Regulation of Protein Kinase a Subunits by Cyclic Adenosine 3’,5’-Monophosphate in a Mouse Sertoli Cell Line (MSC-1): Induction of RIIβ Messenger Ribonucleic Acid is Independent of Continuous Protein Synthesis1
| Autor: | Winnie Eskild, Vidar Hansson, Nils Reinton, Helle K. Knutsen, Kristin Austlid Taskén |
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| Rok vydání: | 1996 |
| Předmět: |
endocrine system
Messenger RNA Protein subunit hemic and immune systems chemical and pharmacologic phenomena Cell Biology General Medicine respiratory system Biology Sertoli cell Molecular biology medicine.anatomical_structure Reproductive Medicine Cell culture Gene expression Protein biosynthesis medicine Beta protein Protein kinase A |
| Zdroj: | Biology of Reproduction. 55:5-10 |
| ISSN: | 1529-7268 0006-3363 |
| DOI: | 10.1095/biolreprod55.1.5 |
| Popis: | We report the basal and cAMP-regulated expression of protein kinase A (PKA) subunits in a mouse Sertoli cell line (MSC-1). Of the PKA subunits expressed by these cells (RI alpha, RII alpha, RII beta, C alpha, C beta), only RII beta was regulated by cAMP. An approximately 8-fold induction of RII beta mRNA and a 3-fold induction of RII beta protein was observed during 48 h of cAMP-stimulation. This cAMP-mediated RII beta mRNA induction, reaching maximal levels after approximately 12 h, did not require ongoing protein synthesis. Fairly rapid decay of maximally induced RII beta mRNA was observed after removal of cAMP (t1/2 approximately 5 h). Further, ongoing transcription and translation were necessary for rapid degradation of RII beta mRNA. Thus, the MSC-1 cells expressed all the PKA subunits present in primary cultures of Sertoli cells and responded to cAMP with increased levels of RII beta at both mRNA and protein levels. Although the nature of some of these responses distinguished the observations in MSC-1 cells from previously described responses in primary cultures, these cells may prove to be useful in future studies addressing cAMP-mediated gene regulation. |
| Databáze: | OpenAIRE |
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