title: Hibernation impact on the catalytic activities of the mitochondrial D-3-hydroxybutyrate dehydrogenase in liver and brain tissues of jerboa (Jaculus orientalis).
abstract: BACKGROUND
  Jerboa (Jaculus orientalis) is a deep hibernating rodent native to subdesert highlands. During hibernation, a high level of ketone bodies i.e. acetoacetate (AcAc) and D-3-hydroxybutyrate (BOH) are produced in liver, which are used in brain as energetic fuel. These compounds are bioconverted by mitochondrial D-3-hydroxybutyrate dehydrogenase (BDH) E.C. 1.1.1.30. Here we report, the function and the expression of BDH in terms of catalytic activities, kinetic parameters, levels of protein and mRNA in both tissues i.e brain and liver, in relation to the hibernating process.
  
  
  RESULTS
  We found that: 1/ In euthemic jerboa the specific activity in liver is 2.4- and 6.4- fold higher than in brain, respectively for AcAc reduction and for BOH oxidation. The same differences were found in the hibernation state. 2/ In euthermic jerboa, the Michaelis constants, KM BOH and KM NAD+ are different in liver and in brain while KM AcAc, KM NADH and the dissociation constants, KD NAD+and KD NADH are similar. 3/ During prehibernating state, as compared to euthermic state, the liver BDH activity is reduced by half, while kinetic constants are strongly increased except KD NAD+. 4/ During hibernating state, BDH activity is significantly enhanced, moreover, kinetic constants (KM and KD) are strongly modified as compared to the euthermic state; i.e. KD NAD+ in liver and KM AcAc in brain decrease 5 and 3 times respectively, while KD NADH in brain strongly increases up to 5.6 fold. 5/ Both protein content and mRNA level of BDH remain unchanged during the cold adaptation process.
  
  
  CONCLUSIONS
  These results cumulatively explained and are consistent with the existence of two BDH enzymatic forms in the liver and the brain. The apoenzyme would be subjected to differential conformational folding depending on the hibernation state. This regulation could be a result of either post-translational modifications and/or a modification of the mitochondrial membrane state, taking into account that BDH activity is phospholipid-dependent.
authors.affiliation: LBMC (GDR-CNRS n degrees 2583), Université de Bourgogne, Faculté des Sciences Gabriel, 6, Boulevard Gabriel, 21000 Dijon, France. mkabine@hotmail.com
authors.forename: Mostafa
authors.initials: M
authors.lastname: Kabine
authors.forename: M'hammed Saïd
authors.initials: MS
authors.lastname: El Kebbaj
authors.forename: Assia
authors.initials: A
authors.lastname: Hafiani
authors.forename: Norbert
authors.initials: N
authors.lastname: Latruffe
authors.forename: Mustapha
authors.initials: M
authors.lastname: Cherkaoui-Malki
mesh_terms: D000818:Animals; D015152:Blotting, Northern; D015153:Blotting, Western; D001921:Brain / Q000201:enzymology*; D002384:Catalysis; D006605:Hibernation; D006884:Hydroxybutyrate Dehydrogenase / Q000235:genetics / Q000378:metabolism*; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008297:Male; D008928:Mitochondria / Q000201:enzymology*; D012333:RNA, Messenger / Q000378:metabolism; D012377:Rodentia / Q000378:metabolism*
chemical_list: D012333:RNA, Messenger; D006884:Hydroxybutyrate Dehydrogenase