| Literature DB >> 6112744 |
E E Baetge, B B Kaplan, D J Reis, T H Joh.
Abstract
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.Entities:
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Year: 1981 PMID： 6112744 PMCID： PMC319990 DOI： 10.1073/pnas.78.2.1269
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205