Regulation of ribonuclease expression by estradiol in Rana catesbeiana (Bullfrog)

Multiple ribonucleases are widely found in living organisms, but the function and regulation of individual ribonucleases are still not clear. In the present study, we found that one oocytic ribonuclease, RC‐RNase, is developmentally expressed in the liver and stored in the oocyte of the bullfrog, wh...

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Bibliographic Details
Published in:Nucleic acids research 2002-07, Vol.30 (14), p.3286-3293
Main Authors: Tang, Pin‐Chi, Huang, Huey‐Chung, Wang, Sui‐Chi, Jeng, Jen‐Chong, Liao, You‐Di
Format: Article
Language:English
Subjects:
Animals
Base Sequence
Cloning, Molecular
Electrophoresis, Polyacrylamide Gel
Enzyme Activation - drug effects
Estradiol - pharmacology
Gene Expression Regulation, Enzymologic - drug effects
Humans
Liver - enzymology
Luciferases - genetics
Luciferases - metabolism
Molecular Sequence Data
Mutation
Promoter Regions, Genetic - genetics
Ranidae - genetics
Ranidae - growth & development
Ranidae - metabolism
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
Ribonucleases - blood
Ribonucleases - genetics
Ribonucleases - metabolism
RNA - metabolism
Time Factors
Transcriptional Activation
Tumor Cells, Cultured
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Summary:Multiple ribonucleases are widely found in living organisms, but the function and regulation of individual ribonucleases are still not clear. In the present study, we found that one oocytic ribonuclease, RC‐RNase, is developmentally expressed in the liver and stored in the oocyte of the bullfrog, while another ribonuclease, RC‐RNase L1, is constitutively expressed and retained in the liver at all stages. In females, the expression of RC‐RNase increased with the degree of maturity and the concentration of plasma estradiol during oogenesis. In males, the RC‐RNase gene was activated in the liver and the newly synthesized protein was secreted into plasma if estradiol was administered. To investigate the mechanism of estrogen‐mediated activation of ribonuclease expression, we cloned the RC‐RNase promoter and analyzed the putative transcription factor binding sites, e.g. TATA box, ERE, AP1 and CAAT box. Using luciferase as a reporter gene, we found that an estrogen response element in the promoter of RC‐RNase was essential for both basic transcription and estradiol‐mediated gene activation in estrogen receptor‐positive MCF7 cells. These results support the hypothesis that RC‐RNase is synthesized in the liver upon stimulation by estradiol during oogenesis, then secreted into the bloodstream and stored in oocytes for embryonic development.
ISSN:0305-1048
1362-4962
1362-4962
DOI:10.1093/nar/gkf442