Amylase and chymotrypsinogen synthesis and secretion by the anesthetized rat pancreas.

To investigate the origin of nonparallel secretion, pancreatic juice was collected in the anesthetized rat, during infusion of [3H]phenylalanine. In the basal state, the amylase to chymotrypsinogen ratios of activities and of [3H] incorporations were 3.5 and 2.5 times higher than in the homogenate, respectively. Both ratios decreased to the value in the homogenate upon caerulein stimulation (600 ng/kg). Inhibition of protein synthesis by cycloheximide (15 ng/kg) did not alter enzyme secretion ratios, and depressed basal protein output only partly, suggesting similar secretory pathways for basal and stimulated secretion. Finally, when [3H]phenylalanine was given before anesthesia, the amylase to chymotrypsinogen ratio of incorporations was again higher in basal secretion than in homogenate, even when further protein synthesis was blocked by cycloheximide before urethane injection. Hence, basal secretion comes from a pancreatic compartment which is functional, although minor, in the conscious animal, and shows a higher rate of amylase synthesis, compared to chymotrypsinogen, than the rest of the gland. It could consist of a subpopulation of acinar cells.