Expression and regulation of Gαq and Gαll mRNAs and proteins in bovine adrenal cells
| Autor: | Dominique Langlois, A. Derrien, J. M. Saez |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
chemistry.chemical_classification
medicine.medical_specialty Messenger RNA Alpha (ethology) Adrenocorticotropic hormone Biology Biochemistry Angiotensin II Molecular biology Endocrinology GTP-binding protein regulators chemistry Gq alpha subunit Internal medicine biology.protein medicine Receptor Inositol phosphate Molecular Biology hormones hormone substitutes and hormone antagonists |
| Zdroj: | Molecular and Cellular Endocrinology. 121:65-74 |
| ISSN: | 0303-7207 |
| Popis: | Bovine adrenal cortical cells (BAC) express corticotropin (ACTH) and angiotensin II (AngII) receptors (AT1 subtype), which are coupled to adenylate cyclase and phosphoinositide pathways, respectively. The coupling of AT1 to phosphoinositide breakdown is mainly pertussis toxin-insensitive suggesting that this receptor is coupled to Gaeq/Gae11. In the present work we have demonstrated that BAC express G alpha q and G alpha 11 mRNA and proteins, and their variation during culture as well as their regulation by ACTH and AngII is different. ACTH enhanced G alpha q mRNA levels mainly by increasing the transcription rate. In addition, ACTH increased both G alpha q and G alpha 11 proteins without changing their half-lives. In contrast, AngII reduced both G alpha q mRNA and protein and increased G alpha 11 mRNA but not G alpha 11 protein. The decrease of G alpha q mRNA levels was mainly due to a marked reduction of its half-life. These changes in G alpha q/G alpha 11 proteins induced by both hormones were associated with an enhanced AngII-induced inositol phosphate accumulation, more marked after stimulation with ACTH than after AngII pretreatment. In summary, the present results demonstrated that BAC express both G alpha q and G alpha 11 and their regulations are different and in contrast to other cell types these regulations do not involve changes in the half-life of G alpha q/G alpha 11 proteins. |
| Databáze: | OpenAIRE |
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