Prehibernation and hibernation effects on the D-3-hydroxybutyrate dehydrogenase of the heavy and light mitochondria from liver jerboa (Jaculus orientalis) and related metabolism.
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.
Mountassif
Driss
D
Laboratoire de Biochimie et de Biologie Moléculaire, Faculté des Sciences, Université Hassan II-Aïn Chock-Casablanca, km 8, route d'El Jadida BP. 5366, Casablanca, Morocco. drissmountassif@yahoo.fr
Kabine
Mostafa
M
Latruffe
Norbert
N
El Kebbaj
M'hammed Saïd
MS
D000818:Animals; D005455:Fluorescent Antibody Technique; D006605:Hibernation / Q000502:physiology*; D006884:Hydroxybutyrate Dehydrogenase / Q000378:metabolism*; D007700:Kinetics; D008930:Mitochondria, Liver / Q000201:enzymology* / Q000378:metabolism; D010743:Phospholipids / Q000378:metabolism; D051381:Rats; D012377:Rodentia / Q000145:classification / Q000378:metabolism*
D010743:Phospholipids; D006884:Hydroxybutyrate Dehydrogenase