Submit Data |  Help |  Video Tutorials |  News |  Publications |  FTP Download |  REST API |  Citing RGD |  Contact   

Increased expression of acidic ribosomal protein (P0) mRNA after phorbol ester treatment of cultured rat thyroid (FRTL-5) cells.

Authors: Saito, T  Ikeda, M  Endo, T  Tsurugi, K  Onaya, T 
Citation: Saito T, etal., Biochem Biophys Res Commun. 1994 Sep 15;203(2):780-8.
Pubmed: (View Article at PubMed) PMID:8093057
DOI: Full-text: DOI:10.1006/bbrc.1994.2251

P0, an acidic protein component of the ribosomal protein in eukaryotic 60 S ribosomal subunit, plays an important role in polypeptide chain elongation during translation. To investigate the role of protein kinase C in thyroid cell protein synthesis, we examined the effect of 12-O-tetradecanoyl-phorbol-13-acetate (TPA) on the expression of P0 mRNA and protein. RNA slot blot hybridization revealed that TPA induced the accumulation of P0 mRNA in FRTL-5 cells in a time- and dose-dependent manner. A maximal increase of 2-fold was observed 18 h after addition of TPA. Cycloheximide markedly inhibited the TPA-induced accumulation of P0 mRNA. Nuclear runoff transcription assays using nuclei prepared from TPA-treated FRTL-5 cells revealed that TPA increased the transcription of P0 mRNA but not of beta-actin. Immunoblotting experiments using anti-P protein antibody showed that TPA also increased the protein amount of P0. These results suggest that TPA activates protein synthesis in thyroid cells by inducing the expression of ribosomal proteins.


Gene Ontology Annotations
Objects Annotated

Additional Information

CRRD Object Information
CRRD ID: 11039468
Created: 2016-03-04
Species: All species
Last Modified: 2016-03-04
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.