作者: Philippe G. Bittar , Yves Charnay , Luc Pellerin , Constantin Bouras , Pierre J. Magistretti
DOI: 10.1097/00004647-199611000-00001
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摘要: In vertebrates, the interconversion of lactate and pyruvate is catalyzed by enzyme dehydrogenase. Two distinct subunits combine to form five tetrameric isoenzymes The LDH-5 subunit (muscle type) has higher maximal velocity (Vmax) present in glycolytic tissues, favoring formation from pyruvate. LDH-1 (heart inhibited therefore preferentially drives reaction toward production There mounting evidence indicating that during activation brain resorts transient processing glucose. Indeed, physiological stimulation been shown 1H-magnetic resonance spectroscopy. However, since whole-brain arteriovenous studies under basal conditions indicate a virtually complete oxidation glucose, vast proportion transiently formed likely be oxidized. These vivo data suggest may certain cells oxidized others. We set out determine whether two isoforms dehydrogenase are localized selective cell types human brain. report here characterization rat antisera, specific for dehydrogenase, respectively. Immunohistochemical, immunodot, western-blot analyses show these antisera specifically recognize their homologous antigens. Immunohistochemistry on 10 control cases demonstrated differential cellular distribution between both hippocampus occipital cortex: neurons exclusively stained with anti-LDH1 while astrocytes antibodies. observations support notion regulated flux neurons.