Postanoxic recovery of spontaneously beating isolated atria: pH related role of adenylate kinase.
The functional activity, adenine nucleotides, and creatine phosphate content of spontaneously beating isolated rabbit atria were measured prior to anoxia, after 1 hr anoxia, and at the end of 1 hr reoxygenation at pH 6.7 and 7.2 During anoxia at pH 7.2 there was 13.3% loss of adenine nucleotides pool, 35.2% loss of ATP, 36.2% increase in ADP, 200% increase in AMP, and a decrease to 8.8% of CP assayed to the beating atria in oxygen. At pH 6.7 there was almost the same decrease in CP, about 10% decrease in ATP, no change in total adenine nucleotides, no change in AMP and a higher increase in ADP (88.7%). The postanoxic recovery was much more complete when the pH was 6.7 during anoxia, and the first 40 min of reoxygenation. The extent of recovery of functional activity correlated well with the level of ATP in all cases not CP. Since the adenylate kinase and ATPase activity both decrease at acidic pH, their combined diminution would tend to preserve the adenine nucleotide pool and thus the better recovery at pH 6.7, because of a decrease in energy demand and unavailability of AMP for the degradation process. This study also supports the notion of compartmented adenine nucleotides connected by the creatine phosphate-creatine energy shuttle.
D000263:Adenylate Kinase / Q000378:metabolism*; D000693:Anaerobiosis; D000818:Animals; D016275:Atrial Function; D006321:Heart / Q000502:physiology*; D006325:Heart Atria / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D000860:Hypoxia / Q000201:enzymology; D066298:In Vitro Techniques; D007700:Kinetics; D008297:Male; D009206:Myocardium / Q000201:enzymology*; D010770:Phosphotransferases / Q000378:metabolism*; D011817:Rabbits
D010770:Phosphotransferases; D000263:Adenylate Kinase