Regulation of a Sodium Channel-associated G-protein by Aldosterone
| Autor: | Michael D. Rokaw, Paul M. Palevsky, Sonia A. Cunningham, Dale J. Benos, Michael E. West, John P. Johnson |
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| Rok vydání: | 1996 |
| Předmět: |
Epithelial sodium channel
medicine.medical_specialty Cell Membrane Permeability Macromolecular Substances Sodium Blotting Western Molecular Sequence Data Palmitic Acid chemistry.chemical_element Palmitic Acids Biochemistry Antibodies Epithelium Sodium Channels Cell Line Xenopus laevis chemistry.chemical_compound GTP-Binding Proteins Internal medicine Heterotrimeric G protein medicine Animals Homeostasis Amino Acid Sequence Aldosterone Molecular Biology Sodium channel activity Renal sodium reabsorption Sodium channel Biological Transport Cell Biology Apical membrane Kinetics Endocrinology chemistry Peptides Protein Processing Post-Translational |
| Zdroj: | Journal of Biological Chemistry. 271:4491-4496 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.271.8.4491 |
| Popis: | The action of aldosterone to increase apical membrane permeability in responsive epithelia is thought to be due to activation of sodium channels. This channel is regulated, in part, by G-proteins, but it is not known if this mechanism is regulated by aldosterone. We report that aldosterone stimulates the expression of the 41-kDa α subunit of the heterotrimeric GTP-binding proteins in A-6 cells. Both mRNA and the total amount of this protein are increased by aldosterone. The G-protein is palmitoylated in response to the steroid, and the newly synthesized subunit is found to co-localize with the sodium channel. Aldosterone stimulation of sodium transport is significantly inhibited by inhibition of palmitoylation. These results suggest that aldosterone regulates sodium channel activity in epithelia through stimulation of the expression and post-translational targeting of a channel regulatory G-protein subunit. |
| Databáze: | OpenAIRE |
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