Abstract
We investigated the morphologic changes in the sarcoplasmic reticulum (SR) in acute myocardial ischemia, induced by occlusion of the coronary artery in the canine heart, by freeze-fracture of SR in situ and in vitro, and they were compared to the alterations in Ca++-stimulated ATPase activity and protein composition of the isolated SR. Both SR in situ and the isolated SR exhibited typical intramembranous particles with diameters of 70 to 90 A in freeze-fracture replicas. The intramembranous particle density of the P face in SR in situ was 3,319 +/- 75 (mean +/- SE) per micrometer2 and that in the isolated SR was 2,667 +/- 60; particles were more numerous on the concave (P) face than on the convex (E) face. In ischemia for 30 to 60 min a significant decrease in the number of particles was found in SR in situ, and the corresponding change was noted in the isolated SR. Simultaneous decreases in Ca++-stimulated ATPase activity and the major ATPase protein of the SR were recognized. The close correlation of the changing pattern between the reduction in Ca++-ATPase and that in intramembranous particle density during ischemia supports the suggestion that a large part of the intramembranous particles represent ATPase protein itself. Decrease in the SR membrane particles strongly suggests the degradation of ATPase protein in the process of ischemic myocardial injury.
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