Pathophysiological mechanisms of altered transmembrane potentials in diseased human atria.
The pathophysiological mechanisms of altered transmembrane potentials in diseased human atria were investigated in 20 patients who were divided into group A (normal) and group B (diseased). The electrophysiological data of right atrial tissues measured with glass microelectrodes included maximum diastolic potentials (MDP), action potential amplitudes (APA) and action potential durations at the time required for 50% repolarization (ADP 50%) and 75% repolarization (APD 75%). The sarcolemma isolated from atrial tissues was used for determination of the sarcolemmal Na+-K+ ATPase activities. Anionic molecular sites distributed in the sarcolemmal complex were characterized by cationized ferritins (CF). The electrophysiological data in groups A and B were: MDP -80.74 +/- 1.94 mV and -44.54 +/- 6.24 mV, APA 92.72 +/- 9.25 mV and 57.74 +/- 10.85 mV, APD 50% 42.48 +/- 6.63 msec and 210.34 +/- 36.38 msec and APD 75% 56.47 +/- 8.55 msec and 281.66 +/- 42.18 msec respectively. The difference in the Na+-K+ ATPase activities between groups A (15.37 +/- 0.46 mumole Pi/mg/hr) and B (12.55 +/- 0.4 mumole Pi/mg/hr) was highly significant. CF molecules were frequently seen to be more irregularly and loosely distributed in the sarcolemmal surfaces of group B atrial myocytes. Based on these results we conclude that depression of the sarcolemmal Na+-K+ ATPase activity and derangement of the anionic binding sites in the sarcolemmal surfaces play an important role in altering transmembrane potentials in diseased human atria.
D000293:Adolescent; D000328:Adult; D002648:Child; D003971:Diastole; D004594:Electrophysiology; D005260:Female; D005293:Ferritins / Q000378:metabolism; D006325:Heart Atria / Q000378:metabolism / Q000473:pathology / Q000503:physiopathology*; D006331:Heart Diseases / Q000378:metabolism / Q000473:pathology / Q000503:physiopathology*; D006651:Histocytochemistry; D006801:Humans; D008297:Male; D008564:Membrane Potentials; D012508:Sarcolemma / Q000201:enzymology / Q000648:ultrastructure; D000254:Sodium-Potassium-Exchanging ATPase / Q000032:analysis
D005293:Ferritins; D000254:Sodium-Potassium-Exchanging ATPase