Tbamitchodral L Alizaion of the 4Aminobutyrate-2-&Oxoglutarate
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Alternative Acetate Production Pathways in Chlamydomonas Reinhardtii During Dark Anoxia and the Dominant Role of Chloroplasts in Fermentative Acetate Productionw
This article is a Plant Cell Advance Online Publication. The date of its first appearance online is the official date of publication. The article has been edited and the authors have corrected proofs, but minor changes could be made before the final version is published. Posting this version online reduces the time to publication by several weeks. Alternative Acetate Production Pathways in Chlamydomonas reinhardtii during Dark Anoxia and the Dominant Role of Chloroplasts in Fermentative Acetate ProductionW Wenqiang Yang,a,1 Claudia Catalanotti,a Sarah D’Adamo,b Tyler M. Wittkopp,a,c Cheryl J. Ingram-Smith,d Luke Mackinder,a Tarryn E. Miller,b Adam L. Heuberger,e Graham Peers,f Kerry S. Smith,d Martin C. Jonikas,a Arthur R. Grossman,a and Matthew C. Posewitzb a Carnegie Institution for Science, Department of Plant Biology, Stanford, California 94305 b Colorado School of Mines, Department of Chemistry and Geochemistry, Golden, Colorado 80401 c Stanford University, Department of Biology, Stanford, California 94305 d Clemson University, Department of Genetics and Biochemistry, Clemson, South Carolina 29634 e Colorado State University, Proteomics and Metabolomics Facility, Fort Collins, Colorado 80523 f Colorado State University, Department of Biology, Fort Collins, Colorado 80523 ORCID ID: 0000-0001-5600-4076 (W.Y.) Chlamydomonas reinhardtii insertion mutants disrupted for genes encoding acetate kinases (EC 2.7.2.1) (ACK1 and ACK2) and a phosphate acetyltransferase (EC 2.3.1.8) (PAT2, but not PAT1) were isolated to characterize fermentative acetate production. ACK1 and PAT2 were localized to chloroplasts, while ACK2 and PAT1 were shown to be in mitochondria. -
Causes and Evaluation of Mildly Elevated Liver Transaminase Levels ROBERT C
Causes and Evaluation of Mildly Elevated Liver Transaminase Levels ROBERT C. OH, LTC, MC, USA, and THOMAS R. HUSTEAD, LTC, MC, USA Tripler Army Medical Center Family Medicine Residency Program, Honolulu, Hawaii Mild elevations in levels of the liver enzymes alanine transaminase and aspartate transaminase are commonly dis- covered in asymptomatic patients in primary care. Evidence to guide the diagnostic workup is limited. If the history and physical examination do not suggest a cause, a stepwise evaluation should be initiated based on the prevalence of diseases that cause mild elevations in transaminase levels. The most common cause is nonalcoholic fatty liver disease, which can affect up to 30 percent of the population. Other common causes include alcoholic liver disease, medication- associated liver injury, viral hepatitis (hepatitis B and C), and hemochromatosis. Less common causes include α1-antitrypsin deficiency, autoimmune hepatitis, and Wilson disease. Extrahepatic conditions (e.g., thyroid disorders, celiac disease, hemolysis, muscle disorders) can also cause elevated liver transaminase levels. Initial testing should include a fasting lipid profile; measurement of glucose, serum iron, and ferritin; total iron-binding capacity; and hepa- titis B surface antigen and hepatitis C virus antibody testing. If test results are normal, a trial of lifestyle modification with observation or further testing for less common causes is appropriate. Additional testing may include ultrasonog- raphy; measurement of α1-antitrypsin and ceruloplasmin; serum protein electrophoresis; and antinuclear antibody, smooth muscle antibody, and liver/kidney microsomal antibody type 1 testing. Referral for further evaluation and possible liver biopsy is recommended if transaminase levels remain elevated for six months or more. -
Mutation of the Fumarase Gene in Two Siblings with Progressive Encephalopathy and Fumarase Deficiency T
Mutation of the Fumarase Gene in Two Siblings with Progressive Encephalopathy and Fumarase Deficiency T. Bourgeron,* D. Chretien,* J. Poggi-Bach, S. Doonan,' D. Rabier,* P. Letouze,I A. Munnich,* A. R6tig,* P. Landneu,* and P. Rustin* *Unite de Recherches sur les Handicaps Genetiques de l'Enfant, INSERM U393, Departement de Pediatrie et Departement de Biochimie, H6pital des Enfants-Malades, 149, rue de Sevres, 75743 Paris Cedex 15, France; tDepartement de Pediatrie, Service de Neurologie et Laboratoire de Biochimie, Hopital du Kremlin-Bicetre, France; IFaculty ofScience, University ofEast-London, UK; and IService de Pediatrie, Hopital de Dreux, France Abstract chondrial enzyme (7). Human tissue fumarase is almost We report an inborn error of the tricarboxylic acid cycle, fu- equally distributed between the mitochondria, where the en- marase deficiency, in two siblings born to first cousin parents. zyme catalyzes the reversible hydration of fumarate to malate They presented with progressive encephalopathy, dystonia, as a part ofthe tricarboxylic acid cycle, and the cytosol, where it leucopenia, and neutropenia. Elevation oflactate in the cerebro- is involved in the metabolism of the fumarate released by the spinal fluid and high fumarate excretion in the urine led us to urea cycle. The two isoenzymes have quite homologous struc- investigate the activities of the respiratory chain and of the tures. In rat liver, they differ only by the acetylation of the Krebs cycle, and to finally identify fumarase deficiency in these NH2-terminal amino acid of the cytosolic form (8). In all spe- two children. The deficiency was profound and present in all cies investigated so far, the two isoenzymes have been found to tissues investigated, affecting the cytosolic and the mitochon- be encoded by a single gene (9,10). -
Anti-Inflammatory Role of Curcumin in LPS Treated A549 Cells at Global Proteome Level and on Mycobacterial Infection
Anti-inflammatory Role of Curcumin in LPS Treated A549 cells at Global Proteome level and on Mycobacterial infection. Suchita Singh1,+, Rakesh Arya2,3,+, Rhishikesh R Bargaje1, Mrinal Kumar Das2,4, Subia Akram2, Hossain Md. Faruquee2,5, Rajendra Kumar Behera3, Ranjan Kumar Nanda2,*, Anurag Agrawal1 1Center of Excellence for Translational Research in Asthma and Lung Disease, CSIR- Institute of Genomics and Integrative Biology, New Delhi, 110025, India. 2Translational Health Group, International Centre for Genetic Engineering and Biotechnology, New Delhi, 110067, India. 3School of Life Sciences, Sambalpur University, Jyoti Vihar, Sambalpur, Orissa, 768019, India. 4Department of Respiratory Sciences, #211, Maurice Shock Building, University of Leicester, LE1 9HN 5Department of Biotechnology and Genetic Engineering, Islamic University, Kushtia- 7003, Bangladesh. +Contributed equally for this work. S-1 70 G1 S 60 G2/M 50 40 30 % of cells 20 10 0 CURI LPSI LPSCUR Figure S1: Effect of curcumin and/or LPS treatment on A549 cell viability A549 cells were treated with curcumin (10 µM) and/or LPS or 1 µg/ml for the indicated times and after fixation were stained with propidium iodide and Annexin V-FITC. The DNA contents were determined by flow cytometry to calculate percentage of cells present in each phase of the cell cycle (G1, S and G2/M) using Flowing analysis software. S-2 Figure S2: Total proteins identified in all the three experiments and their distribution betwee curcumin and/or LPS treated conditions. The proteins showing differential expressions (log2 fold change≥2) in these experiments were presented in the venn diagram and certain number of proteins are common in all three experiments. -
Citric Acid Cycle
CHEM464 / Medh, J.D. The Citric Acid Cycle Citric Acid Cycle: Central Role in Catabolism • Stage II of catabolism involves the conversion of carbohydrates, fats and aminoacids into acetylCoA • In aerobic organisms, citric acid cycle makes up the final stage of catabolism when acetyl CoA is completely oxidized to CO2. • Also called Krebs cycle or tricarboxylic acid (TCA) cycle. • It is a central integrative pathway that harvests chemical energy from biological fuel in the form of electrons in NADH and FADH2 (oxidation is loss of electrons). • NADH and FADH2 transfer electrons via the electron transport chain to final electron acceptor, O2, to form H2O. Entry of Pyruvate into the TCA cycle • Pyruvate is formed in the cytosol as a product of glycolysis • For entry into the TCA cycle, it has to be converted to Acetyl CoA. • Oxidation of pyruvate to acetyl CoA is catalyzed by the pyruvate dehydrogenase complex in the mitochondria • Mitochondria consist of inner and outer membranes and the matrix • Enzymes of the PDH complex and the TCA cycle (except succinate dehydrogenase) are in the matrix • Pyruvate translocase is an antiporter present in the inner mitochondrial membrane that allows entry of a molecule of pyruvate in exchange for a hydroxide ion. 1 CHEM464 / Medh, J.D. The Citric Acid Cycle The Pyruvate Dehydrogenase (PDH) complex • The PDH complex consists of 3 enzymes. They are: pyruvate dehydrogenase (E1), Dihydrolipoyl transacetylase (E2) and dihydrolipoyl dehydrogenase (E3). • It has 5 cofactors: CoASH, NAD+, lipoamide, TPP and FAD. CoASH and NAD+ participate stoichiometrically in the reaction, the other 3 cofactors have catalytic functions. -
Complex Hereditary Spastic Paraplegia Associated with Episodic
Tozawa et al. Human Genome Variation (2021) 8:4 https://doi.org/10.1038/s41439-021-00136-y Human Genome Variation DATA REPORT Open Access Complex hereditary spastic paraplegia associated with episodic visual loss caused by ACO2 variants Takenori Tozawa1,2,AkiraNishimura3, Tamaki Ueno2,4, Akane Shikata5, Yoshihiro Taura1,TakeshiYoshida 6, Naoko Nakagawa7, Takahito Wada 7, Shinji Kosugi7, Tomoko Uehara8, Toshiki Takenouchi 9, Kenjiro Kosaki8 and Tomohiro Chiyonobu1 Abstract Most patients with homozygous or compound heterozygous pathogenic ACO2 variants present with muscular hypotonia features, namely, infantile cerebellar-retinal degeneration. Recently, two studies reported rare familial cases of ACO2 variants presenting as complex hereditary spastic paraplegia (HSP) with broad clinical spectra. Here, we report the case of a 20-year-old Japanese woman with complex HSP caused by compound heterozygous ACO2 variants, revealing a new phenotype of episodic visual loss during febrile illness. The ACO2 gene on chromosome 22 encodes the aco- variants in the ACO2 gene presenting as complex her- nitase 2 (ACO2) protein in the mitochondrial matrix; editary spastic paraplegia (HSP) with a new phenotype of ACO2 catalyzes the stereospecific isomerization of citrate episodic visual loss after every febrile infection and pro- to isocitrate in the tricarboxylic acid (TCA) cycle1. gressive optic atrophy. This is the third familial report and ACO2 fi fi 1234567890():,; 1234567890():,; 1234567890():,; 1234567890():,; Pathogenic variants were rst reported in eight the rst Asian patient with complex HSP caused by individuals from two Arab families, and they had infantile pathogenic ACO2 variants. cerebellar-retinal degeneration (ICRD, OMIM#614559)2. The proband was born to nonconsanguineous healthy Subsequently, ~20 cases of pathogenic homozygous or parents at 38 weeks gestational age after unremarkable compound heterozygous ACO2 variants have been delivery. -
Microrna–Target Pairs in the Rat Kidney Identified by Microrna Microarray, Proteomic, and Bioinformatic Analysis Zhongmin Tian,1,2 Andrew S
Downloaded from genome.cshlp.org on October 1, 2021 - Published by Cold Spring Harbor Laboratory Press Letter MicroRNA–target pairs in the rat kidney identified by microRNA microarray, proteomic, and bioinformatic analysis Zhongmin Tian,1,2 Andrew S. Greene,1,2 Jennifer L. Pietrusz,1 Isaac R. Matus,2 and Mingyu Liang1,3 1Department of Physiology, Medical College of Wisconsin, Milwaukee, Wisconsin 53226, USA; 2Biotechnology and Biomedical Engineering Center, Medical College of Wisconsin, Milwaukee, Wisconsin 53226, USA Mammalian genomes contain several hundred highly conserved genes encoding microRNAs. In silico analysis has predicted that a typical microRNA may regulate the expression of hundreds of target genes, suggesting miRNAs might have broad biological significance. A major challenge is to obtain experimental evidence for predicted microRNA–target pairs. We reasoned that reciprocal expression of a microRNA and a predicted target within a physiological context would support the presence and relevance of a microRNA–target pair. We used microRNA microarray and proteomic techniques to analyze the cortex and the medulla of rat kidneys. Of the 377 microRNAs analyzed, we identified 6 as enriched in the renal cortex and 11 in the renal medulla. From ∼2100 detectable protein spots in two-dimensional gels, we identified 58 proteins as more abundant in the renal cortex and 72 in the renal medulla. The differential expression of several microRNAs and proteins was verified by real-time PCR and Western blot analyses, respectively. Several pairs of reciprocally expressed microRNAs and proteins were predicted to be microRNA–target pairs by TargetScan, PicTar, or miRanda. Seven pairs were predicted by two algorithms and two pairs by all three algorithms. -
Is Gdh a Marker for Mitochondria in Brain? / James C
Fordham University Masthead Logo DigitalResearch@Fordham Chemistry Faculty Publications Chemistry 1986 The ubs cellular localization of glutamate dehydrogenase (gdh): is gdh a marker for mitochondria in brain? / James C. K. Lai, Kwan-Fu Rex Sheu, Young Tai Kim, Donald D. Clarke, and John P. Blass Department of Neurology, Cornell University Medical College and Altschul Laboratory for Dementia Research Burke Rehabilitation Center White Plains, NY 10605 and Department of Medicine Cornell University Medical College New York, NY 10021 James C. K. Lai Cornell University. Department of Neurology and Neuroscience Kwan-Fu Rex Sheu Burke Rehabilitation Center Recommended Citation Lai, James C. K.; Sheu, Kwan-Fu Rex; Kim, Young Tai; and Clarke, Donald Dudley PhD, "The ubcs ellular localization of glutamate dehydrogenase (gdh): is gdh a marker for mitochondria in brain? / James C. K. Lai, Kwan-Fu Rex Sheu, Young Tai Kim, Donald D. Clarke, and John P. Blass Department of Neurology, Cornell University Medical College and Altschul Laboratory for Dementia Research Burke Rehabilitation Center White Plains, NY 10605 and Department of Medicine Cornell University Medical College New York, NY 10021" (1986). Chemistry Faculty Publications. 21. https://fordham.bepress.com/chem_facultypubs/21 This Article is brought to you for free and open access by the Chemistry at DigitalResearch@Fordham. It has been accepted for inclusion in Chemistry Faculty Publications by an authorized administrator of DigitalResearch@Fordham. For more information, please contact [email protected]. Young Tai Kim Cornell University. Medical College Donald Dudley Clarke PhD Fordham University, [email protected] Follow this and additional works at: https://fordham.bepress.com/chem_facultypubs Part of the Biochemistry Commons • Neurochemical Research, Vol. -
Relationship of Liver Enzymes to Insulin Sensitivity and Intra-Abdominal Fat
Diabetes Care Publish Ahead of Print, published online July 31, 2007 Relationship of Liver Enzymes to Insulin Sensitivity and Intra-abdominal Fat Tara M Wallace MD*, Kristina M Utzschneider MD*, Jenny Tong MD*, 1Darcy B Carr MD, Sakeneh Zraika PhD, 2Daniel D Bankson MD, 3Robert H Knopp MD, Steven E Kahn MB, ChB. *Metabolism, Endocrinology and Nutrition, VA Puget Sound Health Care System 1Obstetrics and Gynecology, University of Washington, Seattle, WA 2Pathology and Laboratory Medicine, Veterans Affairs Puget Sound Health Care System, University of Washington, Seattle, WA 3Harborview Medical Center, University of Washington, Seattle, WA Running title: Liver enzymes and insulin sensitivity Correspondence to: Steven E. Kahn, M.B., Ch.B. VA Puget Sound Health Care System (151) 1660 S. Columbian Way Seattle, WA 98108 Email: [email protected] Received for publication 18 August 2006 and accepted in revised form 29 June 2007. 1 Copyright American Diabetes Association, Inc., 2007 Liver enzymes and insulin sensitivity ABSTRACT Objective: To determine the relationship between plasma liver enzyme concentrations, insulin sensitivity and intra-abdominal fat (IAF) distribution. Research Design and Methods: Plasma gamma-glutamyl transferase (GGT), aspartate transaminase (AST), alanine transaminase (ALT) levels, insulin sensitivity (SI), IAF and subcutaneous fat (SCF) areas were measured on 177 non-diabetic subjects (75M/102, 31-75 2 -5 years) with no history of liver disease. Based on BMI (< or ≥27.5 kg/m ) and SI (< or ≥7.0x10 min-1 pM-1) subjects were divided into lean insulin sensitive (LIS, n=53), lean insulin resistant (LIR, n=60) and obese insulin resistant (OIR, n=56) groups. -
Demonstration of Physical Interactions Between Consecutive Enzymes Of
Fur J Blochein. 117. 527-535 (1981) c FEBS 1981 Demonstration of Physical Interactions between Consecutive Enzymes of the Citric Acid Cycle and of the Aspartate-Malate Shuttle A Study Involving Fumarase, Malate Dehydrogenase, Citrate Synthase and Aspartate Aminotransferase Sonia BEECKMANS and Louis KANAREK Laboratorium voor Chemie der Proteinen, Vrije Universiteit Brussel (Received September 15, 198O/Fehruary 26, 1981) By means of covalently immobilized fumarase and mitochondrial or cytoplasmic malate dehydrogenase we were able to detect physical interactions between different enzymes of the citric acid cycle (fumarase with malate dehydrogenase, malate dehydrogenase with citrate synthase and fumarase with citrate synthase) and between the enzymes of both mitochondrial and cytoplasmic halves of the aspartate-malate shuttle (aspartate amino- transferase and malate dehydrogenase). The interactions between fumarase and malate dehydrogenase were also investigated by immobilizing one enzyme indirectly through antibodies bound to Sepharose - protein A. Our results are consistent with a model in which maximally four molecules of malate dehydrogenase are bound to one fumarase molecule. This complex is able to bind either citrate synthase or aspartate aminotransferase. We propose that these enzymes bind alternatively, in order to allow the cell to perform citric acid cycle or shuttle reactions, according to its needs. The physiological meaning and implications on the regulation of me- tabolism of the existence of a large citric acid cycle/malate-aspartate shuttle multienzyme complex are discussed. Whereas it was generally assumed for many years that the Several publications have appeared lately pointing indeed citric acid cycle enzymes are randomly dispersed in the mito- to the existence of physical interactions between enzymes of chondrial matrix, there are in recent literature various publi- the citric acid cycle and aspartate-malate shuttle [7- 141. -
Interpreting Liver Function Tests CONTENTS
A CASE-BASED SERIES ON PRACTICAL PATHOLOGY FOR GPs FEBRUARY 2020 Interpreting liver function tests CONTENTS: • Dealing with abnormal LFTs in the asymptomatic patient • Diagnosing Gilbert’s syndrome © The Royal College of • Establishing the source of raised ALP Pathologists of Australasia 2 Authors: Dr Melissa Gillett Dr Rebecca Brereton MBBS, FRACP, FRCPA, MAACB Specialist Chemical Pathologist, Chemical Pathologist, Fiona Stanley Hospital Network Fiona Stanley Hospital Network Laboratory, PathWest Laboratory Laboratory, PathWest Laboratory Medicine, Murdoch, WA Medicine, Murdoch, WA Common Sense Pathology is developed by the Royal College of Pathologists of Australasia and supported by Australian Doctor Group. © 2020 Royal College of Pathologists of Australasia www.rcpa.edu.au CEO: Dr Debra Graves Email: [email protected] While the views expressed are those of the authors, modified by expert reviewers, they are not necessarily held by the College. Published by Australian Doctor Group Level 2, 26-32 Pyrmont Bridge Road, Pyrmont NSW 2009 Ph: 1300 360 126 Email: [email protected] Website: www.australiandoctorgroup.com.au ACN: 615 959 914 ABN: 94 615 959 914 ISSN: 1039-7116 The views expressed in this publication are not necessarily those of Australian Doctor Group. This issue is produced and owned by the Royal College of Pathologists of Australasia and distributed by Australian Doctor Group. Common Sense Pathology Editor: Dr Steve Flecknoe-Brown Email: [email protected] Editor: Dr Karley Heyworth Email: [email protected] Sub-editor: Lesley Hoye Email: [email protected] Graphic Designer: Kate O’Dea Email: [email protected] For an electronic version of this issue, please visit www.howtotreat.com.au You can also visit the Royal College of Pathologists of Australasia’s website at www.rcpa.edu.au Click on Library and Publications, then Common Sense Pathology. -
Effect of Salt Stress on the Expression and Promoter Methylation of the Genes Encoding the Mitochondrial and Cytosolic Forms of Aconitase and Fumarase in Maize
International Journal of Molecular Sciences Article Effect of Salt Stress on the Expression and Promoter Methylation of the Genes Encoding the Mitochondrial and Cytosolic Forms of Aconitase and Fumarase in Maize Alexander T. Eprintsev 1, Dmitry N. Fedorin 1, Mikhail V. Cherkasskikh 1 and Abir U. Igamberdiev 2,* 1 Department of Biochemistry and Cell Physiology, Voronezh State University, 394018 Voronezh, Russia; [email protected] (A.T.E.); [email protected] (D.N.F.); [email protected] (M.V.C.) 2 Department of Biology, Memorial University of Newfoundland, St. John’s, NL A1B 3X9, Canada * Correspondence: [email protected] Abstract: The influence of salt stress on gene expression, promoter methylation, and enzymatic activity of the mitochondrial and cytosolic forms of aconitase and fumarase has been investigated in maize (Zea mays L.) seedlings. The incubation of maize seedlings in 150-mM NaCl solution resulted in a several-fold increase of the mitochondrial activities of aconitase and fumarase that peaked at 6 h of NaCl treatment, while the cytosolic activity of aconitase and fumarase decreased. This corresponded to the decrease in promoter methylation of the genes Aco1 and Fum1 encoding the mitochondrial forms of these enzymes and the increase in promoter methylation of the genes Aco2 and Fum2 encoding the cytosolic forms. The pattern of expression of the genes encoding the mitochondrial forms of aconitase and fumarase corresponded to the profile of the increase of the stress marker gene Citation: Eprintsev, A.T.; Fedorin, ZmCOI6.1. It is concluded that the mitochondrial and cytosolic forms of aconitase and fumarase are D.N.; Cherkasskikh, M.V.; regulated via the epigenetic mechanism of promoter methylation of their genes in the opposite ways Igamberdiev, A.U.