Altered cytoskeletal protein synthesis in rat cardiac isografts.

Adult rats underwent surgical placement of heterotopic cardiac isografts. From 14 to 60 days postoperatively, native heart and transplanted heart protein synthesis was determined. Right ventricle and left ventricle free walls from native and transplanted hearts were dissected, minced into cubes, and incubated in medium containing sulfur-35 methionine. Tissue was harvested, washed, and homogenized in buffer and fractionated centrifugally. Specific radioactivity of polypeptides from transplant isograft right and left ventricle fractions were 6.36 +/- 5.1 and 4.93 +/- 3.6 (mean +/- SD, x 10(-6) cpm/mg protein), respectively. In contrast, native isograft right and left ventricle specific radioactivity was 1.71 +/- 1.49 and 1.07 +/- 0.88 (mean +/- SD, x 10(-6) cpm/mg protein), respectively. Autoradiograms of two-dimensional electrophoretograms revealed increased radiodensity of resolved polypeptides from transplanted and native hearts, which comigrated with nonsarcomeric (beta, gamma) actins. Skeletin and tubulin were prominent on one-and two-dimensional autoradiograms from 14 to 60 days. Radiolabeling of alpha actin polypeptide maximized at 14 days and was found to decrease at 30 and 60 days in comparison with nonsarcomeric actin isoforms. Correlative myocardial microscopic sections showed no fiber hypertrophy, but fiber atrophy was found. Results suggest a relative increase in polypeptide synthesis in the heterotopic transplanted heart samples.