期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1981
卷号：78
期号：2
页码：1269-1273
DOI：10.1073/pnas.78.2.1269
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Polysomal poly(A)-mRNA was purified from a clonal cell line of rat pheochromocytoma (PC 12) and translated in a reticulocyte cell-free protein-synthesizing system. Tyrosine hydroxylase [tyrosine 3-monooxygenase; L-tyrosine, tetrahyropteridine:oxygen oxidoreductase (3-hydroxylating), EC 1.14.16.2 ] was isolated from other protein by immunoprecipitation and NaDodSO4/polyacrylamide gel electrophoresis. The molecular weight and relative proportion of tyrosine hydroxylase to other proteins synthesized in vitro were identical to those of the enzyme synthesized in vivo in cultured cells. Incubation of PC 12 cells with 10 microM dexamethasone increased the activity and amount of tyrosine hydroxylase 2.5-fold. The ratio of tyrosine hydroxylase to total protein translated from poly(A)-mRNA isolated from cells treated with dexamethasone was 2.5 times higher than the ratio of enzyme to total protein translated from an equal amount of poly(A)-mRNA from untreated cells. The dexamethasone-elicited induction of tyrosine hydroxylase in PC 12 cells therefore is a result of an increased "relative" amount or activity of tyrosine hydroxylase mRNA.
