Parathyroid hormone alteration of free and tRNA-bound proline specific activities in cultured mouse osteoblast-like cells.

The effects of the synthetic amino-terminal fragment of parathyroid hormone [bPTH-(1-34)] on proline uptake and on the specific activities of intracellular free proline and tRNA-bound proline were studied in confluent primary cultures of osteoblast-like cells isolated from neonatal mouse calvaria. Pretreatment of cells for 4 hours with 24 nM bPTH-(1-34) increased subsequent proline uptake by approximately 50-60%; also increased were the specific activities of both intracellular free proline and tRNA-bound proline when [3H]proline was included in the extracellular uptake solution. Specific activities of the free and tRNA-bound proline pools remained elevated after proline uptake times of as long as 30 minutes and 120 minutes, respectively. These results indicate that experiments in which radiolabeled proline is used to evaluate PTH-induced protein synthesis in bone cells must be interpreted cautiously, since apparent changes in protein synthesis might actually reflect, at least in part, PTH-induced changes in the specific activities of precursor pools.