Search

Your search keyword '"MESH: Transaminases"' showing total 9 results
Start Over Descriptor "MESH: Transaminases"
9 results on '"MESH: Transaminases"'

1. Fièvre hémorragique à syndrome rénal associée à l’hantavirus Séoul en France : une observation

Author

J.-F. Dufour, Jean-Marc Reynes, A. Bour, X. Plaisancie, Service de médecine interne et post-urgence [Bourg-en-Bresse], Centre Hospitalier Fleyriat [Bourg en Bresse], Centre National de Référence des Hantavirus - Biologie des Infections Virales Emergentes (CNR-UBIVE), Institut Pasteur [Paris], and Institut Pasteur [Paris] (IP)

Subjects
0301 basic medicine, medicine.medical_specialty, MESH: Acute Kidney Injury, viruses, 030106 microbiology, Hemorrhagic fever with renal syndrome, 03 medical and health sciences, MESH: Hemorrhagic Fever with Renal Syndrome, MESH: Transaminases, [SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseases, Internal Medicine, Medicine, MESH: Fluorescent Antibody Technique, MESH: Thrombocytopenia, Seoul virus, Hantavirus, Gynecology, MESH: Humans, business.industry, Fièvre hémorragique avec syndrome rénal, MESH: Hantavirus, Gastroenterology, virus diseases, MESH: Adult, MESH: Seoul, MESH: Male, 3. Good health, MESH: France, Virus Séoul, [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology, [SDV.SPEE]Life Sciences [q-bio]/Santé publique et épidémiologie, France, business
Abstract

International audience; Introduction. – Rodents are hantavirus hosts. In Europe, hantaviruses are responsible for human infectionsresulting in hemorrhagic fever with renal syndrome. Thousands of Puumala virus infections are reportedannually in Europe, whereas human Seoul virus infections are rarely detected.Case report. – We report the case of a 38-year-old patient who presented initially with flu-like symptoms and transitory blurred vision. He developed thrombocytopenia, acute renal failure, and elevatedaminotransferases levels during the disease course, but the outcome was favorable with a full recovery. Afterwards, the hantavirus serology results were indicative of Seoul virus infection.Conclusion. – This report serves to remind physicians to consider diagnosing hantavirus infection whenobserving the association of fever, acute renal failure and thrombocytopenia. Transitory blurred vision isa specific element to indicate this diagnosis.; Introduction. – Les hantavirus zoonotiques ont pour hôtes naturels les rongeurs. Ils sont responsables d’infections humaines, qui en Europe, se traduisent le plus souvent par un tableau de fièvre hémorragique avec syndrome rénal. Les infections par le virus Puumala sont détectées chaque année par milliers alors que celles par le virus Séoul le sont très rarement.Observation. – Nous rapportons l’observation d’un homme de 38 ans, qui présentait initialement unsyndrome pseudo-grippal associé à une baisse d’acuité visuelle transitoire. Après l’installation d’unethrombopénie, d’une insuffisance rénale aiguë, d’une élévation des transaminases, l’évolution était spon-tanément favorable. Les résultats des sérologies hantavirus étaient en faveur d’une infection par le virusSéoul.Conclusion. – Cette observation rappelle l’importance d’évoquer le diagnostic d’infection à hantavirusdevant l’association d’une fièvre, d’une insuffisance rénale aiguë et d’une thrombopénie. Les troublesvisuels transitoires constituent un élément clinique spécifique évoquant ce diagnostic

Published
2016
Full Text
View/download PDF

2. Protease-activated receptor 1 knockout reduces experimentally induced liver fibrosis

Author

Anne Rullier, Nathalie Dugot-Senant, Jean Rosenbaum, Jennifer Gillibert-Duplantier, Gérard Déléris, Cyril Petibois, Pierre Costet, Gaelle Cubel, Valérie Haurie, Paulette Bioulac-Sage, Danièle Taras, Fibrose hépatique et cancer du foie, Université Bordeaux Segalen - Bordeaux 2-IFR66-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire d'anatomie pathologique, CHU Bordeaux [Bordeaux]-Groupe hospitalier Pellegrin, Animalerie spécialisée, Université Bordeaux Segalen - Bordeaux 2, Chimie Nucléaire Analytique et Bio-environnementale (CNAB), Université Sciences et Technologies - Bordeaux 1 (UB)-Centre National de la Recherche Scientifique (CNRS), and Rosenbaum, Jean

Subjects
Liver Cirrhosis, Male, Physiology, T-Lymphocytes, MESH: Cell Hypoxia, MESH: Chemotaxis, Leukocyte, MESH: Collagen Type I, MESH: Mice, Knockout, MESH: Lipid Peroxidation, MESH: Thrombin, MESH: Genotype, Mice, MESH: Animals, Receptor, Carbon Tetrachloride, Chemokine CCL2, Mice, Knockout, Thrombin, Gastroenterology, Cell Hypoxia, Cell biology, MESH: Receptor, PAR-1, Chemotaxis, Leukocyte, Liver, Coagulation, Intercellular Signaling Peptides and Proteins, Matrix Metalloproteinase 2, MESH: Liver Cirrhosis, medicine.drug, medicine.medical_specialty, Genotype, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Biology, Collagen Type I, Immediate early protein, Immediate-Early Proteins, Receptor, Platelet-Derived Growth Factor beta, Necrosis, MESH: Mice, Inbred C57BL, MESH: Transaminases, Physiology (medical), Internal medicine, medicine, Animals, Receptor, PAR-1, RNA, Messenger, MESH: Intercellular Signaling Peptides and Proteins, MESH: Mice, MESH: Chemokine CCL2, [SDV.BC] Life Sciences [q-bio]/Cellular Biology, Transaminases, MESH: RNA, Messenger, MESH: Necrosis, Hepatology, MESH: Carbon Tetrachloride, Connective Tissue Growth Factor, MESH: Immediate-Early Proteins, Chemotaxis, MESH: Male, Mice, Inbred C57BL, MESH: Matrix Metalloproteinase 2, Disease Models, Animal, MESH: T-Lymphocytes, Endocrinology, Protease-Activated Receptor 1, Hemostasis, Lipid Peroxidation, MESH: Disease Models, Animal, MESH: Receptor, Platelet-Derived Growth Factor beta, Hepatic fibrosis, MESH: Liver
Abstract

Thrombin inhibition protects against liver fibrosis. However, it is not known whether the thrombin profibrogenic effect is due to effects on blood coagulation or to signaling via protease-activated receptors (PARs). We took advantage of the lack of blood coagulation defects in PAR-1-knockout mice. Acute carbon tetrachloride (CCl4) toxicity was similar in wild-type (WT), PAR-1−/−, and PAR-1+/−mice as judged by aminotransferase levels, area of liver necrosis, and liver peroxidation measured by Fourier-transformed infrared spectroscopy. Fifteen mice/group received CCl4or its solvent for 6 wk (300 μl/kg, 3 times a week). Fibrosis area was increased 10-fold by CCl4treatment in WT mice. PAR-1 deficiency protected against fibrosis, with 36% and 56% decrease in PAR-1+/−and PAR-1−/−mice, respectively ( P < 0.001). Similar results were obtained for area of activated fibrogenic cells (64% and 79% decrease in PAR-1+/−and PAR-1−/−mice, respectively, P < 0.001). These findings were corroborated by measurements of type I collagen, matrix metalloproteinase-2, and PDGF-β receptor mRNA levels. There was also a significant decrease in T lymphocyte infiltration in PAR-1-deficient mice. Altogether, these results suggest that thrombin profibrogenic effects are independent of effects on blood coagulation and are instead due to direct effects on fibrogenic cells and possibly on T lymphocytes.

Published
2008
Full Text
View/download PDF

3. Three different classes of aminotransferases evolved prephenate aminotransferase functionality in arogenate-competent microorganisms

Author

Michel Matringe, Gilles Curien, Alexandra Kraut, Lucas Moyet, Matthieu Graindorge, Cécile Giustini, Laboratoire de physiologie cellulaire végétale (LPCV), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Laboratoire d'étude de la dynamique des protéomes (LEDyP), Université Joseph Fourier - Grenoble 1 (UJF)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM), French National Institute for Agricultural Research (INRA), CNRS, Commissariat a l'Energie Atomique et aux Energies Alternatives (CEA), University of Grenoble Alpes, GRAL Labex (Grenoble Alliance for Integrated Structural Cell Biology) [ANR-10-LABEX-04], Curien, Gilles, Matringe, Michel, Martin-Laffon, Jacqueline, Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)

Subjects
Transamination, phenylalanine, enzymatic activity, Phenylalanine, MESH: Amino Acids, Dicarboxylic, Biochemistry, MESH: Cyclohexenes, MESH: Tyrosine, chemistry.chemical_compound, Aromatic amino acids, Pyridoxal phosphate, Tyrosine, Rhodobacter, prephenate aminotransferase, microorganisms, bacteria, MESH: Bacterial Proteins, MESH: Evolution, Molecular, 2. Zero hunger, chemistry.chemical_classification, Synechococcus, aminotransferases, Streptomyces, 3. Good health, Amino acid, Amino Acids, Dicarboxylic, Pyridoxal Phosphate, arogenate, aminoacide, MESH: Pyridoxal Phosphate, Rhizobium, Biology, Microbiology, amination, bacterial metabolism, Mycobacterium, Evolution, Molecular, Bacterial Proteins, MESH: Transaminases, Cyclohexenes, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Humans, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Nitrosomonas, Molecular Biology, Transaminases, MESH: Humans, Cell Biology, metabolic pathway, aromatic aminoacid biosynthesis, Metabolic pathway, enzyme, MESH: Bacteria, Enzyme, Metabolism, chemistry, tyrosine
Abstract

Background: The genes encoding prephenate aminotransferase in arogenate-competent microorganisms for tyrosine synthesis are still unknown. Results: Three different classes of aminotransferase use prephenate as an amino acceptor. Conclusion: Prephenate aminotransferase functionality has arisen more than once during evolution. Significance: This first identification of prephenate aminotransferases in arogenate competent microorganisms affords a better understanding of the origin and fixation of the arogenate route during evolution. The aromatic amino acids phenylalanine and tyrosine represent essential sources of high value natural aromatic compounds for human health and industry. Depending on the organism, alternative routes exist for their synthesis. Phenylalanine and tyrosine are synthesized either via phenylpyruvate/4-hydroxyphenylpyruvate or via arogenate. In arogenate-competent microorganisms, an aminotransferase is required for the transamination of prephenate into arogenate, but the identity of the genes is still unknown. We present here the first identification of prephenate aminotransferases (PATs) in seven arogenate-competent microorganisms and the discovery that PAT activity is provided by three different classes of aminotransferase, which belong to two different fold types of pyridoxal phosphate enzymes: an aspartate aminotransferase subgroup 1 in tested - and -proteobacteria, a branched-chain aminotransferase in tested cyanobacteria, and an N-succinyldiaminopimelate aminotransferase in tested actinobacteria and in the -proteobacterium Nitrosomonas europaea. Recombinant PAT enzymes exhibit high activity toward prephenate, indicating that the corresponding genes encode bona fide PAT. PAT functionality was acquired without other modification of substrate specificity and is not a general catalytic property of the three classes of aminotransferases.

Published
2014
Full Text
View/download PDF

4. Pentoxifylline aggravates fatty liver in obese and diabetic ob/ob mice by increasing intestinal glucose absorption and activating hepatic lipogenesis

Author

Massart, Julie, Robin, Marie-Anne, Noury, Fanny, Fautrel, Alain, Lettéron, P., Bado, A., Eliat, Pierre-Antoine, Fromenty, Bernard, Foie, métabolismes et cancer, Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), Laboratoire Traitement du Signal et de l'Image (LTSI), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES), Hépatotoxicité et xénobiotiques, Détoxication et réparation Tissulaire, Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Foie, métabolismes et cancer, Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )-Institut National de la Santé et de la Recherche Médicale (INSERM)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), Centre de recherche biomédicale Bichat-Beaujon (CRB3), Université Paris Diderot - Paris 7 (UPD7)-Institut National de la Santé et de la Recherche Médicale (INSERM), Plate-forme Rennaise d'Imagerie et Spectroscopie Structurale et Métabolique (PRISM), Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )-Centre national du machinisme agricole, du génie rural, des eaux et forêts (CEMAGREF)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Institut National de la Recherche Agronomique (INRA), INSERM (Institut Nationale de la Santé et de la Recherche Médicale), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut National de la Recherche Agronomique (INRA)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Centre national du machinisme agricole, du génie rural, des eaux et forêts (CEMAGREF)-Institut national de recherche en sciences et technologies pour l'environnement et l'agriculture (IRSTEA)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), Université de Rennes (UR)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), Université de Rennes (UR)-Institut National de la Santé et de la Recherche Médicale (INSERM), Université de Rennes (UR)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rennes (UR)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Foie, métabolismes et cancer, Université de Rennes (UR)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )-Institut National de la Santé et de la Recherche Médicale (INSERM)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), Institut National de la Recherche Agronomique (INRA)-Université de Rennes (UR)-Centre national du machinisme agricole, du génie rural, des eaux et forêts (CEMAGREF)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), and Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Centre national du machinisme agricole, du génie rural, des eaux et forêts (CEMAGREF)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )

Subjects
Blood Glucose, Male, MESH: Inflammation, obesity, Mice, Obese, methylxanthine, Mice, Adipocytes, MESH: Obesity, MESH: Animals, glucose, MESH: Mice, Obese, MESH: Fatty Liver, MESH: Pentoxifylline, Glucose Transporter Type 2, MESH: Oxidative Stress, Basic Helix-Loop-Helix Leucine Zipper Transcription Factors, Nuclear Proteins, MESH: Transcription Factors, Research Papers, Lipids, MESH: Glucose, Jejunum, Liver, MESH: Glycolysis, MESH: Sodium-Glucose Transporter 1, Sterol Regulatory Element Binding Protein 1, Glycolysis, drug-induced liver injury, MESH: Diabetes Mellitus, Type 2, MESH: Triglycerides, MESH: Cell Line, Tumor, ChREBP, MESH: Intestinal Absorption, MESH: Glucose Tolerance Test, MESH: Sterol Regulatory Element Binding Protein 1, Sodium-Glucose Transporter 1, MESH: Mice, Inbred C57BL, MESH: Transaminases, Cell Line, Tumor, Animals, Humans, MESH: Mice, Transaminases, Triglycerides, MESH: Adipocytes, fatty liver, Inflammation, MESH: Lipogenesis, MESH: Humans, Lipogenesis, MESH: Biological Markers, Glucose Tolerance Test, MESH: Lipids, MESH: Male, Mice, Inbred C57BL, Oxidative Stress, pentoxifylline, Diabetes Mellitus, Type 2, Intestinal Absorption, MESH: Jejunum, MESH: Blood Glucose, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, MESH: Glucose Transporter Type 2, MESH: Nuclear Proteins, Biomarkers, Transcription Factors, MESH: Liver
Abstract

International audience; BACKGROUND AND PURPOSE: Pentoxifylline is in clinical trials for non-alcoholic fatty liver disease and diabetic nephropathy. Metabolic and hepatic effects of pentoxifylline were assessed in a murine model of obesity and type 2 diabetes. EXPERIMENTAL APPROACH: Pentoxifylline (100 mg*kg(-1) *day(-1)) was administered for 4 days or 3 weeks in lean and obese/diabetic ob/ob mice. Plasma lipids, glucose, other metabolites and relevant enzymes were measured by standard assays. Hepatic lipids in vivo were assessed with magnetic resonance spectroscopy and by histology. Hepatic extracts were also analysed with RT-PCR and Western blotting. KEY RESULTS: Four days of pentoxifylline treatment slightly increased liver lipids in ob/ob mice. After 3 weeks, pentoxifylline exacerbated fatty liver and plasma transaminases in ob/ob mice but did not induce liver steatosis in lean mice. Plasma glucose was highest in fed, but not fasted, ob/ob mice treated with pentoxifylline. During the first 10 min of an oral glucose tolerance test, blood glucose increased more rapidly in pentoxifylline-treated mice. Jejunal expression of glucose transporter 2 isoform was increased in pentoxifylline-treated obese mice. Hepatic activity of carbohydrate response element binding protein (ChREBP) increased after pentoxifylline in ob/ob, but not lean, mice. Hepatic expression of lipogenic enzymes was highest in pentoxifylline-treated ob/ob mice. However, pentoxifylline reduced markers of oxidative stress and inflammation in ob/ob liver. CONCLUSION AND IMPLICATIONS: Pentoxifylline exacerbated fatty liver in ob/ob mice through enhanced intestinal glucose absorption, increased postprandial glycaemia and activation of hepatic lipogenesis. Long-term treatment with pentoxifylline could worsen fatty liver in some patients with pre-existing hyperglycaemia.

Published
2012
Full Text
View/download PDF

5. Identification of a plant gene encoding glutamate/aspartate-prephenate aminotransferase: the last homeless enzyme of aromatic amino acids biosynthesis

Author

Cécile Giustini, Alexandra Kraut, Michel Matringe, Matthieu Graindorge, Gilles Curien, Anne-Claire Jacomin, Laboratoire de physiologie cellulaire végétale (LPCV), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Laboratoire d'étude de la dynamique des protéomes (LEDyP), Université Joseph Fourier - Grenoble 1 (UJF)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)

Subjects
0106 biological sciences, Arabidopsis thaliana, Transamination, Arabidopsis, Phenylalanine, plant, 01 natural sciences, Biochemistry, Mass Spectrometry, MESH: Recombinant Proteins, chemistry.chemical_compound, Structural Biology, Aromatic amino acids, aromatic amino acids biosynthesis, MESH: Arabidopsis, Tyrosine, prephenate aminotransferase, Cells, Cultured, chemistry.chemical_classification, 0303 health sciences, biology, MESH: Kinetics, MESH: Glutamic Acid, Recombinant Proteins, Amino acid, MESH: Amino Acids, Aromatic, Electrophoresis, Polyacrylamide Gel, Aromatic amino acid, MESH: Cells, Cultured, purification, Biophysics, Glutamic Acid, MESH: Arabidopsis Proteins, Aspartate aminotransferase, 03 medical and health sciences, Amino Acids, Aromatic, MESH: Aspartate Aminotransferases, Biosynthesis, MESH: Transaminases, Genetics, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Aspartate Aminotransferases, Molecular Biology, Transaminases, 030304 developmental biology, MESH: Mass Spectrometry, Arabidopsis Proteins, Cell Biology, Molecular biology, Enzyme assay, enzyme, Enzyme, Metabolism, chemistry, kinetics, biochemical properties, biology.protein, Enzymology, 010606 plant biology & botany, MESH: Electrophoresis, Polyacrylamide Gel
Abstract

International audience; In all organisms synthesising phenylalanine and/or tyrosine via arogenate, a prephenate aminotransferase is required for the transamination of prephenate into arogenate. The identity of the gene encoding this enzyme in the organisms where this activity occurs is still unknown. Glutamate/aspartate-prephenate aminotransferase (PAT) is thus the last homeless enzyme in the aromatic amino acids pathway. We report on the purification, mass spectrometry identification and biochemical characterization of Arabidopsis thaliana prephenate aminotransferase. Our data revealed that this activity is housed by the prokaryotic-type plastidic aspartate aminotransferase (At2g22250). This represents the first identification of a gene encoding PAT.

Published
2010
Full Text
View/download PDF

6. Genomic insight into the amino acid relations of the pea aphid, Acyrthosiphon pisum, with its symbiotic bacterium Buchnera aphidicola

Author

Wilson, A. C. C., Ashton, P. D., Calevro, Federica, Charles, H., Colella, Stefano, Febvay, G., Jander, G., Kushlan, P. F., Macdonald, S. J., Schwartz, J. F., Thomas, G. H., Douglas, A. E., Department of Biology [Miami], University of Miami [Coral Gables], Department of Biology [York], University of York [York, UK], Biologie Fonctionnelle, Insectes et Interactions (BF2I), Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Institut National des Sciences Appliquées (INSA)-Université de Lyon-Institut National des Sciences Appliquées (INSA)-Université de Lyon, An algorithmic view on genomes, cells, and environments (BAMBOO), Inria Grenoble - Rhône-Alpes, Institut National de Recherche en Informatique et en Automatique (Inria)-Institut National de Recherche en Informatique et en Automatique (Inria)-Laboratoire de Biométrie et Biologie Evolutive - UMR 5558 (LBBE), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de Recherche en Informatique et en Automatique (Inria)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS), Boyce Thompson Institute [Ithaca], Cornell University [New York], BBSRC, ANR BB/F005342/1, USDA 2005-35604-15446, University of Miami Start-up Funds, Sarkaria Institute for Insect Physiology and Toxicology, University of Miami Honors Summer Research Program, Biotechnology and Biological Sciences Research Council BB/F005342/1, Université de Lyon-Institut National des Sciences Appliquées (INSA)-Université de Lyon-Institut National des Sciences Appliquées (INSA), and Cornell University

Subjects
MESH: Amino Acids, MESH: Buchnera, Genome, Insect, ACYRTHOSIPHON PISUM, MESH: Peas, MESH: Genome, Bacterial, Models, Biological, GENOME ANNOTATION, HEMIPTERA, Bacterial Proteins, Buchnera, MESH: Transaminases, MESH: Insect Proteins, Animals, MESH: Animals, Amino Acids, MESH: Bacterial Proteins, Transaminases, GENOME EVOLUTION, MESH: Genetic Complementation Test, MESH: Symbiosis, MESH: Genome, Insect, Genetic Complementation Test, ESSENTIAL AMINO ACID, SYMBIOSIS, Peas, MESH: Models, Biological, food and beverages, biochemical phenomena, metabolism, and nutrition, BUCHNERA APHICOLA, Aphids, GENOMIC COMPLEMENTARITY, Insect Proteins, AMINO ACID METABOLISM, MESH: Aphids, Genome, Bacterial, [SDV.EE.IEO]Life Sciences [q-bio]/Ecology, environment/Symbiosis
Abstract

International audience; The pea aphid genome includes 66 genes contributing to amino acid biosynthesis and 93 genes to amino acid degradation. In several respects, the pea aphid gene inventory complements that of its symbiotic bacterium, Buchnera aphidicola (Buchnera APS). Unlike other insects with completely sequenced genomes, the pea aphid lacks the capacity to synthesize arginine, which is produced by Buchnera APS. However, consistent with other insects, it has genes coding for individual reactions in essential amino acid biosynthesis, including threonine dehydratase and branched-chain amino acid aminotransferase, which are not coded in the Buchnera APS genome. Overall the genome data suggest that the biosynthesis of certain essential amino acids is shared between the pea aphid and Buchnera APS, providing the opportunity for precise aphid control over Buchnera metabolism.

Published
2010
Full Text
View/download PDF

7. [Chronic transaminase elevation]

Author

Cadranel, J.-F., Thevenot, T., Agents pathogènes et inflammation - UFC (EA 4266) (API), Université de Franche-Comté (UFC), and Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC)

Subjects
MESH: Humans, MESH: Middle Aged, MESH: Chronic Disease, [SDV.MHEP.HEG]Life Sciences [q-bio]/Human health and pathology/Hépatology and Gastroenterology, Middle Aged, Celiac Disease, MESH: Transaminases, Chronic Disease, Humans, Female, MESH: Female, ComputingMilieux_MISCELLANEOUS, MESH: Celiac Disease, Transaminases
Abstract

National audience

Published
2008
Full Text
View/download PDF

8. L-methionine degradation pathway in Kluyveromyces lactis: identification and functional analysis of the genes encoding L-methionine aminotransferase

Author

Pascal Bonnarme, Cécile Neuvéglise, Serge Casaregola, Dafni-Maria Kagkli, Timothy M. Cogan, Génie et Microbiologie des Procédés Alimentaires (GMPA), Institut National de la Recherche Agronomique (INRA)-Institut National Agronomique Paris-Grignon (INA P-G), Moorepark Food Research Centre, Teagasc - The Agriculture and Food Development Authority (Teagasc), Microbiologie et Génétique Moléculaire (MGM), Institut National de la Recherche Agronomique (INRA)-Institut National Agronomique Paris-Grignon (INA P-G)-Centre National de la Recherche Scientifique (CNRS), and D. Kagkli bénéficie Marie Curie Fellowship (YETI program QLK3_CT_2000_60055)

Subjects
Genetics and Molecular Biology, MESH: Transformation, Genetic, medicine.disease_cause, Applied Microbiology and Biotechnology, MESH: Kluyveromyces, Transformation, 03 medical and health sciences, chemistry.chemical_compound, Kluyveromyces, Plasmid, Transformation, Genetic, Methionine, Genetic, MESH: Plasmids, MESH: Sulfur Compounds, MESH: Transaminases, medicine, Escherichia coli, Sulfhydryl Compounds, MESH: Sulfhydryl Compounds, Gene, Transaminases, 030304 developmental biology, Kluyveromyces lactis, 0303 health sciences, Ecology, biology, Sulfur Compounds, 030306 microbiology, MESH: Escherichia coli, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, biology.organism_classification, Yeast, Metabolic pathway, chemistry, Biochemistry, MESH: Methionine, MESH: Volatilization, Volatilization, Food Science, Biotechnology, Plasmids
Abstract

Kluyveromyces lactis is one of the cheese-ripening yeasts and is believed to contribute to the formation of volatile sulfur compounds (VSCs) through degradation of l -methionine. l -Methionine aminotransferase is potentially involved in the pathway that results in the production of methanethiol, a common precursor of VSCs. Even though this pathway has been studied previously, the genes involved have never been studied. In this study, on the basis of sequence homology, all the putative aminotransferase-encoding genes from K. lactis were cloned in an overproducing vector, pCXJ10, and their effects on the production of VSCs were analyzed. Two genes, Kl ARO8.1 and Kl ARO8.2 , were found to be responsible for l -methionine aminotransferase activity. Transformants carrying these genes cloned in the pCXJ10 vector produced threefold-larger amounts of VSCs than the transformant containing the plasmid without any insert or other related putative aminotransferases produced.

Published
2006
Full Text
View/download PDF

9. Chronic hepatitis C virus infection: does it really impact health-related quality of life? A study in rural Egypt

Author

Mostafa K. Mohamed, Khaled M. Abd Elaziz, Sahar Dewedar, Michaël Schwarzinger, Fabrice Carrat, C. Rekacewicz, Arnaud Fontanet, Epidémiologie et sciences de l'information, Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM), Department of Community, Université Ain Shams-Faculty of Medicine-Environmental and Occupational Medicine, Epidémiologie des Maladies Emergentes - Emerging Diseases Epidemiology, Pasteur-Cnam Risques infectieux et émergents (PACRI), Institut Pasteur [Paris] (IP)-Conservatoire National des Arts et Métiers [CNAM] (CNAM), HESAM Université - Communauté d'universités et d'établissements Hautes écoles Sorbonne Arts et métiers université (HESAM)-HESAM Université - Communauté d'universités et d'établissements Hautes écoles Sorbonne Arts et métiers université (HESAM)-Institut Pasteur [Paris] (IP)-Conservatoire National des Arts et Métiers [CNAM] (CNAM), HESAM Université - Communauté d'universités et d'établissements Hautes écoles Sorbonne Arts et métiers université (HESAM)-HESAM Université - Communauté d'universités et d'établissements Hautes écoles Sorbonne Arts et métiers université (HESAM), Schwarzinger, Michaël, and Institut Pasteur [Paris]-Conservatoire National des Arts et Métiers [CNAM] (CNAM)-Institut Pasteur [Paris]-Conservatoire National des Arts et Métiers [CNAM] (CNAM)

Subjects
Male, Rural Population, medicine.disease_cause, MESH: Egypt, 0302 clinical medicine, SF-12, Quality of life, Visual analogue scale, MESH: Rural Population, Prevalence, 030212 general & internal medicine, education.field_of_study, MESH: Middle Aged, Hepatitis C, Middle Aged, humanities, 3. Good health, MESH: Hepatitis C, Chronic, Developing Countries, HCV, 030211 gastroenterology & hepatology, Egypt, Female, Viral disease, Adult, medicine.medical_specialty, Hepatitis C virus, Population, Article, MESH: Multivariate Analysis, 03 medical and health sciences, MESH: Transaminases, Internal medicine, medicine, Humans, education, Transaminases, MESH: Prevalence, MESH: Humans, Hepatology, business.industry, Public health, MESH: Quality of Life, MESH: Adult, Hepatitis C, Chronic, medicine.disease, Genetic translation, MESH: Male, Chronic infection, [SDV.SPEE] Life Sciences [q-bio]/Santé publique et épidémiologie, Immunology, Multivariate Analysis, Quality of Life, [SDV.SPEE]Life Sciences [q-bio]/Santé publique et épidémiologie, business, MESH: Female, disease labelling effect
Abstract

Aucune info claire sur le CTA application de 12 mois par défaut conformément à la politique générale de Wiley; International audience; Previous Western studies showed a consistent and marked reduction in health-related quality of life (HRQOL) in patients chronically infected with hepatitis C virus (HCV). However, these studies were conducted on patients whose knowledge of their serological status may have affected their HRQOL. This HRQOL survey conducted in the Egyptian rural population provides a unique opportunity to clarify this issue among a population whose serological status is unknown. HRQOL was assessed by an Arabic translation of the Short-Form 12, and a visual analog scale of the relative severity of one's health status. HCV chronic infection was defined by positive tests for anti-HCV antibody and HCV-RNA. HRQOL was compared according to HCV chronic infection status in linear mixed models adjusted for potential confounding factors, such as age, sex, education, and health care-related risk factors, and adjusted for interviewer as a random effect. One hundred forty-six Egyptians chronically infected with HCV had similar Short-Form 12 and visual analog scale scores, compared with 1,140 uninfected controls from the same rural community. In individuals chronically infected with HCV, serum aminotransferase levels did not correlate with HRQOL. In conclusion, this study did not find a significant reduction of HRQOL in patients chronically infected with HCV compared with uninfected, contemporaneous controls. This may be explained in part by a lower morbidity amongst patients chronically infected with HCV in rural Egypt and a higher morbidity amongst uninfected controls as compared with those of Western studies, as well as a lack of awareness of hepatitis C serological status.

Published
2004
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results