Prolonged starvation in rats is accompanied by consistent increases in the total cardiac activity and the nonsedimentable activity of cathepsin D, the major detectable lysosomal acid proteinase in the heart. Fluorescent staining of rabbit hearts with specific anticathepsin D antiserum reveals that the increase occured predominantly in myocytes, but increased formation of autophagic vacuoles cannot be demonstrated in the myocardial cells by electron microscopy. No changes in cathepsin D occur in animals fed pure carbohydrate or pure fat diets for similar periods, indicating that it is caloric deficiency and not dietary protein deficiency that alters catheptic activity. At the same time that cardiac cathepsin D activity increases markedly, acid phosphatase increases slightly, and the activity of beta-acetyl-glucosaminidase is significantly lower than in hearts of fed rats. The data are compatible with the hypothesis that increased activity of lysosomal acid proteinase may contribute to the net protein catabolism and cardiac atrophy that accompany starvation, especially late in the period of food deprivation. A generalized activation of all lysosomal enzymes does not occur with starvation, however, and the activities of some lysosomal enzymes in the heart decrease.
|Original language||English (US)|
|Number of pages||11|
|Journal||Recent advances in studies on cardiac structure and metabolism|
|State||Published - Dec 1 1975|
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