Effect of intermittent normobaric hypoxia on kinetic properties of mitochondrial enzymes.
We studied the effect of intermittent normobaric hypoxia on the formation of adaptive signs and state of mitochondrial enzymes in the cerebral cortex of rats with different resistance to hypoxia. Kinetic parameters for mitochondrial enzymes in the substrate region of the respiratory chain of the cerebral cortex underwent various changes in low resistant and highly resistant rats over the first 2 h after 1-h intermittent normobaric hypoxia. Low resistant animals were characterized by more effective functioning of rotenone-sensitive NADH-cytochrome C reductase and succinate-cytochrome C reductase under conditions of increased reduction status of the cell. These features correlated with the increase in the general resistance of animals. Significant changes in kinetic properties of mitochondrial enzymes and signs of the development of resistance were not found in highly resistant rats. Reciprocal relations between mitochondrial enzyme complexes in the substrate region of the respiratory chain probably play a role of the signal regulatory mechanism, which mediates tissue-specific and general resistance of rats under conditions of intermittent normobaric hypoxia. These effects did not depend on oxygenation of the inhaled gas mixture during the inter-hypoxic period.
Lukyanova
L D
LD
Institute of General Pathology and Pathophysiology, Russian Academy of Medical Sciences, Moscow.
Dudchenko
A M
AM
Tsybina
T A
TA
Germanova
E L
EL
Tkachuk
E N
EN
Erenburg
I V
IV
D000818:Animals; D002540:Cerebral Cortex / Q000201:enzymology; D004579:Electron Transport / Q000187:drug effects; D002534:Hypoxia, Brain / Q000201:enzymology*; D007700:Kinetics; D008297:Male; D008928:Mitochondria / Q000201:enzymology*; D009245:NADH Dehydrogenase / Q000378:metabolism; D051381:Rats; D012402:Rotenone / Q000494:pharmacology; D013384:Succinate Cytochrome c Oxidoreductase / Q000378:metabolism
D012402:Rotenone; D013384:Succinate Cytochrome c Oxidoreductase; D009245:NADH Dehydrogenase