Oxygen delivery in perfused rat kidney: NADH fluorescence and renal functional state.
Changes in steady-state levels of reduced pyridine nucleotide (PN) recorded by continuous monitoring of surface fluorescence were correlated with changes in physiological function of perfused rat kidneys when subjected to anoxia, ischemia, hypothermia, variations in perfusion pressure, inhibition of Na-K ATPase, and uncoupling of oxidative phosphorylation. Biphasic responses of PN reduction and oxidation during ischemic cycles at varying temperatures and anoxic cycles at different perfusion pressures demonstrated the presence of two different cell populations in the kidney cortex, those with sufficient oxygen and those without. The magnitude of PN fluorescence change during ischemia increased with decreasing temperature demonstrating better tissue oxygenation during hypothermia. The measurement of mitochondrial NADH oxidation in the perfused kidney during transitions from CO anoxia to normoxia was made possible by flash photolytic activation of mitochondrial electron transport. The half time for NADH oxidation (125 ms) was independent of the rate of oxygen delivery while the initial rate and extent of reaction was faster and steeper, respectively, at higher perfusion pressure, due to a better tissue oxygenation and faster CO washout.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D004579:Electron Transport; D003576:Electron Transport Complex IV / Q000378:metabolism; D005470:Fluorometry; D066298:In Vitro Techniques; D007668:Kidney / Q000187:drug effects / Q000378:metabolism / Q000502:physiology*; D008297:Male; D008928:Mitochondria / Q000378:metabolism; D009243:NAD; D010042:Ouabain / Q000494:pharmacology; D010084:Oxidation-Reduction; D010085:Oxidative Phosphorylation; D010101:Oxygen Consumption; D010416:Pentachlorophenol / Q000494:pharmacology; D010477:Perfusion; D051381:Rats; D013696:Temperature
D009243:NAD; D010042:Ouabain; D010416:Pentachlorophenol; D003576:Electron Transport Complex IV; D000251:Adenosine Triphosphatases