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12 results on '"Laboratoire Biochimie et Biologie Moléculaire (LBBM)"'

1. Differential Regulation of Peroxisome Proliferator-Activated Receptor (PPAR)-α1 and Truncated PPARα2 as an Adaptive Response to Fasting in the Control of Hepatic Peroxisomal Fatty Acid β-Oxidation in the Hibernating Mammal

Author

Mustapha Cherkaoui-Malki, Norbert Latruffe, Mostafa Kabine, Zakaria El Kebbaj, Michel Dauça, M'Hammed Saïd El Kebbaj, Pierre Andreoletti, Driss Mountassif, Hervé Schohn, Laboratoire Biochimie et Biologie Moléculaire ( LBBM ), Université Hassan II, Lipides - Nutrition - Cancer (U866) ( LNC ), Université de Bourgogne ( UB ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon ( ENSBANA ), Proliférateurs de Peroxysomes - EA3446, Université Henri Poincaré - Nancy 1 ( UHP ), Laboratoire de Biochimie Moléculaire et Cellulaire ( LBMC ), Université de Bourgogne ( UB ), Bancod, Nathalie, Laboratoire Biochimie et Biologie Moléculaire (LBBM), Université Hassan II [Casablanca] (UH2MC), Lipides - Nutrition - Cancer (U866) (LNC), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon (ENSBANA), Université Henri Poincaré - Nancy 1 (UHP), Laboratoire de Biochimie Moléculaire et Cellulaire (LBMC), and Université de Bourgogne (UB)

Subjects
MESH: Oxidation-Reduction, Hibernation, MESH : Transcription Factors, MESH : Hibernation, MESH : Rodentia, MESH: Rodentia, Peroxisome proliferator-activated receptor, MESH: Protein Isoforms, MESH : Fasting, Clofibric Acid, Endocrinology, MESH : Lipid Metabolism, MESH : Mammals, Protein Isoforms, MESH: Animals, MESH: PPAR alpha, Receptor, MESH : Fatty Acids, Beta oxidation, MESH : Adaptation, Physiological, MESH: Lipid Metabolism, Hypolipidemic Agents, Mammals, chemistry.chemical_classification, MESH : Gene Expression Regulation, Fatty Acids, Fibric Acids, MESH: Transcription Factors, Fasting, MESH : Clofibric Acid, Peroxisome, MESH: Gene Expression Regulation, Adaptation, Physiological, MESH: Fatty Acids, Liver, lipids (amino acids, peptides, and proteins), MESH: Hibernation, Oxidation-Reduction, medicine.medical_specialty, MESH : PPAR alpha, MESH: Fasting, Rodentia, Biology, MESH: Mammals, MESH: Clofibric Acid, Internal medicine, Coactivator, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Peroxisomes, medicine, Animals, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, PPAR alpha, [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology, MESH : Oxidation-Reduction, MESH : Liver, MESH : Protein Isoforms, Lipid metabolism, Lipid Metabolism, MESH: Adaptation, Physiological, MESH: Peroxisomes, Gene Expression Regulation, chemistry, Nuclear receptor, MESH : Animals, MESH: Antilipemic Agents, MESH : Peroxisomes, MESH: Liver, MESH : Antilipemic Agents, Transcription Factors
Abstract

Seasonal obesity and fasting-associated hibernation are the two major metabolic events governing hepatic lipid metabolism in hibernating mammals. In this process, however, the role of the nuclear receptor known as peroxisome proliferator-activated receptor (PPAR)-α has not been elucidated yet. Here we show, as in human, that jerboa (Jaculus orientalis) liver expresses both active wild-type PPARα (PPARα1wt) and truncated PPARα forms and that the PPARα1wt to truncated PPARα2 ratio, which indicates the availability of active PPARα1wt, is differentially regulated during fasting-associated hibernation. Functional activation of hepatic jerboa PPARα, during prehibernating and hibernating states, was demonstrated by the induction of its target genes, which encode peroxisomal proteins such as acyl-CoA oxidase 1, peroxisomal membrane protein 70, and catalase, accompanied by a concomitant induction of PPARα thermogenic coactivator PPARγ coactivator-1α. Interestingly, sustained activation of PPARα by its hypolipidemic ligand, ciprofibrate, abrogates the adaptive fasting response of PPARα during prehibernation and overinduces its target genes, disrupting the prehibernation fattening process. In striking contrast, during fasting-associated hibernation, jerboas exhibit preferential up-regulation of hepatic peroxisomal fatty acid oxidation instead of the mitochondrial pathway, which is down-regulated. Taken together, our results strongly suggest that PPARα is subject to a hibernation-dependent splicing regulation in response to feeding-fasting conditions, which defines the activity of PPARα and the activation of its target genes during hibernation bouts of jerboas.Jerboa PPARα is subject to a hibernation-dependent splicing regulation in response to feeding-fasting conditions, which define activation of PPARα and its target genes.

Published
2008
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2. Structural and catalytic properties of the D-3-hydroxybutyrate dehydrogenase from Pseudomonas aeruginosa

Author

M'Hammed Saïd El Kebbaj, Norbert Latruffe, Mustapha Cherkaoui-Malki, Pierre Andreoletti, Driss Mountassif, Laboratoire Biochimie et Biologie Moléculaire ( LBBM ), Université Hassan II, Mathématiques - Analyse, Probabilités, Modélisation - Orléans ( MAPMO ), Université d'Orléans ( UO ) -Centre National de la Recherche Scientifique ( CNRS ), Lipides - Nutrition - Cancer (U866) ( LNC ), Université de Bourgogne ( UB ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon ( ENSBANA ), Laboratoire de Biochimie Moléculaire et Cellulaire ( LBMC ), Université de Bourgogne ( UB ), Laboratoire Biochimie et Biologie Moléculaire (LBBM), Université Hassan II [Casablanca] (UH2MC), Mathématiques - Analyse, Probabilités, Modélisation - Orléans (MAPMO), Centre National de la Recherche Scientifique (CNRS)-Université d'Orléans (UO), Lipides - Nutrition - Cancer (U866) (LNC), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon (ENSBANA), Laboratoire de Biochimie Moléculaire et Cellulaire (LBMC), and Université de Bourgogne (UB)

Subjects
Models, Molecular, MESH : Molecular Weight, MESH : Molecular Sequence Data, MESH : NAD, Protein Conformation, MESH: Amino Acid Sequence, Applied Microbiology and Biotechnology, Chromatography, Affinity, Protein structure, MESH: Protein Conformation, MESH: 3-Hydroxybutyric Acid, MESH : Bacterial Proteins, MESH : DNA, Bacterial, Peptide sequence, Polyacrylamide gel electrophoresis, MESH: Bacterial Proteins, MESH : Protein Conformation, chemistry.chemical_classification, 0303 health sciences, MESH : Sepharose, 3-Hydroxybutyric Acid, MESH: Molecular Weight, Sepharose, MESH : Amino Acid Sequence, MESH: NAD, General Medicine, MESH: Chromatography, Affinity, MESH : Pseudomonas aeruginosa, MESH : Chromatography, Affinity, Amino acid, Biochemistry, MESH: Pseudomonas aeruginosa, Pseudomonas aeruginosa, Electrophoresis, Polyacrylamide Gel, MESH: Biocatalysis, MESH: Models, Molecular, DNA, Bacterial, MESH: Sepharose, MESH : Models, Molecular, Molecular Sequence Data, MESH : Hydroxybutyrate Dehydrogenase, Biology, MESH : Electrophoresis, Polyacrylamide Gel, Microbiology, Cofactor, 03 medical and health sciences, Hydroxybutyrate Dehydrogenase, Affinity chromatography, Bacterial Proteins, MESH : 3-Hydroxybutyric Acid, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Amino Acid Sequence, [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology, 030304 developmental biology, MESH: Molecular Sequence Data, 030306 microbiology, NAD, MESH: DNA, Bacterial, MESH: Hydroxybutyrate Dehydrogenase, Molecular Weight, Open reading frame, chemistry, biology.protein, Biocatalysis, NAD+ kinase, MESH : Biocatalysis, MESH: Electrophoresis, Polyacrylamide Gel
Abstract

International audience; To put forward BDH from Pseudomonas aeruginosa's enzymatic properties, we report a two-step purification of BDH and its gene sequencing allowing the investigation of its structural properties. Purification of BDH was achieved, using ammonium sulfate fractionation and Blue Sepharose CL-6B affinity chromatography. SDS-PAGE analysis reveals a MM of 29 kDa, whereas the native enzyme showed a MM of 120 kDa suggesting a homotetrameric structure. BDH encoding gene sequence shows a nucleotide open reading frame sequence of 771 bp encoding a 265 amino acid residues polypeptide chain. The modeling analysis of the three dimensional structure fits with the importance of amino acids in the catalysis reaction especially a strictly conserved tetrad. Amino-acid residues in interaction with the coenzyme NAD(+) were also identified.

Published
2010
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3. Structural and catalytic properties of the D-3-hydroxybutyrate dehydrogenase from Pseudomonas aeruginosa

Author

Mountassif , Driss, ANDREOLETTI , Pierre, Cherkaoui-Malki , Mustapha, Latruffe , Norbert, El Kebbaj , M'Hammed Saïd, Laboratoire Biochimie et Biologie Moléculaire (LBBM), Université Hassan II [Casablanca] (UH2MC), Mathématiques - Analyse, Probabilités, Modélisation - Orléans (MAPMO), Centre National de la Recherche Scientifique (CNRS)-Université d'Orléans (UO), Lipides - Nutrition - Cancer (U866) (LNC), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon (ENSBANA), Laboratoire de Biochimie Moléculaire et Cellulaire (LBMC), Université de Bourgogne (UB), Laboratoire Biochimie et Biologie Moléculaire ( LBBM ), Université Hassan II, Mathématiques - Analyse, Probabilités, Modélisation - Orléans ( MAPMO ), Université d'Orléans ( UO ) -Centre National de la Recherche Scientifique ( CNRS ), Lipides - Nutrition - Cancer (U866) ( LNC ), Université de Bourgogne ( UB ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon ( ENSBANA ), Laboratoire de Biochimie Moléculaire et Cellulaire ( LBMC ), and Université de Bourgogne ( UB )

Subjects
MESH : Molecular Weight, MESH: Sepharose, MESH : Molecular Sequence Data, MESH : NAD, MESH : Models, Molecular, MESH : Hydroxybutyrate Dehydrogenase, MESH: Amino Acid Sequence, MESH : Electrophoresis, Polyacrylamide Gel, MESH: Protein Conformation, MESH: 3-Hydroxybutyric Acid, MESH : 3-Hydroxybutyric Acid, MESH : Bacterial Proteins, MESH : DNA, Bacterial, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology, MESH: Bacterial Proteins, MESH : Protein Conformation, MESH : Sepharose, MESH: Molecular Sequence Data, MESH : Amino Acid Sequence, MESH: Molecular Weight, MESH: NAD, MESH : Pseudomonas aeruginosa, MESH: Chromatography, Affinity, MESH : Chromatography, Affinity, MESH: DNA, Bacterial, MESH: Hydroxybutyrate Dehydrogenase, MESH: Pseudomonas aeruginosa, MESH : Biocatalysis, MESH: Biocatalysis, MESH: Models, Molecular, MESH: Electrophoresis, Polyacrylamide Gel
Abstract

International audience; To put forward BDH from Pseudomonas aeruginosa's enzymatic properties, we report a two-step purification of BDH and its gene sequencing allowing the investigation of its structural properties. Purification of BDH was achieved, using ammonium sulfate fractionation and Blue Sepharose CL-6B affinity chromatography. SDS-PAGE analysis reveals a MM of 29 kDa, whereas the native enzyme showed a MM of 120 kDa suggesting a homotetrameric structure. BDH encoding gene sequence shows a nucleotide open reading frame sequence of 771 bp encoding a 265 amino acid residues polypeptide chain. The modeling analysis of the three dimensional structure fits with the importance of amino acids in the catalysis reaction especially a strictly conserved tetrad. Amino-acid residues in interaction with the coenzyme NAD(+) were also identified.

Published
2010
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4. Sensitivity of liver metabolism in jerboa (Jaculus orientalis) to ciprofibrate, a peroxisome proliferator

Author

M'Hammed Saïd El Kebbaj, Driss Mountassif, Norbert Latruffe, Khadija Mounaji, Mostafa Kabine, Karima Mounchid, Laboratoire Biochimie et Biologie Moléculaire ( LBBM ), Université Hassan II, Laboratoire d'Histologie et Embryologie ( LHE ), Laboratoire de Physiologie et Génétique Moléculaire ( LPGM ), Lipides - Nutrition - Cancer (U866) ( LNC ), Université de Bourgogne ( UB ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon ( ENSBANA ), Laboratoire Biochimie et Biologie Moléculaire (LBBM), Université Hassan II [Casablanca] (UH2MC), Laboratoire d'Histologie et Embryologie (LHE), Laboratoire de Physiologie et Génétique Moléculaire [Casablanca] (LPGM), Faculté des Sciences Aïn Chock [Casablanca] (FSAC), Université Hassan II [Casablanca] (UH2MC)-Université Hassan II [Casablanca] (UH2MC), Lipides - Nutrition - Cancer (U866) (LNC), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon (ENSBANA), and Latruffe, Norbert

Subjects
Cancer Research, medicine.medical_specialty, D-3-hydroxybutyrate dehydrogenase, Dehydrogenase, Biochemistry, Jaculus orientalis, chemistry.chemical_compound, ciprofibrate, antioxidant enzymes, Internal medicine, Genetics, medicine, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, clinical enzymes, Molecular Biology, [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology, subcellular marker, biology, Liver cell, Peroxisome, Malondialdehyde, Endocrinology, Oncology, chemistry, Catalase, biology.protein, Ketone bodies, Molecular Medicine, NAD+ kinase, Ciprofibrate, medicine.drug
Abstract

International audience; Ciprofibrate is a well-known drug used to normalize lipid parameters and fibrinogen in atherosclerosis patients. In laboratory rodents such as rats or mice, ciprofibrate exhibits peroxisome proliferator activity. However, to date, no clear alterations or side effects caused by ciprofibrate have been noted in humans. In order to further investigate such possible relationships, we studied the effects of sustained ciprofibrate treatment in jerboas (Jaculus orientalis). In these rodents, ciprofibrate does not induce hepatomegaly or promote liver cell DNA replication, confirming that this species more closely resembles humans than do rats or mice. The jerboas were treated daily with ciprofibrate at 3 mg/kg body weight for 4 weeks. Subcellular markers, clinical enzymes and enzymatic antioxidant defenses were then assessed. The results showed a strong decrease in peroxisomal catalase activity and an increase in the level of malondialdehyde (a stress biomarker). Moreover, ciprofibrate in vivo and in vitro inhibited D-3-hydroxybutyrate dehydrogenase, a mitochondrial enzyme of the ketone body interconversion that is important in redox balance (NAD+/NADH+H+ ratio). In conclusion, under these conditions, ciprofibrate induced alterations in the liver oxidative metabolism.

Published
2009
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5. D-3-hydroxybutyrate oxidation in mitochondria by D-3- Hydroxybutyrate dehydrogenase in Tetrahymena pyriformis

Author

Akil, Omar, El Kebbaj, Zakaria, Latruffe, Norbert, El Kebbaj, M'Hammed Saïd, Latruffe, Norbert, Laboratoire Biochimie et Biologie Moléculaire ( LBBM ), Université Hassan II, Lipides - Nutrition - Cancer (U866) ( LNC ), Université de Bourgogne ( UB ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon ( ENSBANA ), Laboratoire Biochimie et Biologie Moléculaire (LBBM), Université Hassan II [Casablanca] (UH2MC), Lipides - Nutrition - Cancer (U866) (LNC), and Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon (ENSBANA)

Subjects
[SDV.BA] Life Sciences [q-bio]/Animal biology, [SDV.BA]Life Sciences [q-bio]/Animal biology, [ SDV.BA ] Life Sciences [q-bio]/Animal biology
Abstract

International audience; Tetrahymena pyriformis a ciliated protozoan, is considered a good indicator of water pollution. However its energy supply is poorly understood. This work was focused on the metabolism of hydroxybutyrate through the study of the membrane bound mitochondrial NAD+-dependent D-3-hydroxybutyrate dehydrogenase (EC. 1.1.1.30) (BDH), a ketone body catalysing enzyme involvedin the interconversion of D-3-hydroxybutyrate to acetoacetate. Due to lack of informations, the physico-chemical properties and kinetic parameters of the enzyme were examined. The results are the following: 1) D-3-hydroxybutyrate is a good substrate for mitochondria. 2) The enzyme catalytic process follows a bi bi-ordered mechanism where the coenzyme binds first, then allowing the substrate linkage to the active site. 3) Two optimal pH values of 8 and 6.5 corresponding to D-3-hydroxybutyrate oxidation and to acetoacetate reduction respectively. On the other hand, pH changes affect the coenzyme binding to the active site. 4) The BDH activity was found strongly linked to submitochondrial vesicles indicating that the protozoan enzyme is membranous and could require lipids for its function as well as it is for the mammalian enzyme. Moreover, an optimal temperature (40°C) and a break appearing in the Arrhenius plot at 19°C were found. The break suggests a membrane lipid fluidity-dependency of BDH conformational change. 5) Several ligands of the active site including methylmalonate and succinate modulate the BDH activity and are competitive inhibitors toward D-3-hydroxybutyrate. 6) Divalent cations, Mg2+, Mn2+ and Zn2+ protect BDH against thermal inactivation. The protection is the strongest in the presence of Zn2+. Moreover, Ca2+ and Mg2+ are enzyme activators and modulate the substrate binding to the active site. On the other hand, EDTA, a chelating agent, inhibits the enzyme but prevents inhibition by substrate excess. This work provides new insights on the energy metabolism of T. pyriformis wild strain where D-3-hydroxybutyrate is a choice substrate where the properties of BDH have been established especially the activating role of non heavy divalent cations.

Published
2009

6. Immunoaffinity purification and characterization of mitochondrial membrane-bound D-3-hydroxybutyrate dehydrogenase from Jaculus orientalis

Author

Mustapha Cherkaoui-Malki, Pierre Andreoletti, Driss Mountassif, Adnane Moutaouakkil, Zakaria El Kebbaj, M'Hammed Saïd El Kebbaj, Norbert Latruffe, Laboratoire Biochimie et Biologie Moléculaire ( LBBM ), Université Hassan II, Lipides - Nutrition - Cancer (U866) ( LNC ), Université de Bourgogne ( UB ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon ( ENSBANA ), Latruffe, Norbert, Laboratoire Biochimie et Biologie Moléculaire (LBBM), Université Hassan II [Casablanca] (UH2MC), Lipides - Nutrition - Cancer (U866) (LNC), and Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon (ENSBANA)

Subjects
lcsh:Animal biochemistry, MESH : Aged, MESH : Rodentia, MESH: Rodentia, MESH: Base Sequence, Biochemistry, MESH: Lipid Peroxidation, MESH : Information Services, Antigen-Antibody Reactions, MESH: Health Education, Epitopes, MESH: Organizations, MESH: Libraries, MESH: Antigen-Antibody Reactions, lcsh:QD415-436, MESH: Animals, MESH : Organizations, MESH : Physician's Role, MESH: Bacterial Proteins, Immunosorbent Techniques, chemistry.chemical_classification, MESH: Conserved Sequence, Methodology Article, MESH : Computer Communication Networks, MESH: Chromatography, Affinity, MESH : Pseudomonas aeruginosa, MESH : Chromatography, Affinity, MESH : Immunosorbent Techniques, MESH: Ethnic Groups, MESH : Ethnic Groups, MESH: Epitopes, MESH : Patient Satisfaction, MESH : United States, MESH: Mitochondria, MESH : Antigen-Antibody Reactions, Molecular Sequence Data, MESH : Hydroxybutyrate Dehydrogenase, MESH: Sequence Alignment, Rodentia, MESH: Information Services, MESH : Epitopes, lcsh:Biochemistry, MESH : Mitochondrial Membranes, Bacterial Proteins, MESH : Conserved Sequence, Complementary DNA, MESH : Libraries, Molecular Biology, [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology, MESH: Immunosorbent Techniques, MESH: Molecular Sequence Data, MESH: Humans, MESH : Consumer Participation, MESH : Humans, MESH: Adult, MESH: Patient Satisfaction, MESH: Hydroxybutyrate Dehydrogenase, MESH: Consumer Participation, chemistry, Lipid Peroxidation, MESH: Female, MESH: Liver, MESH : Sequence Analysis, DNA, MESH: Continental Population Groups, MESH: Sequence Analysis, DNA, MESH : Molecular Sequence Data, Dehydrogenase, Chromatography, Affinity, MESH: Mitochondrial Membranes, MESH: Antibodies, Bacterial, MESH : Bacterial Proteins, MESH : Female, MESH: Computer Communication Networks, Conserved Sequence, MESH: Aged, biology, MESH : Lipid Peroxidation, MESH : Sequence Alignment, MESH: Physician's Role, MESH : Adult, Antibodies, Bacterial, Mitochondria, Amino acid, Liver, Mitochondrial Membranes, Pseudomonas aeruginosa, MESH: Pseudomonas aeruginosa, MESH : Mitochondria, MESH : Mass Media, MESH: Mass Media, MESH : Male, Hydroxybutyrate Dehydrogenase, Affinity chromatography, MESH : Health Education, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, MESH: United States, Animals, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, MESH : Antibodies, Bacterial, lcsh:QP501-801, Jaculus orientalis, MESH : Continental Population Groups, Base Sequence, MESH : Liver, Sequence Analysis, DNA, biology.organism_classification, Molecular biology, MESH: Male, Enzyme, Polyclonal antibodies, biology.protein, MESH : Base Sequence, NAD+ kinase, MESH : Animals, Sequence Alignment
Abstract

Background The interconversion of two important energy metabolites, 3-hydroxybutyrate and acetoacetate (the major ketone bodies), is catalyzed by D-3-hydroxybutyrate dehydrogenase (BDH1: EC 1.1.1.30), a NAD+-dependent enzyme. The eukaryotic enzyme is bound to the mitochondrial inner membrane and harbors a unique lecithin-dependent activity. Here, we report an advanced purification method of the mammalian BDH applied to the liver enzyme from jerboa (Jaculus orientalis), a hibernating rodent adapted to extreme diet and environmental conditions. Results Purifying BDH from jerboa liver overcomes its low specific activity in mitochondria for further biochemical characterization of the enzyme. This new procedure is based on the use of polyclonal antibodies raised against BDH from bacterial Pseudomonas aeruginosa. This study improves the procedure for purification of both soluble microbial and mammalian membrane-bound BDH. Even though the Jaculus orientalis genome has not yet been sequenced, for the first time a D-3-hydroxybutyrate dehydrogenase cDNA from jerboa was cloned and sequenced. Conclusion This study applies immunoaffinity chromatography to purify BDH, the membrane-bound and lipid-dependent enzyme, as a 31 kDa single polypeptide chain. In addition, bacterial BDH isolation was achieved in a two-step purification procedure, improving the knowledge of an enzyme involved in the lipid metabolism of a unique hibernating mammal. Sequence alignment revealed conserved putative amino acids for possible NAD+ interaction.

Published
2008
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7. Prehibernation and hibernation effects on the D-3-hydroxybutyrate dehydrogenase of the heavy and light mitochondria from liver jerboa (Jaculus orientalis) and related metabolism

Author

Driss Mountassif, Norbert Latruffe, M'Hammed Saïd El Kebbaj, Mostafa Kabine, Laboratoire Biochimie et Biologie Moléculaire ( LBBM ), Université Hassan II, Lipides - Nutrition - Cancer (U866) ( LNC ), Université de Bourgogne ( UB ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon ( ENSBANA ), Latruffe, Norbert, Laboratoire Biochimie et Biologie Moléculaire (LBBM), Université Hassan II [Casablanca] (UH2MC), Lipides - Nutrition - Cancer (U866) (LNC), and Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon (ENSBANA)

Subjects
Hibernation, MESH: Rats, MESH : Hibernation, MESH : Hydroxybutyrate Dehydrogenase, MESH : Rodentia, MESH: Rodentia, Fluorescent Antibody Technique, Mitochondria, Liver, Rodentia, Dehydrogenase, Mitochondrion, Biochemistry, MESH : Phospholipids, Hydroxybutyrate Dehydrogenase, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Animals, MESH: Animals, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Inner mitochondrial membrane, MESH: Fluorescent Antibody Technique, Jaculus orientalis, [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Phospholipids, MESH: Phospholipids, chemistry.chemical_classification, MESH: Kinetics, biology, MESH : Rats, General Medicine, Metabolism, biology.organism_classification, Rats, MESH: Hydroxybutyrate Dehydrogenase, Kinetics, MESH : Fluorescent Antibody Technique, Enzyme, chemistry, MESH : Mitochondria, Liver, Ketone bodies, MESH: Hibernation, sense organs, MESH : Animals, MESH : Kinetics, MESH: Mitochondria, Liver
Abstract

The D-3-hydroxybutyrate dehydrogenase (BDH) (EC 1.1.1.30) from liver jerboa (Jaculus orientalis), a ketone body converting enzyme in mitochondria, in two populations of mitochondria (heavy and light) has been studied in different jerboa states (euthermic, prehibernating and hibernating). The results reveal: (1) important variations between states in terms of ketones bodies, glucose and lipid levels; (2) significant differences between the BDH of the two mitochondrial populations in term of protein expression and kinetic properties. These results suggest that BDH leads an important conformational change depending on the physiological state of jerboa. This BDH structural change could be the consequence of the lipid composition modifications in inner mitochondrial membrane leading to changes in BDH catalytic properties.

Published
2007
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8. Clarin-1 gene transfer rescues auditory synaptopathy in model of Usher syndrome

Author

Omar Akil, Didier Dulon, Samantha Papal, Vincent Michel, Paul Avan, Alice Emptoz, Aziz El-Amraoui, Olinda Alegria-Prévot, Sedigheh Delmaghani, Pranav Patni, Lawrence R. Lustig, Christine Petit, Alain Aghaie, Abdelaziz Tlili, Elise Pepermans, Yohan Bouleau, Saaid Safieddine, Margot Tertrais, Matteo Cortese, Philippe F.Y. Vincent, Neurophysiologie de la Synapse Auditive, Université de Bordeaux (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-CHU de Bordeaux Pellegrin [Bordeaux]-Neuroscience Institute, Génétique et Physiologie de l'Audition, Institut Pasteur [Paris] (IP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU), ED 515 - Complexité du vivant, Université Pierre et Marie Curie - Paris 6 (UPMC), University of California [San Francisco] (UC San Francisco), University of California (UC), Columbia University [New York], Equipe Biophysique Neurosensorielle [Neuro-Dol], Neuro-Dol (Neuro-Dol), Université d'Auvergne - Clermont-Ferrand I (UdA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université d'Auvergne - Clermont-Ferrand I (UdA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Neuro-Dol (Neuro-Dol), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Clermont Auvergne [2017-2020] (UCA [2017-2020])-Université Clermont Auvergne [2017-2020] (UCA [2017-2020]), Centre National de la Recherche Scientifique (CNRS), Collège de France - Chaire Génétique et physiologie cellulaire, Collège de France (CdF (institution)), SP and MC benefited from fellowships from the Ministry of National Education, Research and Technology of France, and PP from the European Union’s Horizon 2020 Marie Sklodowska-Curie grant 665807. This work was supported by European Research Council (ERC) advanced grant 'Hair bundle' (ERC-2011-AdG 294570), the European Union Seventh Framework Programme under grant agreement HEALTH-F2-2010-242013 (TREATRUSH), the French National Research Agency (ANR) as part of the second 'Investissements d’Avenir' programme (light4deaf, ANR-15-RHUS-0001), ANR-HearInNoise-(ANR-17-CE16-0017), LHW-Stiftung, FAUN Stiftung (Suchert Foundation), LABEX Life-senses (ANR-10-LABX-65), and a grant from the Fondation Pour l’Audition to DD (2015-APA Research Grant)., We thank Jean-Pierre Hardelin and Jacques Boutet de Monvel for critical reading of the manuscript., ANR-15-RHUS-0001,LIGHT4DEAF,ECLAIRER LA SURDITÉ : UNE APPROCHE HOLISTIQUE DU SYNDROME D'USHER(2015), ANR-11-IDEX-0004,SUPER,Sorbonne Universités à Paris pour l'Enseignement et la Recherche(2011), European Project: 294570,EC:FP7:ERC,ERC-2011-ADG_20110310,HAIRBUNDLE(2012), European Project: 242013,EC:FP7:HEALTH,FP7-HEALTH-2009-single-stage,TREATRUSH(2010), Neuroscience Institute-Université de Bordeaux ( UB ) -CHU de Bordeaux Pellegrin [Bordeaux]-Institut National de la Santé et de la Recherche Médicale ( INSERM ), Université Pierre et Marie Curie - Paris 6 ( UPMC ) -Collège de France ( CdF ) -Institut Pasteur [Paris]-Institut National de la Santé et de la Recherche Médicale ( INSERM ), Biologie du fruit et pathologie ( BFP ), Université Bordeaux Segalen - Bordeaux 2-Institut National de la Recherche Agronomique ( INRA ) -Université Sciences et Technologies - Bordeaux 1, Laboratoire Biochimie et Biologie Moléculaire ( LBBM ), Université Hassan II, Neuro-Dol ( Neuro-Dol ), Université d'Auvergne - Clermont-Ferrand I ( UdA ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Université d'Auvergne - Clermont-Ferrand I ( UdA ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Neuro-Dol - Clermont Auvergne ( Neuro-Dol ), Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Université Clermont Auvergne ( UCA ) -Université Clermont Auvergne ( UCA ), Comité Français de la Semoulerie Industrielle ( CFSI ), Génétique et physiologie de l'audition, This work was supported by European Research Council (ERC) advanced grant 'Hair bundle' (ERC-2011-AdG 294570), the European Union Seventh Framework Programme under grant agreement HEALTH-F2-2010-242013 (TREATRUSH), the French National Research Agency (ANR) as part of the second 'Investissements d’Avenir' programme (light4deaf, ANR-15-RHUS-0001), ANR-HearInNoise-(ANR-17-CE16-0017), LHW-Stiftung, FAUN Stiftung (Suchert Foundation), LABEX Life-senses (ANR-10-LABX-65), and a grant from the Fondation Pour l’Audition to DD (2015-APA Research Grant)., ANR-15-RHUS-0001,LIGHT4DEAF,ECLAIRER LA SURDITÉ : UNE APPROCHE HOLISTIQUE DU SYNDROME D'USHER ( 2015 ), ANR-17-CE16-0017,HearInNoise,Surdité d’apparition tardive et progressive: de la physiopathologie à la thérapie ( 2017 ), ANR-11-IDEX-0004-02/10-LABX-0065,LIFESENSES,DES SENS POUR TOUTE LA VIE ( 2011 ), European Project : 294570,EC:FP7:ERC,ERC-2011-ADG_20110310,HAIRBUNDLE ( 2012 ), European Project : 242013,EC:FP7:HEALTH,FP7-HEALTH-2009-single-stage,TREATRUSH ( 2010 ), Neuroscience Institute-Université de Bordeaux (UB)-CHU de Bordeaux Pellegrin [Bordeaux]-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut Pasteur [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU), University of California [San Francisco] (UCSF), University of California, Chaire Génétique et physiologie cellulaire, Oficjalska, Danuta, ECLAIRER LA SURDITÉ : UNE APPROCHE HOLISTIQUE DU SYNDROME D'USHER - - LIGHT4DEAF2015 - ANR-15-RHUS-0001 - RHUS - VALID, Sorbonne Universités à Paris pour l'Enseignement et la Recherche - - SUPER2011 - ANR-11-IDEX-0004 - IDEX - VALID, Assembling the puzzle of the operating auditory hair bundle - HAIRBUNDLE - - EC:FP7:ERC2012-12-01 - 2017-11-30 - 294570 - VALID, and Fighting blindness of Usher syndrome: diagnosis, pathogenesis and retinal treatment (TreatRetUsher) - TREATRUSH - - EC:FP7:HEALTH2010-02-01 - 2014-01-31 - 242013 - VALID

Subjects
0301 basic medicine, Calcium Channels, L-Type, Usher syndrome, PDZ domain, Cell Cycle Proteins, AMPA receptor, Ribbon synapse, Biology, 03 medical and health sciences, Mice, 0302 clinical medicine, Gene therapy, Postsynaptic potential, Hair Cells, Auditory, medicine, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, otorhinolaryngologic diseases, Animals, Humans, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Receptors, AMPA, Mice, Knockout, Gene Transfer Techniques, Membrane Proteins, General Medicine, Genetic Therapy, Dependovirus, medicine.disease, Cell biology, Cytoskeletal Proteins, Disease Models, Animal, Calcium channels, 030104 developmental biology, medicine.anatomical_structure, Knockout mouse, Synapses, Synaptopathy, Human medicine, Hair cell, [ SCCO ] Cognitive science, Carrier Proteins, Usher Syndromes, 030217 neurology & neurosurgery, Research Article, Neuroscience
Abstract

Clarin-1, a tetraspan-like membrane protein defective in Usher syndrome type IIIA (USH3A), is essential for hair bundle morphogenesis in auditory hair cells. We report a new synaptic role for clarin-1 in mouse auditory hair cells elucidated by characterization of Clrn1 total (Clrn1(ex4-/-)) and postnatal hair cell-specific conditional (Clrn1(ex4fl/fl) Myo15-Cre(+/-)) knockout mice. Clrn1(ex4-/-) mice were profoundly deaf, whereas Clrn1(ex4fl/fl) Myo15-Cre(+/-) mice displayed progressive increases in hearing thresholds, with, initially, normal otoacoustic emissions and hair bundle morphology. Inner hair cell (IHC) patch-clamp recordings for the 2 mutant mice revealed defective exocytosis and a disorganization of synaptic F-actin and Ca(V)1.3 Ca2+ channels, indicative of a synaptopathy. Postsynaptic defects were also observed, with an abnormally broad distribution of AMPA receptors associated with a loss of afferent dendrites and defective electrically evoked auditory brainstem responses. Protein-protein interaction assays revealed interactions between clarin-1 and the synaptic Ca(V)1.3 Ca2+ channel complex via the Ca-V beta(2) auxiliary subunit and the PDZ domain-containing protein harmonin (defective in Usher syndrome type IC). Cochlear gene therapy in vivo, through adeno-associated virus-mediated Clrn1 transfer into hair cells, prevented the synaptic defects and durably improved hearing in Clrn1(ex4fl/fl) Myo15-Cre(+/-) mice. Our results identify clarin-1 as a key organizer of IHC ribbon synapses, and suggest new treatment possibilities for USH3A patients.

Published
2018
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9. Effect of Melatonin Implants during the Non-Breeding Season on the Onset of Ovarian Activity and the Plasma Prolactin in Dromedary Camel

Author

Hanan Bouâouda, Mounir Ouzir, Khalid El Allali, Mohammed El Mzibri, Adnane Moutaouakkil, Mohamed Rachid Achaâban, Béatrice Bothorel, Ahmed Tibary, A Sghiri, Najia El Abbadi, Paul Pévet, Institut des Neurosciences Cellulaires et Intégratives (INCI), Université Louis Pasteur - Strasbourg I-Centre National de la Recherche Scientifique (CNRS), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS), Biology and Mediacl Research Unit, Centre National de l'Energie, des Sciences et Techniques Nucléaires, Laboratoire Biochimie et Biologie Moléculaire (LBBM), Université Hassan II [Casablanca] (UH2MC), Harvard Medical School [Boston] (HMS), Université Mohammed V de Rabat [Agdal], Centre National de l'Energie des Sciences et des Techniques Nucléaires (CNESTEN), and Washington State University (WSU)

Subjects
medicine.medical_specialty, endocrine system, Dromedary camel, [SDV]Life Sciences [q-bio], melatonin, Melatonin, 03 medical and health sciences, 0302 clinical medicine, Internal medicine, Follicular phase, medicine, Seasonal breeder, Melatonin secretion, breeding season, ComputingMilieux_MISCELLANEOUS, Original Research, photoperiodism, [SDV.BA.MVSA]Life Sciences [q-bio]/Animal biology/Veterinary medicine and animal Health, 030219 obstetrics & reproductive medicine, lcsh:Veterinary medicine, General Veterinary, dromedary camel, business.industry, ultrasonography, Plasma prolactin, Endocrinology, lcsh:SF600-1100, Veterinary Science, Implant, business, ovarian activity, 030217 neurology & neurosurgery, hormones, hormone substitutes, and hormone antagonists, medicine.drug
Abstract

To examine a possible control of reproductive seasonality by melatonin, continual-release subcutaneous melatonin implants were inserted 4.5 months before the natural breeding season (October–April) into female camels (Melatonin-treated group). The animals were exposed to an artificial long photoperiod (16L:8D) for 41 days prior to implant placement to facilitate receptivity to the short-day signal that is expected with melatonin implants. The treated and control groups (untreated females) were maintained separately under outdoor natural conditions. Ovarian follicular development was monitored in both groups by transrectal ultrasonography and by plasma estradiol-17β concentrations performed weekly for 8 weeks and then for 14 weeks following implant insertion. Plasma prolactin concentrations were determined at 45 and 15 days before and 0, 14, 28, 56, and 98 days after implant insertion. Plasma melatonin concentration was determined to validate response to the artificial long photoperiod and to verify the pattern of release from the implants. Results showed that the artificial long photoperiod induced a melatonin secretion peak of significantly (P

Published
2018
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10. Biochemical and histological alterations of cellular metabolism from jerboa (Jaculus orientalis) by 2,4-dichlorophenoxyacetic acid: Effects on d-3-hydroxybutyrate dehydrogenase

Author

Khadija Mounaji, Norbert Latruffe, Driss Mountassif, Karima Mounchid, M'Hammed Saïd El Kebbaj, Mostafa Kabine, Laboratoire Biochimie et Biologie Moléculaire ( LBBM ), Université Hassan II, Laboratoire d'Histologie et Embryologie ( LHE ), Laboratoire de Physiologie et Génétique Moléculaire ( LPGM ), Laboratoire de Biochimie Moléculaire et Cellulaire ( LBMC ), Université de Bourgogne ( UB ), and Latruffe, Norbert

Subjects
medicine.medical_specialty, Histology, 2,4-Dichlorophenoxyacetic acid, Antioxidant, Health, Toxicology and Mutagenesis, medicine.medical_treatment, Biology, medicine.disease_cause, Jaculus orientalis, chemistry.chemical_compound, In vivo, Internal medicine, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, medicine, [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology, D-3-Hydroxybutyrate dehydrogenase, Cholesterol, General Medicine, Metabolism, Clinical parameters, biology.organism_classification, Endocrinology, chemistry, Biochemistry, Toxicity, Antioxidant enzymes, Subcellular markers, Agronomy and Crop Science, Oxidative stress
Abstract

International audience; 2,4-Dichlorophenoxyacetic acid (2,4D) is one of the widely used herbicide of the phenoxy family with possible startling number of adverse effects on species other than the weeds which is designed to kill. The effects of 2,4D were investigated in jerboa (Jaculus orientalis), a wild animal of subdesert highlands. The jerboas have been daily treated intraperitonally with 2,4D 3 mg/kg body weight for 4 weeks. Plasmatic markers, and antioxidants defences systems were assessed and histological alterations were evaluated. The in vivo and in vitro effects of 2,4D on the mitochondrial D-3-hydroxybutyrate dehydrogenase (BDH) were also determined. Our results showed a strong decrease of triglycerides level and HDL cholesterol and an increase in GOT level and LDL cholesterol. The microscopic evaluation showed that 2,4D induced necrosis of seminiferous tubules cells in testis, hyperplasia of hepatocytes in liver and presence of multinucleated giant cells in brain. The results show also an inhibitory effect on BDH in terms of activity and kinetic parameters. All of these results show that 2,4D induces toxicity which affects energy metabolism, morphological perturbation and oxidative stress.

Published
2008
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11. Structural and catalytic properties of the D-3-hydroxybutyrate dehydrogenase from Pseudomonas aeruginosa

Author

Mountassif, Driss, Andreoletti, Pierre, Cherkaoui-Malki, Mustapha, Latruffe, Norbert, El Kebbaj, M'Hammed Saïd, Latruffe, Norbert, Laboratoire Biochimie et Biologie Moléculaire (LBBM), Université Hassan II [Casablanca] (UH2MC), Mathématiques - Analyse, Probabilités, Modélisation - Orléans (MAPMO), Université d'Orléans (UO)-Centre National de la Recherche Scientifique (CNRS), Lipides - Nutrition - Cancer (U866) (LNC), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon (ENSBANA), Laboratoire de Biochimie Moléculaire et Cellulaire (LBMC), and Université de Bourgogne (UB)

Subjects
MESH: Sepharose, MESH: Molecular Sequence Data, MESH: Molecular Weight, MESH: NAD, MESH: Amino Acid Sequence, MESH: Chromatography, Affinity, MESH: DNA, Bacterial, MESH: Hydroxybutyrate Dehydrogenase, MESH: Protein Conformation, MESH: 3-Hydroxybutyric Acid, MESH: Pseudomonas aeruginosa, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, MESH: Bacterial Proteins, MESH: Biocatalysis, MESH: Models, Molecular, MESH: Electrophoresis, Polyacrylamide Gel
Abstract

International audience; To put forward BDH from Pseudomonas aeruginosa's enzymatic properties, we report a two-step purification of BDH and its gene sequencing allowing the investigation of its structural properties. Purification of BDH was achieved, using ammonium sulfate fractionation and Blue Sepharose CL-6B affinity chromatography. SDS-PAGE analysis reveals a MM of 29 kDa, whereas the native enzyme showed a MM of 120 kDa suggesting a homotetrameric structure. BDH encoding gene sequence shows a nucleotide open reading frame sequence of 771 bp encoding a 265 amino acid residues polypeptide chain. The modeling analysis of the three dimensional structure fits with the importance of amino acids in the catalysis reaction especially a strictly conserved tetrad. Amino-acid residues in interaction with the coenzyme NAD(+) were also identified.

Published
2010
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12. Characterization of two D-beta-hydroxybutyrate dehydrogenase populations in heavy and light mitochondria from jerboa (Jaculus orientalis) liver

Author

Mountassif , Driss, Kabine , Mostafa, Latruffe , Norbert, El Kebbaj , M'Hammed Saïd, Laboratoire Biochimie et Biologie Moléculaire ( LBBM ), Université Hassan II, Laboratoire de Biochimie Moléculaire et Cellulaire ( LBMC ), and Université de Bourgogne ( UB )

Subjects
MESH : Mitochondria, Liver, MESH : Hydroxybutyrate Dehydrogenase, MESH : Rodentia, MESH : Animals, MESH : Kinetics, [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology
Abstract

International audience; Mitochondrial membrane-bound and phospholipid-dependent D-beta-hydroxybutyrate dehydrogenase (BDH) (EC 1.1.1.30), a ketone body converting enzyme in mitochondria, has been studied in two populations of mitochondria (heavy and light) of jerboa (Jaculus orientalis) liver. The results reveal significant differences between the BDH of the two mitochondrial populations in terms of protein expression, kinetic parameters and physico-chemical properties. These results suggest that the beta-hydroxybutyrate dehydrogenases from heavy and light mitochondria are isoform variants. These differences in BDH distribution could be the consequence of cell changes in the lipid composition of the inner mitochondrial membrane of heavy and light mitochondria. These changes could modify both BDH insertion and BDH lipid-dependent catalytic properties.

Published
2006
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