Translation-level control of amylase and protein synthesis by epinephrine.
The synthesis of RNA, protein, and amylase has been studied in normal and epinephrine-treated slices of rat parotid gland. Epinephrine stimulates synthesis of total cell protein and specifically of amylase, but amylase synthesis is preferentially increased. There is no change in either the specific radioactivity or pattern of labeling of total RNA. In the presence of actinomycin D, epinephrine stimulates secretion of amylase, as well as protein and amylase synthesis. RNA synthesis under these conditions is reduced to 10 per cent of control values. Slices obtained from animals treated with actinomycin D nine and a half hours prior to study show responses to epinephrine comparable to those from control animals, with RNA synthesis inhibited by 70 per cent. Since amylase synthesis is stimulated by epinephrine in the absence of RNA synthesis, control of the production of this enzyme is probably exerted at the level of translation.
D000681:Amylases / Q000096:biosynthesis*; D000818:Animals; D002247:Carbon Isotopes; D000242:Cyclic AMP / Q000378:metabolism; D003609:Dactinomycin / Q000494:pharmacology; D003864:Depression, Chemical; D004837:Epinephrine / Q000494:pharmacology*; D005815:Genetic Code; D066298:In Vitro Techniques; D008297:Male; D010306:Parotid Gland / Q000187:drug effects / Q000378:metabolism*; D014176:Protein Biosynthesis; D012313:RNA / Q000096:biosynthesis*; D051381:Rats; D013268:Stimulation, Chemical; D014316:Tritium; D014529:Uridine / Q000378:metabolism
D002247:Carbon Isotopes; D014316:Tritium; D003609:Dactinomycin; D012313:RNA; D000242:Cyclic AMP; D000681:Amylases; D014529:Uridine; D004837:Epinephrine