Myocardial infarction alters myofilament calcium sensitivity and mechanical behavior of myocytes.

To determine whether myocardial infarction leads to alterations in myofilament isometric tension as a function of Ca2+ concentration, unloaded shortening velocity, and sarcomere compliance, these properties were examined in skinned myocytes 7 days after coronary artery occlusion. Changes in myofilament proteins were also evaluated Myocardial infarction was characterized by a 10-15% reduction in myofilament isometric tension at submaximum Ca2+ levels in the physiological range. However, developed tension at maximum activation was unaltered. Conversely, unloaded shortening velocity was decreased by 31% in the remaining viable cells, whereas resting tension was increased by 30-40%. The regulatory protein troponin I content was reduced, but phosphorylation of troponin I and troponin T was increased. Myosin isoenzymes and troponin T contents were not altered. In conclusion, molecular responses occurred acutely after myocardial infarction, and these adaptations may depress the mechanical behavior of the unaffected cells, contributing to acute impairment in global cardiac pump function beyond that resulting from myocyte loss.