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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.

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



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