldehyde, in order to understand the effects of endogenous formaldehyde on mice with normal DNA repair function. Results: Due to deficiencies in both ADH5 and ALDH2, few mice survived past post-natal day 21. In fact, the survival of pups within the first few days after birth was significantly decreased. Remarkably, two Aldh2−/−/Adh5−/− mice survived for 25 days after birth, and we measured their total body weight and organ weights. The body weight of Aldh2−/−/Adh5−/− mice decreased significantly by almost 37% compared to the Aldh2−/−/Adh5+/− and Aldh2−/−/Adh5+/+ mice of the same litter. In addition, the absolute weight of each organ was also significantly reduced. Conclusion: Mice deficient in both formaldehyde-metabolizing enzymes ADH5 and ALDH2 were found to develop partial synthetic lethality and mortality shortly after birth.
Age-Dependent Protein Abundance of Cytosolic Alcohol and Aldehyde Dehydrogenases in Human Liver S

Supplemental material to this article can be found at: http://dmd.aspetjournals.org/content/suppl/2017/08/21/dmd.117.076463.DC2 http://dmd.aspetjournals.org/content/suppl/2017/06/12/dmd.117.076463.DC1 1521-009X/45/9/1044–1048$25.00 https://doi.org/10.1124/dmd.117.076463 DRUG METABOLISM AND DISPOSITION Drug Metab Dispos 45:1044–1048, September 2017 Copyright ª 2017 by The American Society for Pharmacology and Experimental Therapeutics Age-dependent Protein Abundance of Cytosolic Alcohol and Aldehyde Dehydrogenases in Human Liver s Deepak Kumar Bhatt, Andrea Gaedigk, Robin E. Pearce, J. Steven Leeder, and Bhagwat Prasad Department of Pharmaceutics, University of Washington, Seattle, Washington (D.K.B., B.P.); Department of Clinical Pharmacology, Toxicology & Therapeutic Innovation, Children’s Mercy-Kansas City, Missouri and School of Medicine, University of Missouri-Kansas City, Kansas City, Missouri (A.G., R.E.P., J.S.L.) Received April 21, 2017; accepted June 5, 2017 ABSTRACT Hepatic cytosolic alcohol and aldehyde dehydrogenases (ADHs and the adult levels, respectively. For all proteins, the abundance steeply ALDHs) catalyze the biotransformation of xenobiotics (e.g., cyclo- increased during the first year of life, which mostly reached adult Downloaded from phosphamide and ethanol) and vitamin A. Because age-dependent levels during early childhood (age between 1 and 6 years). Only for hepatic abundance of these proteins is unknown, we quantified ADH1A protein abundance in adults (age > 18 year) was ∼40% lower protein expression of ADHs and ALDH1A1 in a large cohort of pediatric relative to the early childhood group. Abundances of ADHs and and adult human livers by liquid chromatography coupled with tandem ALDH1A1 were not associated with sex in samples with age > 1 year mass spectrometry proteomics.
Alcohol-Responsive Genes Identified in Human Ipsc-Derived Neural Cultures

bioRxiv preprint doi: https://doi.org/10.1101/381673; this version posted July 31, 2018. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. Alcohol-responsive genes identified in human iPSC-derived neural cultures Kevin P. Jensen1,2,#, Richard Lieberman3,#, Henry R. Kranzler4,5, Joel Gelernter1,2, and Jonathan Covault3,6* 1 Department of Psychiatry, Yale University School of Medicine, New Haven, CT 06511 2 VA Connecticut Healthcare System, West Haven, CT 06516 3 Alcohol Research Center, Department of Psychiatry, University of Connecticut School of Medicine, Farmington, CT 06030-1410 4 Center for Studies of Addiction, Department of Psychiatry, Perelman School of Medicine of the University of Pennsylvania, Philadelphia, PA 19104 5 VISN4 MIRECC, Crescenz VAMC, Philadelphia, PA 19104 6 Institute for Systems Genomics, University of Connecticut, Storrs, CT 06269 # These authors contributed equally to this work *Correspondence: Department of Psychiatry UCONN Health 263 Farmington Avenue Farmington, CT 06030-1410 Telephone: 860-679-7560 Fax: 860-679-1296 Email: [email protected] Running title: Transcriptional effects of alcohol in human neural cultures 1 bioRxiv preprint doi: https://doi.org/10.1101/381673; this version posted July 31, 2018. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license.
Confirmation of Pathogenic Mechanisms by SARS-Cov-2–Host

Messina et al. Cell Death and Disease (2021) 12:788 https://doi.org/10.1038/s41419-021-03881-8 Cell Death & Disease ARTICLE Open Access Looking for pathways related to COVID-19: confirmation of pathogenic mechanisms by SARS-CoV-2–host interactome Francesco Messina 1, Emanuela Giombini1, Chiara Montaldo1, Ashish Arunkumar Sharma2, Antonio Zoccoli3, Rafick-Pierre Sekaly2, Franco Locatelli4, Alimuddin Zumla5, Markus Maeurer6,7, Maria R. Capobianchi1, Francesco Nicola Lauria1 and Giuseppe Ippolito 1 Abstract In the last months, many studies have clearly described several mechanisms of SARS-CoV-2 infection at cell and tissue level, but the mechanisms of interaction between host and SARS-CoV-2, determining the grade of COVID-19 severity, are still unknown. We provide a network analysis on protein–protein interactions (PPI) between viral and host proteins to better identify host biological responses, induced by both whole proteome of SARS-CoV-2 and specific viral proteins. A host-virus interactome was inferred, applying an explorative algorithm (Random Walk with Restart, RWR) triggered by 28 proteins of SARS-CoV-2. The analysis of PPI allowed to estimate the distribution of SARS-CoV-2 proteins in the host cell. Interactome built around one single viral protein allowed to define a different response, underlining as ORF8 and ORF3a modulated cardiovascular diseases and pro-inflammatory pathways, respectively. Finally, the network-based approach highlighted a possible direct action of ORF3a and NS7b to enhancing Bradykinin Storm. This network-based representation of SARS-CoV-2 infection could be a framework for pathogenic evaluation of specific 1234567890():,; 1234567890():,; 1234567890():,; 1234567890():,; clinical outcomes.
Is There a Role for Ethanol Assay Using Alcohol Dehydrogenase in a Basic Drugs and Alcohol Screen of Blood Following Routine Autopsies?

Journal of Clinical Pathology and Forensic Medicine Vol. 3(2), pp. 17-19, December 2012 Available online at http://www.academicjournals.org/JCPFM DOI: 10.5897/JCPFM12.003 ISSN 2I41-2405 ©2012 Academic Journals Short Communication Is there a role for ethanol assay using alcohol dehydrogenase in a basic drugs and alcohol screen of blood following routine autopsies? William Tormey 1,2 and Tara Moore 3 1Biomedical Sciences, University of Ulster Cromore Road, Coleraine, BT52 1SA, Northern Ireland. 2Department of Chemical Pathology, Beaumont Hospital, Dublin 9, Ireland. 3Biomedical Sciences, University of Ulster, Cromore Road, Coleraine, BT52 1SA, Northern Ireland. Accepted 22 March, 2012 The external examination system of determining the cause of death as operated in Dundee, Scotland is controversial. The addition of a blood or urine specimen for drugs and alcohol processed by hospital autoanalysers will reduce error in death certification. This is even more convenient to organise with a shorter turn-around time than imaging by computed tomography (CT) or magnetic resonance imaging (MRI). These measures may reduce the autopsy rate and ameliorate the distress of families of the deceased. Key words: Autopsy, alcohol, death. INTRODUCTION For over a decade, there has been controversy over the dehydrogenase and the back reaction nicotinamide appropriateness of the high rate of coroner’s autopsies adenine dinucleotide (NAD) to NADH measured (Pounder, 2000; Rutty et al., 2001). Advocacy of the spectrophotometrically at 340 nm on the Olympus 5400 “view and grant” system of issuing the cause of death as autoanalyser for the analysis of alcohol. The data sheet operated in Dundee, Scotland has been challenged and claims that the assay can accurately quantitate alcohol imaging is suggested as a partial answer to lessen the concentrations within the range of 10 to 600 mg/dl.
How Is Alcohol Metabolized by the Body?

Overview: How Is Alcohol Metabolized by the Body? Samir Zakhari, Ph.D. Alcohol is eliminated from the body by various metabolic mechanisms. The primary enzymes involved are aldehyde dehydrogenase (ALDH), alcohol dehydrogenase (ADH), cytochrome P450 (CYP2E1), and catalase. Variations in the genes for these enzymes have been found to influence alcohol consumption, alcohol-related tissue damage, and alcohol dependence. The consequences of alcohol metabolism include oxygen deficits (i.e., hypoxia) in the liver; interaction between alcohol metabolism byproducts and other cell components, resulting in the formation of harmful compounds (i.e., adducts); formation of highly reactive oxygen-containing molecules (i.e., reactive oxygen species [ROS]) that can damage other cell components; changes in the ratio of NADH to NAD+ (i.e., the cell’s redox state); tissue damage; fetal damage; impairment of other metabolic processes; cancer; and medication interactions. Several issues related to alcohol metabolism require further research. KEY WORDS: Ethanol-to acetaldehyde metabolism; alcohol dehydrogenase (ADH); aldehyde dehydrogenase (ALDH); acetaldehyde; acetate; cytochrome P450 2E1 (CYP2E1); catalase; reactive oxygen species (ROS); blood alcohol concentration (BAC); liver; stomach; brain; fetal alcohol effects; genetics and heredity; ethnic group; hypoxia The alcohol elimination rate varies state of liver cells. Chronic alcohol con- he effects of alcohol (i.e., ethanol) widely (i.e., three-fold) among individ- sumption and alcohol metabolism are on various tissues depend on its uals and is influenced by factors such as strongly linked to several pathological concentration in the blood T chronic alcohol consumption, diet, age, consequences and tissue damage. (blood alcohol concentration [BAC]) smoking, and time of day (Bennion and Understanding the balance of alcohol’s over time.
Computational Exploration of the Medium-Chain Dehydrogenase / Reductase Superfamily

From the Department of Medical Biochemistry and Biophysics Karolinska Institutet, Stockholm, Sweden COMPUTATIONAL EXPLORATION OF THE MEDIUM-CHAIN DEHYDROGENASE / REDUCTASE SUPERFAMILY Linus J. Östberg Stockholm 2017 All previously published papers were reproduced with permission from the publisher. Published by Karolinska Institutet. Printed by E-Print AB 2017 ©Linus J. Östberg, 2017 ISBN 978-91-7676-650-7 COMPUTATIONAL EXPLORATION OF THE MEDIUM-CHAIN DEHYDROGENASE / REDUCTASE SUPERFAMILY THESIS FOR DOCTORAL DEGREE (Ph.D.) By Linus J. Östberg Principal Supervisor: Opponent: Prof. Jan-Olov Höög Prof. Jaume Farrés Karolinska Institutet Autonomous University of Barcelona Department of Medical Biochemistry and Department of Biochemistry and Biophysics Molecular Biology Co-supervisor: Examination Board: Prof. Bengt Persson Prof. Erik Lindahl Uppsala University Stockholm University Department of Cell and Molecular Biology Department of Biochemistry and Biophysics Assoc. Prof. Tanja Slotte Stockholm University Department of Ecology, Environment and Plant Sciences Prof. Elias Arnér Karolinska Institutet Department of Medical Biochemistry and Biophysics ABSTRACT The medium-chain dehydrogenase/reductase (MDR) superfamily is a protein family with more than 170,000 members across all phylogenetic branches. In humans there are 18 repre- sentatives. The entire MDR superfamily contains many protein families such as alcohol dehy- drogenase, which in mammals is in turn divided into six classes, class I–VI (ADH1–6). Most MDRs have enzymatical functions, catalysing the conversion of alcohols to aldehyde/ketones and vice versa, but the function of some members is still unknown. In the first project, a methodology for identifying and automating the classification of mammalian ADHs was developed using BLAST for identification and class-specific hidden Markov models were generated for identification.
1 Here Are the Quiz 4 Questions You Will Answer Online Using the Quiz

Chemistry 6720, quiz 4 handout Here are the quiz 4 questions you will answer online using the quiz tool in canvas instructure. Some of the questions deal with citric acid cycle enzymes that use mechanistic strategies covered in the lectures. Since we did not cover all of those specific enzymes in lecture, be sure to review the citric acid cycle ahead of taking the quiz online so you can answer the appropriate questions regarding mechanistic strategies/themes for the enzymes. In doing so, practice drawing mechanisms for each enzyme of the citric acid cycle. You will probably need to look up the mechanisms for isocitrate dehydrogenase, aconitase, succinate dehydrogenase, and succinyl-CoA synthetase in a general biochemistry text. I will not be asking specific details of the mechanisms for those 4 enzymes, but you will still need to be generally familiar with how they operate to answer a few of the questions below. You do not need to know the chemistry of FAD reduction for the quiz. Be sure to note the quiz deadline in canvas to be sure you get your answers submitted by the deadline. 1. Shown at the right is a Fischer projection for D-glucose. Use the strategy described in the lecture to assign the configurations (R or S) of the chiral centers at C2, C3, C4, and C5. 2. Using the structures shown to the right, assign the methyl groups of isopropanol, and the hydrogens at C2 and C3 of succinate, as either ProR or ProS. Use the strategy covered in lecture to guide you in making the assignments.
Original Article Compensatory Upregulation of Aldo-Keto Reductase 1B10 to Protect Hepatocytes Against Oxidative Stress During Hepatocarcinogenesis

Am J Cancer Res 2019;9(12):2730-2748 www.ajcr.us /ISSN:2156-6976/ajcr0097527 Original Article Compensatory upregulation of aldo-keto reductase 1B10 to protect hepatocytes against oxidative stress during hepatocarcinogenesis Yongzhen Liu1, Jing Zhang1, Hui Liu1, Guiwen Guan1, Ting Zhang1, Leijie Wang1, Xuewei Qi1, Huiling Zheng1, Chia-Chen Chen1, Jia Liu1, Deliang Cao2, Fengmin Lu3, Xiangmei Chen1 1State Key Laboratory of Natural and Biomimetic Drugs, Department of Microbiology and Infectious Disease Center, School of Basic Medical Sciences, Peking University Health Science Center, Beijing 100191, P. R. China; 2Department of Medical Microbiology, Immunology and Cell Biology, Simmons Cancer Institute at Southern Illinois University School of Medicine, 913 N, Rutledge Street, Springfield, IL 62794, USA; 3Peking University People’s Hospital, Peking University Hepatology Institute, Beijing 100044, P. R. China Received May 26, 2019; Accepted November 15, 2019; Epub December 1, 2019; Published December 15, 2019 Abstract: Aldo-keto reductase 1B10 (AKR1B10), a member of aldo-keto reductase superfamily, contributes to detox- ification of xenobiotics and metabolization of physiological substrates. Although increased expression of AKR1B10 was found in hepatocellular carcinoma (HCC), the role of AKR1B10 in the development of HCC remains unclear. This study aims to illustrate the role of AKR1B10 in hepatocarcinogenesis based on its intrinsic oxidoreduction abilities. HCC cell lines with AKR1B10 overexpression or knockdown were treated with doxorubicin or hydrogen peroxide to determinate the influence of aberrant AKR1B10 expression on cells’ response to oxidative stress. Using Akr1b8 (the ortholog of human AKR1B10) knockout mice, diethylnitrosamine (DEN) induced liver injury, chronic inflammation and hepatocarcinogenesis were explored. Clinically, the pattern of serum AKR1B10 relevant to disease progres- sion was investigated in a patient cohort with chronic hepatitis B (n=30), liver cirrhosis (n=30) and HCC (n=40).
ARTICLE Evidence of Positive Selection on a Class I ADH Locus

ARTICLE Evidence of Positive Selection on a Class I ADH Locus Yi Han,* Sheng Gu,* Hiroki Oota,† Michael V. Osier,‡ Andrew J. Pakstis, William C. Speed, Judith R. Kidd, and Kenneth K. Kidd The alcohol dehydrogenase (ADH) family of enzymes catalyzes the reversible oxidation of alcohol to acetaldehyde. Seven ADH genes exist in a segment of ∼370 kb on 4q21. Products of the three class I ADH genes that share 95% sequence identity are believed to play the major role in the first step of ethanol metabolism. Because the common belief that selection has operated at the ADH1B*47His allele in East Asian populations lacks direct biological or statistical evidence, we used genomic data to test the hypothesis. Data consisted of 54 single-nucleotide polymorphisms (SNPs) across the ADH clusters in a global sampling of 42 populations. Both the Fst statistic and the long-range haplotype (LRH) test provided positive evidence of selection in several East Asian populations. The ADH1B Arg47His functional polymorphism has the highest Fst of the 54 SNPs in the ADH cluster, and it is significantly above the mean Fst of 382 presumably neutral sites tested on the same 42 population samples. The LRH test that uses cores including that site and extending on both sides also gives significant evidence of positive selection in some East Asian populations for a specific haplotype carrying the ADH1B*47His allele. Interestingly, this haplotype is present at a high frequency in only some East Asian populations, whereas the specific allele also exists in other East Asian populations and in the Near East and Europe but does not show evidence of selection with use of the LRH test.
Anti-ADH5 Monoclonal Antibody, Clone FQS23996(C) (DCABH-6425) This Product Is for Research Use Only and Is Not Intended for Diagnostic Use

Anti-ADH5 monoclonal antibody, clone FQS23996(C) (DCABH-6425) This product is for research use only and is not intended for diagnostic use. PRODUCT INFORMATION Product Overview Rabbit monoclonal to ADH5 Antigen Description Class-III ADH is remarkably ineffective in oxidizing ethanol, but it readily catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione. Immunogen Synthetic peptide (the amino acid sequence is considered to be commercially sensitive) within Human ADH5 aa 1-100. The exact sequence is proprietary.Database link: P11766 Isotype IgG Source/Host Rabbit Species Reactivity Mouse, Rat, Human Clone FQS23996(C) Purity Tissue culture supernatant Conjugate Unconjugated Applications WB, IHC-P, IP, Flow Cyt Positive Control Human fetal liver, HepG2, Human fetal kidney and SH-SY5Y lysates. Human brain and kidney tissue. Permeabilized SH-SY5Y cells. Immunoprecipitation pellet from Human fetal liver lysate. Format Liquid Size 100 μl Buffer pH: 7.2; Preservative: 0.01% Sodium azide; Constituents: 49% PBS, 50% Glycerol, 0.05% BSA Preservative 0.01% Sodium Azide Storage Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term. Avoid freeze / thaw cycle. Ship Shipped at 4°C. GENE INFORMATION 45-1 Ramsey Road, Shirley, NY 11967, USA Email: [email protected] Tel: 1-631-624-4882 Fax: 1-631-938-8221 1 © Creative Diagnostics All Rights Reserved Gene Name ADH5 alcohol dehydrogenase 5 (class III), chi polypeptide [ Homo sapiens ] Official Symbol ADH5 Synonyms
Alcohol Dehydrogenase

Catalog Number: 100161, 151430, 159858 Alcohol Dehydrogenase Molecular Weight: 141,000 comprised of four subunits of 35,000 each.8 CAS # : 9031-72-5 Synonyms: ADH; Alcohol : NAD+ oxidoreductase Source: Yeast E.C. 1.1.1.1 Description: Alcohol dehydrogenase catalyzes the reaction: The common reaction in yeast cells is reduction of acetaldehyde to ethanol. In vitro the enzyme is generally assayed and used in a more alkaline pH region, a condition which favors a shift of equilibrium towards the oxidation of ethanol. Composition: A metalloenzyme containing four tightly bound zinc atoms per molecule.18,19 Per subunit, there are two distinct active site sulfhydryl groups which can be distinguished on the basis of differential reactivity with iodoacetate and butyl isocyanate.17 A histidine residue is considered to have an essential role.9 Optimum pH: For the oxidation of ethanol, pH 8.6-9.0 (the enzyme becomes increasingly unstable at higher pH). For the reduction of acetaldehyde a pH nearer to 7.0 is considered optimum. This reaction is kinetically complex with pH being only one factor determining optimum conditions. 1% Extinction coefficient: E 260= 12.6. Isoelectric point: 5.4.16 Solubility: Dissolves readily at 5 mg/ml in 0.01 M sodium phosphate pH 7.5 to give a clear colorless solution. Activators: Sulfyhydryl activating reagents, mercaptoethanol, dithiothreitol, cysteine, etc., and heavy metal chelating reagents. Specificity: Yeast ADH which has a more narrow specificity than that of liver enzyme, accepts ethanol, is somewhat active on the straight chain primary alcohols, and acts to a very limited extent on certain secondary and branched chain alcohols.10 NADP does not serve as coenzyme.