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Le stress oxydatif, caractérisé par un profond déséquilibre oxydoréducteur de la cellule, conduit à la formation de composés capables de réagir avec les macromolécules cellulaires. Pour faire face à l’atteinte oxydative, les cellules disposent de systèmes de défense, chargés d’éliminer les espèces oxydantes, et de systèmes de réparation qui interviennent lorsque les lésions se sont déjà produites.
L’ADN est une cible des agents oxydants. Ceux-ci peuvent induire des cassures de brins ou/et des sites labiles en milieu alcalin. Nous avons mis en évidence par la technique de l’élétrophorèse en gel d’agarose que l’agent inducteur de stress oxydatif utilisé dans nos expériences, l’hydroperoxyde de tert-butyle, n’induit pas de fragmentation de l’ADN des hépatocytes isolés. Les cassures que nous avons observées par la technique de FADU (Fluorimetric Analysis of DNA Unwinding) sont donc de types simple brin.
La poly(ADP-ribose) polymérase, enzyme nucléaire, reconnait les cassures de brins et est activée par celles-ci. Elle catalyse alors le transfert d’unité (ADP-ribose) depuis le NAD+ sur elle-même et sur d’autres protéines nucléaires.
Lorsque les lésions à l’ADN sont trop importantes, le contenu intracellulaire en NAD+ diminue suite à sa consommation par la poly(ADP-ribose) polymérase activée. C’est effectivement ce que nous avons observé lorsque des hépatocytes isolés de rat sont incubés en présence d’un inducteur expérimental du stress oxydatif : l’hyperperoxyde de tert-butyle.
Néanmoins, cette diminution du taux en NAD+ n’est pas responsable de la perte en ATP ni de la lyse cellulaire observées dans ces mêmes conditions. La cytotoxicité du peroxyde n’est don c pas expliqué par la voie d’activation de la poly(ADP-ribose) polymérase suite à) des cassures de brins de l’ADN

Oxidative Stress --- ADP Ribose Transferases --- Medical Laboratory Science --- Tert-Butylhydroperoxide

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Featuring a diverse array of model organisms and scientific techniques, Sirtuins: Methods and Protocols collects detailed contributions from experts in the field addressing this vital family of genes. Opening with methods to generate sirtuin biology tools, the book continues by covering methods to identify sirtuin substrates, to measure sirtuin activity, and to study sirtuin biology. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls.   Comprehensive and easy to use, Sirtuins: Methods and Protocols presents detailed protocols for sirtuin research that can be followed directly or modified to investigate new areas of sirtuin biology.

Sirtuins. --- Proteins. --- Proteins --- Group III Histone Deacetylases --- Intracellular Signaling Peptides and Proteins --- ADP Ribose Transferases --- Histone Deacetylases --- Pentosyltransferases --- Amino Acids, Peptides, and Proteins --- Glycosyltransferases --- Amidohydrolases --- Transferases --- Chemicals and Drugs --- Hydrolases --- Enzymes --- Enzymes and Coenzymes --- Sirtuins --- Human Anatomy & Physiology --- Health & Biological Sciences --- Animal Biochemistry --- Silent Mating Type Information Regulator 2-like Proteins --- Sir2-like Proteins --- Silent Mating Type Information Regulator 2 like Proteins --- Sir2 like Proteins --- Coenzymes and Enzymes --- Biocatalysts --- Transferase --- Glycoside Transferases --- Transferases, Glycoside --- Gene Products, Protein --- Gene Proteins --- Protein Gene Products --- Proteins, Gene --- Class I Histone Deacetylases --- Class II Histone Deacetylases --- HDAC Proteins --- Histone Deacetylase --- Histone Deacetylase Complexes --- Complexes, Histone Deacetylase --- Deacetylase Complexes, Histone --- Deacetylase, Histone --- Deacetylases, Histone --- ADP Ribose Transferase --- ADPRT --- ADPRTs --- ART Transferase --- ART Transferases --- ARTase --- ARTases --- Mono ADP-ribose Transferases --- Mono ADPribose Transferase --- Mono ADPribose Transferases --- Mono(ADP-Ribose) Transferase --- Mono(ADP-Ribosyl)transferase --- Mono(ADPribosyl)transferase --- Mono-ADP-Ribosyltransferase --- MonoADPribosyltransferase --- NAD ADP-Ribosyltransferase --- NAD(+)-L-arginine ADP-D-ribosyltransferase --- NAD-Agmatine ADP-Ribosyltransferase --- NAD-Arginine ADP-Ribosyltransferase --- NADP-ADPRTase --- NADP-Arginine ADP-Ribosyltransferase --- ADP-Ribosyltransferase --- Mono(ADP-Ribose) Transferases --- NAD(P)(+)-Arginine ADP-Ribosyltransferase --- NAD+ ADP-Ribosyltransferase --- ADP Ribosyltransferase --- ADP-Ribosyltransferase, NAD --- ADP-Ribosyltransferase, NAD+ --- ADP-Ribosyltransferase, NAD-Agmatine --- ADP-Ribosyltransferase, NAD-Arginine --- ADP-Ribosyltransferase, NADP-Arginine --- ADP-ribose Transferases, Mono --- ADPribose Transferase, Mono --- ADPribose Transferases, Mono --- Mono ADP Ribosyltransferase --- Mono ADP ribose Transferases --- NAD ADP Ribosyltransferase --- NAD Agmatine ADP Ribosyltransferase --- NAD Arginine ADP Ribosyltransferase --- NAD+ ADP Ribosyltransferase --- NADP ADPRTase --- NADP Arginine ADP Ribosyltransferase --- Ribose Transferase, ADP --- Ribose Transferases, ADP --- Transferase, ADP Ribose --- Transferase, ART --- Transferase, Mono ADPribose --- Transferases, ADP Ribose --- Transferases, ART --- Transferases, Mono ADP-ribose --- Transferases, Mono ADPribose --- Intracellular Signaling Peptides --- Intracellular Signaling Proteins --- Peptides, Intracellular Signaling --- Proteins, Intracellular Signaling --- Signaling Peptides, Intracellular --- Signaling Proteins, Intracellular --- Proteids --- Amidases --- NAD-Dependent Histone Deacetylases --- Sir2-like Deacetylases --- Sirtuin Histone Deacetylases --- Deacetylases, NAD-Dependent Histone --- Deacetylases, Sir2-like --- Histone Deacetylases, NAD-Dependent --- NAD Dependent Histone Deacetylases --- Sir2 like Deacetylases --- Life sciences. --- Proteomics. --- Animal genetics. --- Life Sciences. --- Animal Genetics and Genomics. --- Genetics --- Molecular biology --- Biosciences --- Sciences, Life --- Science

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Vibrio cholerae, the causative organism of the disease Cholera, colonizes the small intestine and produces several different toxins among which the enterotoxin, or more widely known as cholera toxin (CT), happens to be the major virulence determinant that is responsible for the diarrheal syndrome. This book provides for the first time comprehensive and up-to-date information about all the toxins of Vibrio cholerae, their physical and chemical structures, their biosynthesis and its genetic regulation, their physiology, the molecular biology of their interactions with the host as well as their role in the development of an appropriate and effective cholera vaccine. It also offers relevant and necessary background information on the basic biology of the Vibrio cholerae cell and cholera bacteriophages.

Cholera toxin. --- Cholera toxin --- Bacterial Toxins --- ADP Ribose Transferases --- Enterotoxins --- Toxins, Biological --- Pentosyltransferases --- Biological Factors --- Glycosyltransferases --- Chemicals and Drugs --- Transferases --- Enzymes --- Enzymes and Coenzymes --- Cholera Toxin --- Biology --- Medicine --- Health & Biological Sciences --- Microbiology & Immunology --- Infectious Diseases --- Enterotoxins. --- Enterotoxin --- Cholera enterotoxin --- Cholera exotoxin --- Choleragen --- Choleragenoid --- CT (Cholera toxin) --- CTX (Cholera toxin) --- Procholeragenoid --- Vibrio cholerae enterotoxin --- Medicine. --- Medical microbiology. --- Pharmacology. --- Food --- Biochemistry. --- Cell biology. --- Microbiology. --- Biomedicine. --- Medical Microbiology. --- Food Science. --- Biochemistry, general. --- Cell Biology. --- Pharmacology/Toxicology. --- Biotechnology. --- Bacterial toxins --- NAD-ADP-ribosyltransferase --- Food science. --- Cytology. --- Toxicology. --- Chemicals --- Pharmacology --- Poisoning --- Poisons --- Cell biology --- Cellular biology --- Cells --- Cytologists --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Chemistry --- Medical sciences --- Science --- Microbial biology --- Microorganisms --- Toxicology --- Composition --- Food—Biotechnology. --- Drug effects --- Medical pharmacology --- Chemotherapy --- Drugs --- Pharmacy --- Physiological effect