Sarcoplasmic reticulum function in determining atrioventricular contractile differences in rat heart.
The relationships between the contractile characteristics and the sarcoplasmic reticulum (SR) function of rat atrial and ventricular trabeculae were compared. The isometric developed tension (DT) and the rates of contraction (+ dT/dt) and relaxation (-dT/dt) normalized to cross-sectional area were 3.7, 2.2, and 1.8 times lower, respectively, in intact atrial strips compared with ventricular strips, whereas + dT/dt and -dT/dt (normalized to DT) were 2.3 and 2.8 times higher, respectively, in atria. Atria exhibited a maximal potentiation of DT after shorter rest periods than ventricles and a lower reversal for prolonged rest periods. Caffeine-induced tension transients in saponin-permeabilized fibers suggested that the Ca2+ concentration released in atrial myofibrils reached a lower maximum and decayed more slowly than in ventricular preparations. However, the tension-time integrals indicated an equivalent capacity of sequestrable Ca2+ in SR from both tissues. In atrial, as in ventricular myocardium, the SR Ca2+ uptake was more efficiently supported by ATP produced by the SR-bound MM form of creatine kinase (CK; MM-CK) than by externally added ATP, suggesting a tight functional coupling between the SR Ca2+ adenosinetriphosphatase (ATPase) and MM-CK. The maximal rate of oxalate-supported Ca2+ uptake was two times higher in atrial than in ventricular tissue homogenates. The SR Ca(2+)-ATPase 2a mRNA content normalized to 18S RNA was 38% higher in atria than in ventricles, whereas the amount of mRNA encoding the alpha-myosin heavy chain, calsequestrin, and the ryanodine receptor was similar in both tissues. Thus a lower amount of readily releasable Ca2+ together with a faster uptake rate may partly account for the shorter time course and lower tension development in intact atrial myocardium compared with ventricular myocardium.
Minajeva
A
A
Department of Pathological Physiology, Medical Faculty, University of Tartu, Estonia.
Kaasik
A
A
Paju
K
K
Seppet
E
E
Lompré
A M
AM
Veksler
V
V
Ventura-Clapier
R
R
D000818:Animals; D016275:Atrial Function; D002110:Caffeine / Q000494:pharmacology; D002118:Calcium / Q000378:metabolism; D000252:Calcium-Transporting ATPases / Q000096:biosynthesis; D002155:Calsequestrin / Q000096:biosynthesis; D003238:Connective Tissue / Q000502:physiology; D004558:Electric Stimulation; D005260:Female; D006321:Heart / Q000502:physiology*; D066298:In Vitro Techniques; D008297:Male; D018485:Muscle Fibers, Skeletal / Q000187:drug effects / Q000502:physiology; D009200:Myocardial Contraction / Q000187:drug effects / Q000502:physiology*; D009206:Myocardium / Q000378:metabolism; D018995:Myosin Heavy Chains / Q000096:biosynthesis; D012333:RNA, Messenger / Q000096:biosynthesis; D012337:RNA, Ribosomal, 18S / Q000096:biosynthesis; D051381:Rats; D017208:Rats, Wistar; D019837:Ryanodine Receptor Calcium Release Channel / Q000096:biosynthesis; D012519:Sarcoplasmic Reticulum / Q000187:drug effects / Q000502:physiology*; D014158:Transcription, Genetic; D016276:Ventricular Function
D002155:Calsequestrin; D012333:RNA, Messenger; D012337:RNA, Ribosomal, 18S; D019837:Ryanodine Receptor Calcium Release Channel; D002110:Caffeine; D018995:Myosin Heavy Chains; D000252:Calcium-Transporting ATPases; D002118:Calcium