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Contig Protein Description Symbol Anterior Posterior Ratio
Table S2. List of proteins detected in anterior and posterior intestine pooled samples. Data on protein expression are mean ± SEM of 4 pools fed the experimental diets. The number of the contig in the Sea Bream Database (http://nutrigroup-iats.org/seabreamdb) is indicated. Contig Protein Description Symbol Anterior Posterior Ratio Ant/Pos C2_6629 1,4-alpha-glucan-branching enzyme GBE1 0.88±0.1 0.91±0.03 0.98 C2_4764 116 kDa U5 small nuclear ribonucleoprotein component EFTUD2 0.74±0.09 0.71±0.05 1.03 C2_299 14-3-3 protein beta/alpha-1 YWHAB 1.45±0.23 2.18±0.09 0.67 C2_268 14-3-3 protein epsilon YWHAE 1.28±0.2 2.01±0.13 0.63 C2_2474 14-3-3 protein gamma-1 YWHAG 1.8±0.41 2.72±0.09 0.66 C2_1017 14-3-3 protein zeta YWHAZ 1.33±0.14 4.41±0.38 0.30 C2_34474 14-3-3-like protein 2 YWHAQ 1.3±0.11 1.85±0.13 0.70 C2_4902 17-beta-hydroxysteroid dehydrogenase 14 HSD17B14 0.93±0.05 2.33±0.09 0.40 C2_3100 1-acylglycerol-3-phosphate O-acyltransferase ABHD5 ABHD5 0.85±0.07 0.78±0.13 1.10 C2_15440 1-phosphatidylinositol phosphodiesterase PLCD1 0.65±0.12 0.4±0.06 1.65 C2_12986 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-1 PLCD1 0.76±0.08 1.15±0.16 0.66 C2_4412 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2 PLCG2 1.13±0.08 2.08±0.27 0.54 C2_3170 2,4-dienoyl-CoA reductase, mitochondrial DECR1 1.16±0.1 0.83±0.03 1.39 C2_1520 26S protease regulatory subunit 10B PSMC6 1.37±0.21 1.43±0.04 0.96 C2_4264 26S protease regulatory subunit 4 PSMC1 1.2±0.2 1.78±0.08 0.68 C2_1666 26S protease regulatory subunit 6A PSMC3 1.44±0.24 1.61±0.08 -
Endogenous Protein Interactome of Human UDP-Glucuronosyltransferases Exposed by Untargeted Proteomics
ORIGINAL RESEARCH published: 03 February 2017 doi: 10.3389/fphar.2017.00023 Endogenous Protein Interactome of Human UDP-Glucuronosyltransferases Exposed by Untargeted Proteomics Michèle Rouleau, Yannick Audet-Delage, Sylvie Desjardins, Mélanie Rouleau, Camille Girard-Bock and Chantal Guillemette * Pharmacogenomics Laboratory, Canada Research Chair in Pharmacogenomics, Faculty of Pharmacy, Centre Hospitalier Universitaire de Québec Research Center, Laval University, Québec, QC, Canada The conjugative metabolism mediated by UDP-glucuronosyltransferase enzymes (UGTs) significantly influences the bioavailability and biological responses of endogenous molecule substrates and xenobiotics including drugs. UGTs participate in the regulation of cellular homeostasis by limiting stress induced by toxic molecules, and by Edited by: controlling hormonal signaling networks. Glucuronidation is highly regulated at genomic, Yuji Ishii, transcriptional, post-transcriptional and post-translational levels. However, the UGT Kyushu University, Japan protein interaction network, which is likely to influence glucuronidation, has received Reviewed by: little attention. We investigated the endogenous protein interactome of human UGT1A Ben Lewis, Flinders University, Australia enzymes in main drug metabolizing non-malignant tissues where UGT expression is Shinichi Ikushiro, most prevalent, using an unbiased proteomics approach. Mass spectrometry analysis Toyama Prefectural University, Japan of affinity-purified UGT1A enzymes and associated protein complexes in liver, -
PHASE II DRUG METABOLIZING ENZYMES Petra Jancovaa*, Pavel Anzenbacherb,Eva Anzenbacherova
Biomed Pap Med Fac Univ Palacky Olomouc Czech Repub. 2010 Jun; 154(2):103–116. 103 © P. Jancova, P. Anzenbacher, E. Anzenbacherova PHASE II DRUG METABOLIZING ENZYMES Petra Jancovaa*, Pavel Anzenbacherb, Eva Anzenbacherovaa a Department of Medical Chemistry and Biochemistry, Faculty of Medicine and Dentistry, Palacky University, Hnevotinska 3, 775 15 Olomouc, Czech Republic b Department of Pharmacology, Faculty of Medicine and Dentistry, Palacky University, Hnevotinska 3, 775 15 Olomouc E-mail: [email protected] Received: March 29, 2010; Accepted: April 20, 2010 Key words: Phase II biotransformation/UDP-glucuronosyltransferases/Sulfotransferases, N-acetyltransferases/Glutathione S-transferases/Thiopurine S-methyl transferase/Catechol O-methyl transferase Background. Phase II biotransformation reactions (also ‘conjugation reactions’) generally serve as a detoxifying step in drug metabolism. Phase II drug metabolising enzymes are mainly transferases. This review covers the major phase II enzymes: UDP-glucuronosyltransferases, sulfotransferases, N-acetyltransferases, glutathione S-transferases and methyltransferases (mainly thiopurine S-methyl transferase and catechol O-methyl transferase). The focus is on the presence of various forms, on tissue and cellular distribution, on the respective substrates, on genetic polymorphism and finally on the interspecies differences in these enzymes. Methods and Results. A literature search using the following databases PubMed, Science Direct and EBSCO for the years, 1969–2010. Conclusions. Phase II drug metabolizing enzymes play an important role in biotransformation of endogenous compounds and xenobiotics to more easily excretable forms as well as in the metabolic inactivation of pharmacologi- cally active compounds. Reduced metabolising capacity of Phase II enzymes can lead to toxic effects of clinically used drugs. Gene polymorphism/ lack of these enzymes may often play a role in several forms of cancer. -
Endogenous Protein Interactome of Human
Human UGT1A interaction network 1 Endogenous protein interactome of human UDP- 2 glucuronosyltransferases exposed by untargeted proteomics 3 4 5 Michèle Rouleau, Yannick Audet-Delage, Sylvie Desjardins, Mélanie Rouleau, Camille Girard- 6 Bock and Chantal Guillemette* 7 8 Pharmacogenomics Laboratory, Canada Research Chair in Pharmacogenomics, Centre 9 Hospitalier Universitaire (CHU) de Québec Research Center and Faculty of Pharmacy, Laval 10 University, G1V 4G2, Québec, Canada 11 12 13 14 15 *Corresponding author: 16 Chantal Guillemette, Ph.D. 17 Canada Research Chair in Pharmacogenomics 18 Pharmacogenomics Laboratory, CHU de Québec Research Center, R4720 19 2705 Boul. Laurier, Québec, Canada, G1V 4G2 20 Tel. (418) 654-2296 Fax. (418) 654-2298 21 E-mail: [email protected] 22 23 24 25 26 27 28 29 30 31 32 Running title: Human UGT1A interaction network 33 1 Human UGT1A interaction network 1 Number of: Pages: 26 2 Tables: 2 3 Figures: 5 4 References: 62 5 Supplemental Tables: 7 6 Supplemental Figures: 5 7 8 Number of words: Total: 7882 9 Abstract: 229 10 Introduction: 549 11 Results: 1309 12 Discussion: 1403 13 Body Text: 3261 14 15 16 17 18 Abbreviations: AP: affinity purification; UGT, UDP-glucuronosyltransferases; IP, immuno- 19 precipitation; PPIs, protein-protein interactions; UDP-GlcA, Uridine diphospho-glucuronic acid; 20 ER, endoplasmic reticulum; MS, mass spectrometry. 21 22 Keywords: UGT; Proteomics; Protein-protein interaction; Affinity purification; Mass 23 spectrometry; Metabolism; Human tissues; 24 2 Human UGT1A interaction network 1 ABSTRACT 2 3 The conjugative metabolism mediated by UDP-glucuronosyltransferase enzymes (UGTs) 4 significantly influences the bioavailability and biological responses of endogenous molecule 5 substrates and xenobiotics including drugs. -
Straightjacket/Α2δ3 Deregulation Is Associated with Cardiac Conduction Defects in Myotonic Dystrophy Type 1
bioRxiv preprint doi: https://doi.org/10.1101/431569; this version posted October 2, 2018. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Straightjacket/α2δ3 deregulation is associated with cardiac conduction defects in Myotonic Dystrophy type 1 Emilie Plantié1, Masayuki Nakamori2, Yoan Renaud3, Aline Huguet4, Caroline Choquet5, Cristiana Dondi1, Lucile Miquerol5, Masanori Takahashi6, Geneviève Gourdon4, Guillaume Junion1, Teresa Jagla1, Monika Zmojdzian1* and Krzysztof Jagla1* 1 GReD, CNRS UMR6293, INSERM U1103, University of Clermont Auvergne, 28, Place Henri Dunant, 63000 Clermont-Ferrand, France 2 Department of Neurology, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan 3 BYONET (www.byonet.fr) 4 Imagine Institute, Inserm UMR1163, 24, boulevard de Montparnasse, 75015 Paris, France 5 Aix-Marseille University, CNRS UMR7288, IBDM Luminy Campus Case 907, 13288 Marseille cedex 9, France 6 Department of Functional Diagnostic Science, Osaka University Graduate School of Medicine, 1-7 Yamadaoka, Suita, Osaka 565-0871, Japan • Correspondence to: Krzysztof Jagla [email protected] and Monika Zmojdzian [email protected] tel. +33 473178181; GReD, CNRS UMR6293, INSERM U1103, University of Clermont Auvergne, 28, Place Henri Dunant, 63000 Clermont-Ferrand, France 1 bioRxiv preprint doi: https://doi.org/10.1101/431569; this version posted October 2, 2018. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. ABSTRACT Cardiac conduction defects decrease life expectancy in myotonic dystrophy type 1 (DM1), a complex toxic CTG repeat disorder involving misbalance between two RNA- binding factors, MBNL1 and CELF1. -
Kidney V-Atpase-Rich Cell Proteome Database
A comprehensive list of the proteins that are expressed in V-ATPase-rich cells harvested from the kidneys based on the isolation by enzymatic digestion and fluorescence-activated cell sorting (FACS) from transgenic B1-EGFP mice, which express EGFP under the control of the promoter of the V-ATPase-B1 subunit. In these mice, type A and B intercalated cells and connecting segment principal cells of the kidney express EGFP. The protein identification was performed by LC-MS/MS using an LTQ tandem mass spectrometer (Thermo Fisher Scientific). For questions or comments please contact Sylvie Breton ([email protected]) or Mark A. Knepper ([email protected]). -
Studies on Bilirubin and Steroid Glucuronidation
Centre for Drug research Division of Pharmaceutical Chemistry Faculty of Pharmacy University of Helsinki Finland UDP-GLUCURONOSYLTRANSFERASES IN SICKNESS AND HEALTH STUDIES ON BILIRUBIN AND STEROID GLUCURONIDATION Nina Sneitz ACADEMIC DISSERTATION To be presented, with the permission of the Faculty of Pharmacy of the University of Helsinki, for public examination in Auditorium 1, Korona Information Centre, on 25 October 2013, at 12 noon. Helsinki 2013 Supervisor: Dr. Moshe Finel Centre for Drug Research (CDR) Faculty of Pharmacy University of Helsinki Finland Reviewers: Professor Peter Mackenzie Department of Clinical Pharmacology School of Medicine Flinders University Australia Professor Hannu Raunio Faculty of Health Sciences School of Pharmacy University of Eastern Finland Finland Opponent: Professor Philip Lazarus Department of Pharmaceutical Sciences College of Pharmacy Washington State University College of Pharmacy USA © Nina Sneitz 2013 ISBN 978-952-10-9292-3 (Paperback) ISBN 978-952-10-9293-0 (PDF) ISSN 1799-7372 http://ethesis.helsinki.fi/ Helsinki University Printing House Helsinki 2013 CONTENTS Abstract 5 Acknowledgements 7 List of original publications 8 Abbreviations 9 1 Introduction 10 2 Review of the Literature 12 2.1 UDP-glucuronosyltransferases in brief 12 2.2 Bilirubin metabolism and Familial hyperbilirubinemias 15 2.2.1 Bilirubin: properties and metabolism 15 2.2.2 Gilbert syndrome 17 2.2.3 Crigler-Najjar syndromes 18 2.2.3.1 Current therapy for Crigler-Najjar syndrome 20 2.2.3.2 Gene therapy in treatment of Crigler-Najjar syndrome 20 2.3 Steroid hormones and their metabolism 22 2.3.1 Glucuronidation of steroid hormones 24 2.3.2 Steroids and health 26 2.4 Steroid glucuronidation and UGT structure 28 3 Aims of the study 30 4 Materials and Methods 31 4.1 Materials 31 4.1.1. -
UCLA Electronic Theses and Dissertations
UCLA UCLA Electronic Theses and Dissertations Title Disease-specific differences in glycosylation of mouse and human skeletal muscle Permalink https://escholarship.org/uc/item/73v762qp Author McMorran, Brian James Publication Date 2017 Peer reviewed|Thesis/dissertation eScholarship.org Powered by the California Digital Library University of California UNIVERSITY OF CALIFORNIA Los Angeles Disease-specific differences in glycosylation of mouse and human skeletal muscle A dissertation submitted in partial satisfaction of the requirements for the Degree of Philosophy in Cellular and Molecular Pathology by Brian James McMorran 2017 © Copyright by Brian James McMorran 2017 ABSTRACT OF THE DISSERTATION Disease-specific differences in glycosylation of mouse and human skeletal muscle by Brian James McMorran Doctor of Philosophy in Cellular and Molecular Pathology University of California, Los Angeles, 2017 Professor Linda G. Baum, Chair Proper glycosylation of proteins at the muscle cell membrane, or sarcolemma, is critical for proper muscle function. The laminin receptor alpha-dystroglycan (α-DG) is heavily glycosylated and mutations in 24 genes involved in proper α-DG glycosylation have been identified as causing various forms of congenital muscular dystrophy. While work over the past decade has elucidated the structure bound by laminin and the enzymes required for its creation, very little is known about muscle glycosylation outside of α-DG glycosylation. The modification of glycan structures with terminal GalNAc residues at the rodent neuromuscular junction (NMJ) has remained the focus of work in mouse muscle glycosylation, while qualitative lectin histochemistry studies performed three decades ago represent the majority of human muscle glycosylation research. This thesis quantifies differentiation-, species-, and disease-specific differences in mouse and human skeletal muscle glycosylation. -
Evaluation of Vitamin D Biosynthesis and Pathway Target Genes Reveals
UC Irvine UC Irvine Previously Published Works Title Evaluation of vitamin D biosynthesis and pathway target genes reveals UGT2A1/2 and EGFR polymorphisms associated with epithelial ovarian cancer in African American Women. Permalink https://escholarship.org/uc/item/36m4z61b Journal Cancer medicine, 8(5) ISSN 2045-7634 Authors Grant, Delores J Manichaikul, Ani Alberg, Anthony J et al. Publication Date 2019-05-01 DOI 10.1002/cam4.1996 License https://creativecommons.org/licenses/by/4.0/ 4.0 Peer reviewed eScholarship.org Powered by the California Digital Library University of California Received: 31 July 2018 | Revised: 3 December 2018 | Accepted: 8 January 2019 DOI: 10.1002/cam4.1996 ORIGINAL RESEARCH Evaluation of vitamin D biosynthesis and pathway target genes reveals UGT2A1/2 and EGFR polymorphisms associated with epithelial ovarian cancer in African American Women Delores J. Grant1 | Ani Manichaikul2 | Anthony J. Alberg3 | Elisa V. Bandera4 | Jill Barnholtz‐Sloan5 | Melissa Bondy6 | Michele L. Cote7 | Ellen Funkhouser8 | Patricia G. Moorman9 | Lauren C. Peres2 | Edward S. Peters10 | Ann G. Schwartz7 | Paul D. Terry11 | Xin‐Qun Wang12 | Temitope O. Keku13 | Cathrine Hoyo14 | Andrew Berchuck15 | Dale P. Sandler16 | Jack A. Taylor16 | Katie M. O’Brien16 | Digna R. Velez Edwards17 | Todd L. Edwards18 | Alicia Beeghly‐Fadiel19 | Nicolas Wentzensen20 | Celeste Leigh Pearce21,22 | Anna H. Wu22 | Alice S. Whittemore23,24 | Valerie McGuire23 | Weiva Sieh25,26 | Joseph H. Rothstein25,26 | Francesmary Modugno27,28,29 | Roberta Ness30 | Kirsten Moysich31 | Mary Anne Rossing32,33 | Jennifer A. Doherty34 | Thomas A. Sellers35 | Jennifer B. Permuth‐Way35 | Alvaro N. Monteiro35 | Douglas A. Levine36,37 | Veronica Wendy Setiawan38 | Christopher A. Haiman38 | Loic LeMarchand39 | Lynne R. -
Cam41996 Am.Pdf
Evaluation of vitamin D biosynthesis and pathway target genes reveals UGT2A1/2 and EGFR polymorphisms associated with epithelial ovarian cancer in African American Women RUNNING TITLE: Genetic association with variants in the vitamin D pathway KEYWORDS: ovarian cancer, genetic association, vitamin D pathway, African ancestry risk Delores J. Grant1, Ani Manichaikul2, Anthony J. Alberg3, Elisa V. Bandera4, Jill Barnholtz-Sloan5, Melissa Bondy6, Michele L. Cote7, Ellen Funkhouser8, Patricia G. Moorman9, Lauren C. Peres2, Edward S. Peters10, Ann G. Schwartz7, Paul D. Terry11, Xin-Qun Wang2, Temitope O. Keku12, Cathrine Hoyo13, Andrew Berchuck14, Dale P. Sandler15, Jack A. Taylor15, Katie M. O’Brien16, Digna R. Velez Edwards17, Todd L. Edwards18, Alicia Beeghly-Fadiel19, Nicolas Wentzensen20, Celeste Leigh Pearce21,22, Anna H. Wu22, Alice S. Whittemore23,24, Valerie McGuire23, Weiva Sieh25,26, Joseph H. Rothstein25,26, Francesmary Modugno27,28,29, Roberta Ness30, Kirsten Moysich31, Mary Anne Rossing32,33, Jennifer A. Doherty34, Thomas A. Sellers35, Jennifer B. Permuth-Way35, Alvaro N. Monteiro35, Douglas A. Levine36,37, Veronica Wendy Setiawan38, Christopher A. Haiman38, Loic LeMarchand39, Lynne R. Wilkens40, Beth Y. Karlan41, Usha Menon42, Susan Ramus43,44, Simon Gayther45,46, Aleksandra Gentry-Maharaj42, Kathryn L. Terry47,48, Daniel W. Cramer47,48, Ellen L. Goode49, Melissa C. Larson50, Scott H. Kaufmann51, Rikki Cannioto52, Kunle Odunsi53, John L. Etter31, Ruea-Yea Huang54, Marcus Q. Bernardini55, Alicia A. Tone55, Taymaa May55, Marc T. Goodman56,57, Pamela J. Thompson56, Michael E. Carney58, Shelley S. Tworoger59, Elizabeth M. Poole60, Diether Lambrechts61,62, Ignace Vergote63, Adriaan Vanderstichele63, Els Van Nieuwenhuysen63, Hoda Anton-Culver64, Argyrios Ziogas65, James D. Brenton66, Line Bjorge67,68, Helga B. -
1 Identifying Clinically-Relevant Population-Specific
Identifying Clinically-Relevant Population-Specific IsomiRs in African Americans and European Americans with Lung Cancer Thesis highlights ● Lung cancer is the leading cause of cancer-related deaths in the United States (U.S.) with over 139,000 deaths per year. African Americans (AAs) have a higher mortality and lower 5-year survival rate than European Americans (EAs). ● AAs smoke less than EAs. When they do smoke, AAs choose menthol cigarettes more than EAs (88.5% vs. 25.7%). ● Smoking-associated biomarkers have been explored at the genomic, metabolomic, and transcriptomic level, providing evidence for miRNA variants (isomiRs) as potential regulators of menthol metabolizing enzymes (MMEs). ● The miRNA and candidate isomiR, miR-374b-5p|3’a-1, had significantly higher expression in AAs that correlated with lower CYP1B1 and UGT2B4 expression. ● The miRNA and candidate isomiR, miR-374b-5p|3’a-1, had significantly higher expression in AAs upon menthol exposure. This did not correlate with lower CYP1B1 and UGT2B4 expression, suggesting other miRNAs, isomiRs, or menthol metabolizing enzymes may be involved. ● Adopting a precision medicine approach to upregulate miR-374b isomiRs may preferentially benefit AAs, and help to reduce mortality and survival disparities. Honors Thesis Proposal by Savanna Touré (’21) For the Academic Year (2020-2021) Advisor: Dr. Khadijah A. Mitchell Committee: Drs. Elaine Reynolds and Daniel Griffith 1 I. TABLE OF CONTENTS II. Biographical Sketch……………………………………………………………………….5 III. Abstract…………………………………………………………………………………....7 IV. Introduction……………………………………………………………………….……….8 A. Racial disparities in lung cancer mortality and survival B. Known behavioral determinants of racial disparities in lung cancer: smoking C. Known biological determinants of racial disparities in lung cancer: genomic and metabolomic level D. -
(UGT) Genes in Human Cancers and Their Association with Clinical Outcomes
cancers Article The Expression Profiles and Deregulation of UDP-Glycosyltransferase (UGT) Genes in Human Cancers and Their Association with Clinical Outcomes Dong Gui Hu 1,* , Shashikanth Marri 2, Peter I. Mackenzie 1, Julie-Ann Hulin 1, Ross A. McKinnon 1 and Robyn Meech 1 1 Dicipline of Clinical Pharmacology, College of Medicine and Public Health, Flinders University, Bedford Park, SA 5042, Australia; peter.mackenzie@flinders.edu.au (P.I.M.); julieann.hulin@flinders.edu.au (J.-A.H.); ross.mckinnon@flinders.edu.au (R.A.M.); robyn.meech@flinders.edu.au (R.M.) 2 Dicipline of Molecular Medicine and Pathology, College of Medicine and Public Health, Flinders University, Bedford Park, SA 5042, Australia; shashikanth.marri@flinders.edu.au * Correspondence: donggui.hu@flinders.edu.au; Tel.: +61-08-82043085 Simple Summary: The human UDP-glycosyltransferase (UGT) superfamily plays a critical role in the metabolism of numerous endogenous and exogenous small lipophilic compounds, including carcinogens, drugs, and bioactive molecules with pro- or anti-cancer activity. Previous studies have documented the expression of UGT genes in several cancers derived from drug-metabolizing organs (e.g., liver, colon, kidney). The present study represents the first to comprehensively assess the expression profiles of UGT genes and their impact on patient survival in nearly 30 different cancers Citation: Hu, D.G.; Marri, S.; primarily derived from non-drug-metabolizing organs. Briefly, our comprehensive analysis of the Mackenzie, P.I.; Hulin, J.-A.; transcriptomic (RNAseq) and clinical datasets of 9514 patients from 33 different cancers shows McKinnon, R.A.; Meech, R. The the widespread expression of UGT genes, indicative of active drug metabolism within the tumor Expression Profiles and Deregulation through the UGT conjugation pathway.