DOCSLIB.ORG

SUPPLEMENTARY DATA Supplementary Table 1. Effects Of

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
SUPPLEMENTARY DATA Supplementary Table 1. Effects Of SUPPLEMENTARY DATA Supplementary Table 1. Effects of 43 risk SNPs for type 2 diabetes or hyperglycemia on the levels of eight amino acids in non‐diabetic METSIM participants. SNP Gene Alleles T2D and/or MAF N HWE Alanine Glutamine Valine Leucine Isoleucine Phenylalanine Tyrosine Histidine maj/min GLU SNP total P-val % B P % B P % B P % B P % B P % B P % B P % B P rs780094 GCKR G/A GLU, T2D 37.7 5227 1.00 1.9 1.6E-11 -1.2 1.0E-05 0.2 0.719 1.2 0.001 2.3 3.1E-06 0.1 0.763 -1.1 0.001 -0.8 0.003 rs8042680 PRC1 A/G T2D 31.3 5735 0.09 0.3 0.386 0.0 0.888 1.2 0.001 1.2 0.002 1.7 0.001 0.6 0.088 0.4 0.419 0.5 0.097 rs11708067 ADCY5 G/T GLU, T2D 15.8 5086 0.42 -1.2 0.001 -1.0 0.003 0.1 0.881 -0.3 0.607 0.5 0.548 -0.3 0.471 -1.1 0.032 -0.2 0.722 rs7578326 IRS1 G/A T2D 34.7 5819 1.00 0.1 0.936 -0.4 0.202 -0.7 0.047 -0.8 0.019 -1.5 0.003 -0.1 0.701 -0.7 0.037 -0.5 0.039 rs10811661 CDKN2B A/G T2D 14.8 6708 0.98 -0.6 0.082 -1.0 0.004 0.5 0.262 -0.2 0.889 0.4 0.579 0.6 0.079 0.1 0.713 -0.2 0.612 rs10885122 ADRA2A G/C GLU 15.5 5100 0.44 -0.8 0.034 -0.2 0.666 -0.1 0.893 0.1 0.920 0.7 0.396 -0.3 0.400 -0.4 0.530 -1.0 0.013 rs864745 JAZF1 A/G T2D 48.4 6713 0.34 -0.6 0.029 0.3 0.212 -0.3 0.324 -0.6 0.109 -1.1 0.008 -0.3 0.225 0.4 0.302 0.3 0.114 rs7501939 HNF1B A/C T2D 32.9 6426 0.86 0.0 0.856 -0.6 0.021 -0.1 0.873 0.9 0.082 1.2 0.009 0.0 0.998 0.4 0.264 0.4 0.120 rs13292136 CHCHD9 C/T T2D 13.8 5951 0.85 0.2 0.663 -0.1 0.790 0.7 0.132 0.3 0.694 0.8 0.329 0.5 0.171 1.3 0.012 0.4 0.294 rs896854 TP53INP1 A/C T2D 46.0 5796 0.88 0.6 0.013 0.0 0.843 0.0 0.853 0.3 0.327 -0.1 0.848 0.0 0.874 0.1 0.650 -0.5 0.059 rs10923931 NOTCH2 G/T T2D 14.0 6712 0.89 -0.3 0.304 0.3 0.423 -0.2 0.802 0.1 0.974 -0.6 0.174 -0.8 0.014 0.2 0.912 -0.1 0.934 rs1552224 CENTD2 T/C T2D 24.8 5906 0.05 0.7 0.016 -0.1 0.731 0.0 0.813 0.7 0.144 0.8 0.162 0.2 0.529 -0.1 0.800 0.1 0.842 rs7961581 TSPAN8 A/G T2D 19.7 6707 0.40 0.6 0.066 0.2 0.737 0.6 0.103 0.6 0.257 1.4 0.018 0.4 0.274 0.8 0.034 0.4 0.197 rs13266634 SLC30A8 T/A T2D, GLU 39.3 6712 0.94 -0.6 0.020 -0.4 0.061 -0.4 0.107 -0.3 0.486 -0.9 0.035 0.3 0.232 -0.5 0.103 -0.3 0.202 rs560887 G6PC2 C/T GLU 27.8 4983 0.01 -0.3 0.316 -0.2 0.711 0.8 0.032 1.2 0.024 1.3 0.037 0.5 0.081 0.5 0.295 -0.1 0.730 rs10423928 GIPR G/A GLU 21.7 5711 0.80 -0.7 0.026 0.5 0.136 -0.3 0.569 -0.4 0.429 -0.4 0.638 -0.6 0.071 0.3 0.580 0.2 0.412 rs7944584 MADD C/T GLU 18.0 5082 0.33 -0.3 0.410 0.1 0.868 -0.8 0.087 -1.1 0.029 -0.8 0.121 0.0 0.835 -0.3 0.675 0.2 0.690 rs9939609 FTO T/A T2D 40.0 6707 0.98 -0.3 0.429 -0.3 0.155 -0.1 0.819 0.0 0.948 0.4 0.394 0.0 0.950 -0.2 0.670 0.5 0.027 rs174550 FADS1 C/A GLU 42.7 5073 0.85 0.0 0.931 0.3 0.218 0.6 0.068 -0.4 0.434 0.9 0.070 0.5 0.048 0.4 0.176 0.1 0.639 rs2191349 DGBK C/T GLU, T2D 43.1 5019 0.76 -0.5 0.080 -0.2 0.722 -0.7 0.051 -0.2 0.538 -0.3 0.506 -0.1 0.621 -0.5 0.128 -0.1 0.564 rs4457053 ZBED3 G/C T2D 21.2 5901 0.57 0.6 0.055 0.4 0.314 0.0 0.926 -0.6 0.269 0.1 0.559 -0.1 0.868 0.4 0.457 0.1 0.686 rs7034200 GLIS3 C/T GLU 48.8 4929 0.01 0.2 0.370 0.5 0.085 0.6 0.059 0.2 0.637 0.2 0.731 0.2 0.421 0.1 0.866 0.3 0.338 rs2283228 KCNQ1 C/A T2D 6.1 6714 0.57 0.9 0.072 -0.2 0.740 -0.6 0.443 -0.2 0.716 -0.4 0.567 0.3 0.492 -0.2 0.836 -0.2 0.489 rs12779790 CDC123 A/G T2D 21.3 6700 0.44 0.0 0.846 -0.2 0.609 -0.3 0.323 0.1 0.893 -0.5 0.474 0.6 0.073 0.4 0.295 0.1 0.876 rs4402960 IGF2BP2 A/G T2D 31.9 6709 0.42 0.4 0.148 0.3 0.304 0.0 0.740 0.2 0.499 0.7 0.082 0.1 0.734 0.0 0.940 0.2 0.370 rs11605924 CRY2 G/A GLU 47.0 4765 0.43 -0.1 0.764 -0.3 0.353 -0.3 0.348 -0.7 0.097 -0.6 0.177 0.0 0.926 0.5 0.121 -0.5 0.133 ©2012 American Diabetes Association. Published online at http://diabetes.diabetesjournals.org/lookup/suppl/doi:10.2337/db11-1378/-/DC1 SUPPLEMENTARY DATA rs243021 BCL11A A/C T2D 43.6 5837 0.92 -0.4 0.176 0.2 0.657 -0.3 0.334 0.2 0.703 -0.5 0.265 -0.2 0.352 -0.4 0.289 -0.4 0.089 rs10010131 WFS1 G/A T2D 44.6 6714 0.71 0.1 0.512 0.1 0.697 0.5 0.100 0.0 0.951 0.6 0.108 0.1 0.715 0.3 0.551 0.1 0.942 rs1801282 PPARG A/T T2D 15.3 6716 0.78 -0.1 0.798 -0.2 0.508 -0.6 0.159 -0.2 0.779 -1.0 0.134 0.3 0.439 -0.3 0.490 -0.6 0.132 rs10830963 MTNR1B C/G T2D, GLU 35.8 6701 0.32 0.1 0.601 0.2 0.342 0.4 0.213 0.0 0.894 -0.1 0.682 -0.4 0.108 -0.4 0.195 0.1 0.746 rs4607103 ADAMTS9 C/A T2D 25.8 6716 0.38 -0.1 0.597 -0.4 0.121 0.2 0.635 0.5 0.431 0.6 0.422 0.4 0.267 0.1 0.785 0.4 0.285 rs11071657 FAM148A C/G GLU 30.5 5078 0.18 0.2 0.476 -0.1 0.799 -0.2 0.390 0.7 0.125 0.0 0.912 0.2 0.674 0.2 0.707 0.2 0.603 rs7754840 CDKAL1 C/A T2D 36.9 6716 0.96 0.0 0.876 0.1 0.553 -0.2 0.454 -0.6 0.132 -0.5 0.248 0.1 0.425 0.0 0.889 -0.1 0.966 rs4607517 GCK T/C GLU, T2D 9.8 5114 1.00 0.6 0.197 -0.2 0.550 0.2 0.884 -0.2 0.822 -0.4 0.477 0.1 0.984 0.5 0.416 0.6 0.159 rs340874 PROX1 T/A GLU, T2D 39.7 5049 0.10 0.2 0.346 -0.4 0.185 -0.1 0.731 0.4 0.340 0.6 0.155 0.3 0.244 0.1 0.963 -0.2 0.549 rs7578597 THADA C/T T2D 5.1 6714 0.90 -0.3 0.501 -0.3 0.612 0.5 0.586 -0.3 0.678 1.2 0.202 0.3 0.598 0.1 0.907 -0.2 0.743 rs231362 KCNQ1 C/T T2D 47.9 5143 0.98 -0.4 0.225 0.0 0.895 0.0 0.822 0.1 0.626 0.5 0.282 0.2 0.539 0.0 0.858 0.2 0.856 rs11920090 SLC2A2 A/G GLU 13.1 5108 0.87 0.2 0.810 0.6 0.240 -0.3 0.477 0.5 0.525 -0.4 0.572 0.7 0.060 0.7 0.225 0.4 0.353 rs5219 KCNJ11 C/T T2D 47.4 6692 0.99 -0.2 0.684 0.2 0.594 0.4 0.120 0.2 0.377 -0.1 0.961 -0.2 0.461 0.0 0.792 0.3 0.257 rs1111875 HHEX A/G T2D 46.6 6716 0.59 0.2 0.484 0.0 0.998 0.2 0.462 0.3 0.421 -0.1 0.981 -0.1 0.842 0.3 0.311 0.1 0.497 rs7903146 TCF7L2 G/A T2D, GLU 17.5 6715 0.45 0.1 0.697 -0.3 0.417 -0.2 0.530 0.0 0.933 0.0 0.705 0.3 0.328 -0.1 0.681 -0.2 0.486 rs11634397 ZFAND6 A/G T2D 40.6 5837 0.98 0.1 0.709 -0.3 0.420 0.0 0.982 -0.2 0.638 -0.4 0.438 0.0 0.781 0.1 0.439 0.0 0.901 rs2612067 HMGA2 G/A T2D 6.8 5879 0.55 -0.4 0.519 -0.5 0.487 0.1 0.932 0.6 0.495 -0.3 0.733 -0.2 0.699 0.1 0.859 0.0 0.934 Major/minor alleles are shown.
Load more

Recommended publications
  • The Aldehyde Dehydrogenase ALDH2*2 Allele Exhibits Dominance Over ALDH2*1 in Transduced Hela Cells
    The aldehyde dehydrogenase ALDH2*2 allele exhibits dominance over ALDH2*1 in transduced HeLa cells. Q Xiao, … , T Johnston, D W Crabb J Clin Invest. 1995;96(5):2180-2186. https://doi.org/10.1172/JCI118272. Research Article Individuals heterozygous or homozygous for the variant aldehyde dehydrogenase (ALDH2) allele (ALDH2*2), which encodes a protein differing only at residue 487 from the normal protein, have decreased ALDH2 activity in liver extracts and experience cutaneous flushing when they drink alcohol. The mechanisms by which this allele exerts its dominant effect is unknown. To study this effect, the human ALDH2*1 cDNA was cloned and the ALDH2*2 allele was generated by site-directed mutagenesis. These cDNAs were transduced using retroviral vectors into HeLa and CV1 cells, which do not express ALDH2. The normal allele directed synthesis of immunoreactive ALDH2 protein (ALDH2E) with the expected isoelectric point. Extracts of these cells contained increased aldehyde dehydrogenase activity with low Km for the aldehyde substrate. The ALDH2*2 allele directed synthesis of mRNA and immunoreactive protein (ALDH2K), but the protein lacked enzymatic activity. When ALDH2*1-expressing cells were transduced with ALDH2*2 vectors, both mRNAs were expressed and immunoreactive proteins with isoelectric points ranging between those of ALDH2E and ALDH2K were present, indicating that the subunits formed heteromers. ALDH2 activity in these cells was reduced below that of the parental ALDH2*1-expressing cells. Thus, the ALDH2*2 allele is sufficient to cause ALDH2 deficiency in vitro. Find the latest version: https://jci.me/118272/pdf The Aldehyde Dehydrogenase ALDH2*2 Allele Exhibits Dominance over ALDH2*1 in Transduced HeLa Cells Qing Xiao, * Henry Weiner,* Timothy Johnston,* and David W.
    [Show full text]
  • Corning® Supersomes™ Ultra Human Aldehyde Oxidase
    Corning® Supersomes™ Ultra Human Aldehyde Oxidase Aldehyde Oxidase (AO) is a cytosolic enzyme that plays an important role in non-CYP mediated drug metabolism and pharmacokinetics. AO has garnered significant attention in the pharmaceutical industry due to multiple drug failures during clinical trials that were associated with the AO pathway and an increase in the number of aromatic aza-heterocycle moieties found in drug leads that have been identified as substrates for AO. Traditionally, recombinant AO (rAO) is expressed in bacteria. However, this approach has disadvantages such as different protein post-translation modifications that lead to different function as compared to mammalian cells. Corning has developed Corning Supersomes Ultra Aldehyde Oxidase, a recombinant human AO enzyme utilizing a mammalian cell-based expression system to address these issues. This product will enable early assessment of the liability of AO for drug metabolism and clearance. Corning Supersomes Ultra Human Aldehyde Oxidase has been over-expressed in HEK-293 cells and exhibited a significantly higher activity as compared to AO expressed in E. coli. Time- dependent enzyme kinetics, using known substrates and inhibitors, between the rAO and the native form found in human liver cytosol produced a good correlation. Features and Benefits of Corning Supersomes Ultra Aldehyde Oxidase Mammalian cell expression system Corning Supersomes Ultra Human Aldehyde Oxidase Performance Corning Supersomes Ultra AO have been engineered in HEK-293 mammalian cells, thereby eliminating the biosafety concerns Activity Comparison Utilizing Probe Substrate (Zaleplon, 250 µM) associated with baculovirus. Stable and reliable in vitro tool 25 Corning Supersomes Ultra AO are a stable and reliable in vitro tool for the study of AO-mediated metabolism, which provides a 20 quantitative contribution of drug clearance.
    [Show full text]
  • RT² Profiler PCR Array (Rotor-Gene® Format) Human Amino Acid Metabolism I
    RT² Profiler PCR Array (Rotor-Gene® Format) Human Amino Acid Metabolism I Cat. no. 330231 PAHS-129ZR For pathway expression analysis Format For use with the following real-time cyclers RT² Profiler PCR Array, Rotor-Gene Q, other Rotor-Gene cyclers Format R Description The Human Amino Acid Metabolism I RT² Profiler PCR Array profiles the expression of 84 key genes important in biosynthesis and degradation of functional amino acids. Of the 20 amino acids required for protein synthesis, six of them (arginine, cysteine, glutamine, leucine, proline, and tryptophan), collectively known as the functional amino acids, regulate key metabolic pathways involved in cellular growth, and development, as well as other important biological processes such as immunity and reproduction. For example, leucine activates mTOR signaling and increases protein synthesis, leading to lymphocyte proliferation. Therefore, a lack of leucine can compromise immune function. Metabolic pathways interrelated with the biosynthesis and degradation of these amino acids include vitamin and cofactor biosynthesis (such as SAM or S-Adenosyl Methionine) as well as neurotransmitter metabolism (such as glutamate). This array includes genes for mammalian functional amino acid metabolism as well as genes involved in methionine metabolism, important also for nutrient sensing and sulfur metabolism. Using realtime PCR, you can easily and reliably analyze the expression of a focused panel of genes involved in functional amino acid metabolism with this array. For further details, consult the RT² Profiler PCR Array Handbook. Shipping and storage RT² Profiler PCR Arrays in the Rotor-Gene format are shipped at ambient temperature, on dry ice, or blue ice packs depending on destination and accompanying products.
    [Show full text]
  • Cytochrome P450 Oxidative Metabolism: Contributions to the Pharmacokinetics, Safety, and Efficacy of Xenobiotics
    1521-009X/44/8/1229–1245$25.00 http://dx.doi.org/10.1124/dmd.116.071753 DRUG METABOLISM AND DISPOSITION Drug Metab Dispos 44:1229–1245, August 2016 Copyright ª 2016 by The American Society for Pharmacology and Experimental Therapeutics Special Section on Emerging Novel Enzyme Pathways in Drug Metabolism—Commentary Cytochrome P450 and Non–Cytochrome P450 Oxidative Metabolism: Contributions to the Pharmacokinetics, Safety, and Efficacy of Xenobiotics Robert S. Foti and Deepak K. Dalvie Pharmacokinetics and Drug Metabolism, Amgen, Cambridge, Massachusetts (R.S.F.); and Pharmacokinetics, Dynamics, and Metabolism, Pfizer, La Jolla, California (D.K.D.) Downloaded from Received May 24, 2016; accepted June 10, 2016 ABSTRACT The drug-metabolizing enzymes that contribute to the metabolism this end, this Special Section on Emerging Novel Enzyme Pathways or bioactivation of a drug play a crucial role in defining the in Drug Metabolism will highlight a number of advancements that dmd.aspetjournals.org absorption, distribution, metabolism, and excretion properties of have recently been reported. The included articles support the that drug. Although the overall effect of the cytochrome P450 (P450) important role of non-P450 enzymes in the clearance pathways of family of drug-metabolizing enzymes in this capacity cannot be U.S. Food and Drug Administration–approved drugs over the past understated, advancements in the field of non-P450–mediated me- 10 years. Specific examples will detail recent reports of aldehyde tabolism have garnered increasing attention in recent years. This is oxidase, flavin-containing monooxygenase, and other non-P450 perhaps a direct result of our ability to systematically avoid P450 pathways that contribute to the metabolic, pharmacokinetic, or liabilities by introducing chemical moieties that are not susceptible pharmacodynamic properties of xenobiotic compounds.
    [Show full text]
  • Expression and Characterization of Pantoea CO Dehydrogenase To
    www.nature.com/scientificreports OPEN Expression and characterization of Pantoea CO dehydrogenase to utilize CO-containing industrial Received: 31 October 2016 Accepted: 06 February 2017 waste gas for expanding the Published: 14 March 2017 versatility of CO dehydrogenase Eun Sil Choi1,2,*, Kyoungseon Min3,*, Geun-Joong Kim2, Inchan Kwon1 & Yong Hwan Kim3 Although aerobic CO dehydrogenases (CODHs) might be applicable in various fields, their practical applications have been hampered by low activity and no heterologous expression. We, for the first time, could functionally express recombinant PsCODH in E. coli and obtained a highly concentrated recombinant enzyme using an easy and convenient method. Its electron acceptor spectra, optimum −1 conditions (pH 6.5 and 30 °C), and kinetic parameters (kcat of 12.97 s , Km of 0.065 mM, and specific activity of 0.86 Umg−1) were examined. Blast furnace gas (BFG) containing 20% CO, which is a waste gas from the steel-making process, was tested as a substrate for PsCODH. Even with BFG, the recombinant PsCODH retained 88.2% and 108.4% activity compared with those of pure CO and 20% CO, respectively. The results provide not only a promising strategy to utilize CO-containing industrial waste gases as cheap, abundant, and renewable resources but also significant information for further studies about cascade reactions producing value-added chemicals via CO2 as an intermediate produced by a CODH- based CO-utilization system, which would ultimately expand the versatility of CODH. Carbon monoxide (CO), which is a pollutant in the atmosphere, is massively emitted through both natural (e.g., production by plants and volcanic activity) and artificial processes (e.g., incomplete combustion of fuels and industrial processes)1–3.
    [Show full text]
  • Amino Acid Disorders
    471 Review Article on Inborn Errors of Metabolism Page 1 of 10 Amino acid disorders Ermal Aliu1, Shibani Kanungo2, Georgianne L. Arnold1 1Children’s Hospital of Pittsburgh, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA; 2Western Michigan University Homer Stryker MD School of Medicine, Kalamazoo, MI, USA Contributions: (I) Conception and design: S Kanungo, GL Arnold; (II) Administrative support: S Kanungo; (III) Provision of study materials or patients: None; (IV) Collection and assembly of data: E Aliu, GL Arnold; (V) Data analysis and interpretation: None; (VI) Manuscript writing: All authors; (VII) Final approval of manuscript: All authors. Correspondence to: Georgianne L. Arnold, MD. UPMC Children’s Hospital of Pittsburgh, 4401 Penn Avenue, Suite 1200, Pittsburgh, PA 15224, USA. Email: [email protected]. Abstract: Amino acids serve as key building blocks and as an energy source for cell repair, survival, regeneration and growth. Each amino acid has an amino group, a carboxylic acid, and a unique carbon structure. Human utilize 21 different amino acids; most of these can be synthesized endogenously, but 9 are “essential” in that they must be ingested in the diet. In addition to their role as building blocks of protein, amino acids are key energy source (ketogenic, glucogenic or both), are building blocks of Kreb’s (aka TCA) cycle intermediates and other metabolites, and recycled as needed. A metabolic defect in the metabolism of tyrosine (homogentisic acid oxidase deficiency) historically defined Archibald Garrod as key architect in linking biochemistry, genetics and medicine and creation of the term ‘Inborn Error of Metabolism’ (IEM). The key concept of a single gene defect leading to a single enzyme dysfunction, leading to “intoxication” with a precursor in the metabolic pathway was vital to linking genetics and metabolic disorders and developing screening and treatment approaches as described in other chapters in this issue.
    [Show full text]
  • Supplementary Materials
    Supplementary Materials COMPARATIVE ANALYSIS OF THE TRANSCRIPTOME, PROTEOME AND miRNA PROFILE OF KUPFFER CELLS AND MONOCYTES Andrey Elchaninov1,3*, Anastasiya Lokhonina1,3, Maria Nikitina2, Polina Vishnyakova1,3, Andrey Makarov1, Irina Arutyunyan1, Anastasiya Poltavets1, Evgeniya Kananykhina2, Sergey Kovalchuk4, Evgeny Karpulevich5,6, Galina Bolshakova2, Gennady Sukhikh1, Timur Fatkhudinov2,3 1 Laboratory of Regenerative Medicine, National Medical Research Center for Obstetrics, Gynecology and Perinatology Named after Academician V.I. Kulakov of Ministry of Healthcare of Russian Federation, Moscow, Russia 2 Laboratory of Growth and Development, Scientific Research Institute of Human Morphology, Moscow, Russia 3 Histology Department, Medical Institute, Peoples' Friendship University of Russia, Moscow, Russia 4 Laboratory of Bioinformatic methods for Combinatorial Chemistry and Biology, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Moscow, Russia 5 Information Systems Department, Ivannikov Institute for System Programming of the Russian Academy of Sciences, Moscow, Russia 6 Genome Engineering Laboratory, Moscow Institute of Physics and Technology, Dolgoprudny, Moscow Region, Russia Figure S1. Flow cytometry analysis of unsorted blood sample. Representative forward, side scattering and histogram are shown. The proportions of negative cells were determined in relation to the isotype controls. The percentages of positive cells are indicated. The blue curve corresponds to the isotype control. Figure S2. Flow cytometry analysis of unsorted liver stromal cells. Representative forward, side scattering and histogram are shown. The proportions of negative cells were determined in relation to the isotype controls. The percentages of positive cells are indicated. The blue curve corresponds to the isotype control. Figure S3. MiRNAs expression analysis in monocytes and Kupffer cells. Full-length of heatmaps are presented.
    [Show full text]
  • The Evolution and Population Genetics of the ALDH2 Locus: Random Genetic Drift, Selection, and Low Levels of Recombination
    doi: 10.1046/j.1529-8817.2003.00060.x The evolution and population genetics of the ALDH2 locus: random genetic drift, selection, and low levels of recombination Hiroki Oota1, Andrew J. Pakstis1, Batsheva Bonne-Tamir2, David Goldman3, Elena Grigorenko4, Sylvester L. B. Kajuna5, Nganyirwa J. Karoma5, Selemani Kungulilo6, Ru-Band Lu7, Kunle Odunsi8, Friday Okonofua9, Olga V. Zhukova10, Judith R. Kidd1 and Kenneth K. Kidd1,∗ 1Department of Genetics, Yale University School of Medicine, 333 Cedar Street, P.O. Box 208005, New Haven, CT 06520-8005, USA 2Department of Human Genetics, Sackler School of Medicine, Tel Aviv University, Tel Aviv, Israel 3Laboratory of Neurogenetics, National Institute of Alcohol Abuse and Alcoholism, Rockville, MD 20852, USA 4Department of Psychology, Yale University, New Haven, CT 06520, USA 5The Hubert Kairuki Memorial University, Dar es Salaam, Tanzania 6Muhimbili University College of Health Sciences, Dar es Salaam, Tanzania 7Department of Psychiatry, Tri-Service General hospital, National Defense Medical Center, Taipei, Taiwan, R.O.C. 8Department of Gynecological Oncology, Roswell Park Cancer Institute, Buffalo, NY 14263, USA 9Department of Obstetrics and Gynecology, Faculty of Medicine, University of Benin, Benin City, Nigeria 10N.I. Vavilov Institute of General Genetics RAS, Moscow, Russia Summary The catalytic deficiency of human aldehyde dehydrogenase 2 (ALDH2) is caused by a nucleotide substitution (G1510A; Glu487Lys) in exon 12 of the ALDH2 locus. This SNP,and four non-coding SNPs, including one in the promoter, span 40 kb of ALDH2; these and one downstream STRP have been tested in 37 worldwide populations. Only four major SNP-defined haplotypes account for almost all chromosomes in all populations.
    [Show full text]
  • DROSOPHILA INFORMATION SERVICE March 1981
    DROSOPHILA INFORMATION SERVICE 56 March 1981 Material contributed by DROSOPHILA WORKERS and arranged by P. W. HEDRICK with bibliography edited by I. H. HERSKOWITZ Material presented here should not be used in publications without the consent of the author. Prepared at the DIVISION OF BIOLOGICAL SCIENCES UNIVERSITY OF KANSAS Lawrence, Kansas 66045 - USA DROSOPHILA INFORMATION SERVICE Number 56 March 1981 Prepared at the Division of Biological Sciences University of Kansas Lawrence, Kansas - USA For information regarding submission of manuscripts or other contributions to Drosophila Information Service, contact P. W. Hedrick, Editor, Division of Biological Sciences, University of Kansas, Lawrence, Kansas 66045 - USA. March 1981 DROSOPHILA INFORMATION SERVICE 56 DIS 56 - I Table of Contents ON THE ORIGIN OF THE DROSOPHILA CONFERENCES L. Sandier ............... 56: vi 1981 DROSOPHILA RESEARCH CONFERENCE .......................... 56: 1 1980 DROSOPHILA RESEARCH CONFERENCE REPORT ...................... 56: 1 ERRATA ........................................ 56: 3 ANNOUNCEMENTS ..................................... 56: 4 HISTORY OF THE HAWAIIAN DROSOPHILA PROJECT. H.T. Spieth ............... 56: 6 RESEARCH NOTES BAND, H.T. Chyniomyza amoena - not a pest . 56: 15 BAND, H.T. Ability of Chymomyza amoena preadults to survive -2 C with no preconditioning . 56: 15 BAND, H.T. Duplication of the delay in emergence by Chymomyza amoena larvae after subzero treatment . 56: 16 BATTERBAM, P. and G.K. CHAMBERS. The molecular weight of a novel phenol oxidase in D. melanogaster . 56: 18 BECK, A.K., R.R. RACINE and F.E. WURGLER. Primary nondisjunction frequencies in seven chromosome substitution stocks of D. melanogaster . 56: 17 BECKENBACH, A.T. Map position of the esterase-5 locus of D. pseudoobscura: a usable marker for "sex-ratio ..
    [Show full text]
  • Supplementary Table S4. FGA Co-Expressed Gene List in LUAD
    Supplementary Table S4. FGA co-expressed gene list in LUAD tumors Symbol R Locus Description FGG 0.919 4q28 fibrinogen gamma chain FGL1 0.635 8p22 fibrinogen-like 1 SLC7A2 0.536 8p22 solute carrier family 7 (cationic amino acid transporter, y+ system), member 2 DUSP4 0.521 8p12-p11 dual specificity phosphatase 4 HAL 0.51 12q22-q24.1histidine ammonia-lyase PDE4D 0.499 5q12 phosphodiesterase 4D, cAMP-specific FURIN 0.497 15q26.1 furin (paired basic amino acid cleaving enzyme) CPS1 0.49 2q35 carbamoyl-phosphate synthase 1, mitochondrial TESC 0.478 12q24.22 tescalcin INHA 0.465 2q35 inhibin, alpha S100P 0.461 4p16 S100 calcium binding protein P VPS37A 0.447 8p22 vacuolar protein sorting 37 homolog A (S. cerevisiae) SLC16A14 0.447 2q36.3 solute carrier family 16, member 14 PPARGC1A 0.443 4p15.1 peroxisome proliferator-activated receptor gamma, coactivator 1 alpha SIK1 0.435 21q22.3 salt-inducible kinase 1 IRS2 0.434 13q34 insulin receptor substrate 2 RND1 0.433 12q12 Rho family GTPase 1 HGD 0.433 3q13.33 homogentisate 1,2-dioxygenase PTP4A1 0.432 6q12 protein tyrosine phosphatase type IVA, member 1 C8orf4 0.428 8p11.2 chromosome 8 open reading frame 4 DDC 0.427 7p12.2 dopa decarboxylase (aromatic L-amino acid decarboxylase) TACC2 0.427 10q26 transforming, acidic coiled-coil containing protein 2 MUC13 0.422 3q21.2 mucin 13, cell surface associated C5 0.412 9q33-q34 complement component 5 NR4A2 0.412 2q22-q23 nuclear receptor subfamily 4, group A, member 2 EYS 0.411 6q12 eyes shut homolog (Drosophila) GPX2 0.406 14q24.1 glutathione peroxidase
    [Show full text]
  • Download Thesis
    This electronic thesis or dissertation has been downloaded from the King’s Research Portal at https://kclpure.kcl.ac.uk/portal/ Optimising the use of Azathioprine in the treatment of Inflammatory Bowel Disease Smith, Melissa Ann Awarding institution: King's College London The copyright of this thesis rests with the author and no quotation from it or information derived from it may be published without proper acknowledgement. END USER LICENCE AGREEMENT Unless another licence is stated on the immediately following page this work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International licence. https://creativecommons.org/licenses/by-nc-nd/4.0/ You are free to copy, distribute and transmit the work Under the following conditions: Attribution: You must attribute the work in the manner specified by the author (but not in any way that suggests that they endorse you or your use of the work). Non Commercial: You may not use this work for commercial purposes. No Derivative Works - You may not alter, transform, or build upon this work. Any of these conditions can be waived if you receive permission from the author. Your fair dealings and other rights are in no way affected by the above. Take down policy If you believe that this document breaches copyright please contact [email protected] providing details, and we will remove access to the work immediately and investigate your claim. Download date: 29. Sep. 2021 Optimising the use of Azathioprine in the treatment of Inflammatory Bowel Disease Dr Melissa Ann Smith MD (Res) 2013 MD thesis Azathioprine in IBD Melissa Ann Smith Table of Contents Table of Contents ...........................................................................................................................
    [Show full text]
  • Retinoid Metabolism in the Rat Small Intestine
    Downloaded from https://www.cambridge.org/core British Journal of Nutrition (2005), 93, 59–63 DOI: 10.1079/BJN20041306 q The Authors 2005 Retinoid metabolism in the rat small intestine . IP address: Simmy Thomas, Ramamoorthy Prabhu and Kunissery A. Balasubramanian* 170.106.40.139 The Wellcome Trust Research Laboratory, Department of Gastrointestinal Sciences, Christian Medical College, Vellore-632004, India (Received 1 April 2004 – Revised 27 July 2004 – Accepted 21 September 2004) , on 27 Sep 2021 at 00:14:50 Vitamin A (retinol) is essential for epithelial cell growth, differentiation and proliferation. The absorption of retinol occurs in the small intestine, and the metabolism of this vitamin is not well studied in this organ. The intestinal epithelium has a high rate of cell proliferation and differentiation, and the present study looked at the level of retinoids and metabolizing enzymes involved in their interconversion along the villus–crypt axis under normal conditions. Intes- tine was removed from control rats, and enterocytes at various stages of maturation and differentiation were quantified by the metal chelation method. Using HPLC, various retinoid concentrations in the cell homogenate and the metabolizing enzymes in the cytosol were quantified. The proliferating crypt cells , subject to the Cambridge Core terms of use, available at were found to have a higher level of retinoic acid as well as of the enzymes involved in its formation, such as retinaldehyde oxidase and retinol dehydro- genase, compared with the villus cells, suggesting a possible role for this compound in intestinal epithelial cell proliferation and differentiation. The high level of retinol and high retinaldehyde reductase activity in the villus cells suggest the important role played by this enzyme in the conversion of dietary b- carotene to retinol via retinaldehyde.
    [Show full text]