Abstract
Treatment of isolated bone cells with purified bovine parathyroid hormone (5 ng/ml-2 ¼g/ml) augmented the incorporation of 214C-uridine into acid-soluble RNA precursor pools and into RNA. Stimulation developed within 15 min and gradually declined after 30 min. A synthetic N-terminal 1–34 amino acid fragment of PTH was one-half as potent as native hormone. A 2–34 amino acid fragment, oxidized native hormone, and several basic polypeptides were inactive. PTH enhanced the labeling of cellular UDP and UTP pools appreciably and increased that of UMP slightly but failed to modify the total radioactivity of cellular free uridine, pointing to uridine or UMP phosphorylation (or both) as the site(s) of PTH action. Stimulation of 2–14C-uridine incorporation was not associated withalterations in total cell ATP levels. The effect of PTH on uridine metabolism appeared during simultaneous treatment of bone cells with actinomycin D, indicating that it was independent of RNAsynthesis. Exogenous (Bt)2 cAMP (0.1–1.0 min) an...
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