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Title: Steroid-regulated intracellular signals involved in proliferation of rat epithelial cells. II. Glucocorticoid regulation of phosphoprotein maturation in rat hepatoma cells

Miscellaneous ·
OSTI ID:6650529

Cultured BDS1 rat hepatoma cells, growth-arrested in the presence of serum and glucocorticoid, were induced to synchronously enter the cell cycle upon removal of steroid from the medium. Analysis of total RNA isolated from the proliferating cells revealed a peak of transcript levels at 0.5 hours for c-fos, at 2 hours for c-myc and at 8 hours for both c-ras{sup Ha} and c-ras{sup Ki}. The onset of DNA synthesis, as measured by ({sup 3}H)thymidine incorporation, occurred after an 8 hour time lag and peaked at 16 hours after the removal of dexamethasone. The induction of DNA polymerase alpha activity occurred during the onset of DNA synthesis and peaked at 24 hours. Cytoplasmic extracts from non-growing BDS1 cells did not contain an inhibitory activity that could suppress the activity of DNA polymerase alpha. A high molecular weight (M{sub r}210,000) DNA polymerase alpha protein was present in proliferating but not in quiescent cell extracts. In M1.54 rat liver hepatoma cells that contain mouse mammary tumor provirus (MMTV), the phosphorylated viral precursor polypeptide (Pr74), is cleaved posttranslationally into p24, after a 4 hour exposure to glucocortocoid. Twenty hours after hormone withdrawal, p24 is degraded whereas Pr74 remained ten-fold over its basal level.

Research Organization:
California Univ., Berkeley, CA (USA)
OSTI ID:
6650529
Resource Relation:
Other Information: Thesis (Ph. D.)
Country of Publication:
United States
Language:
English