No abstract

To determine whether the synthesis of secretory proteins changes with age, the incorporation of [14C]-leucine into exportable proteins of the parotid gland was compared in 2- and 24-month-old rats. The proteins were separated by SDS-gel electrophoresis of the post-microsomal supernatant and identified by comparing the banding patterns in gels prepared from unstimulated glands with those from the glands stimulated to secrete. The amount of radioactivity incorporated into the bands corresponding to exportable proteins was significantly less in the older group, indicating that the synthesis of secretory proteins declines with age.

The age-related differences in the synthesis of exportable and nonexportable proteins of the parotid salivary gland were compared in 2- and 24-months-old rats. Parotid slices from these rats were incubated in the presence of [14C]leucine and the amount of radioactivity incorporated into the water-soluble proteins of the postmicrosomal supernatant was compared. The exportable and nonexportable proteins were identified by electrophoretic separation of these proteins by comparing the banding patterns of the gel preparations from unstimulated glands to those from the glands stimulated to secrete. The radioactivity determination in various protein bands from these rats indicated that the synthesis of exportable secretory proteins declined with age, while that of nonexportable proteins did not appear to change.

The rate of release of a secretory enzyme, alpha-amylase, from the parotid lobules of 2 and 24 month old rats has been compared to determine whether the secretory activity of the cells change during aging. Upon incubation in the presence of a secretogogue, isoproterenol (10(-5) M), about the same proportions of the glandular alpha-amylase are released at about the same rate from these lobules. The isoproterenol-stimulated release of the enzyme is inhibited nearly completely by preincubating the lobules with propranolol (10(-5) M) in both age groups, indicating that the enzyme secretion occurs through the stimulation of beta-receptors. When viewed in the electron microscope, the cell membranes bordering the secretory lumen in isoproterenol-incubated lobules reveal festooned appearances which suggest that the enzyme release occurs by means of exocytosis. These observations indicate that the ability of the parotid cells to release secretory products through the beta-receptor mediation does not significantly change with increasing age.