Role of protein phosphatase in the regulation of Na+-K+-ATPase by vasopressin in the cortical collecting duct
| Autor: | N. Coutry, Nicolette Farman, Jean-Pierre Bonvalet, Monique Laplace, Marcel Blot-Chabaud |
|---|---|
| Přispěvatelé: | Faculté de Médecine Xavier Bichat |
| Rok vydání: | 1996 |
| Předmět: |
endocrine system
medicine.medical_specialty Vasopressin Kidney Cortex Physiology Vasopressins Sodium-Potassium-Exchanging ATPase [SDV]Life Sciences [q-bio] Phosphatase Biophysics Renal Agents Dephosphorylation 03 medical and health sciences Mice 0302 clinical medicine Internal medicine medicine Animals Na+/K+-ATPase Phosphorylation ComputingMilieux_MISCELLANEOUS 030304 developmental biology Epithelial polarity 0303 health sciences urogenital system Chemistry Cell Biology Protein phosphatase 2 Phosphoric Monoester Hydrolases Cell biology Endocrinology hormones hormone substitutes and hormone antagonists 030217 neurology & neurosurgery |
| Zdroj: | Journal of Membrane Biology Journal of Membrane Biology, Springer Verlag (Germany), 1996, 153 (3), pp.233-239. ⟨10.1007/s002329900126⟩ |
| ISSN: | 0022-2631 1432-1424 |
| Popis: | In the cortical collecting duct (CCD), arginin vasopressin (AVP) has been shown to increase the number and activity of basolateral Na+-K+-ATPase by recruiting or activating a latent pool of pumps. However, the precise mechanism of this phenomenon is still unknown. The aim of this study was to investigate whether this AVP-induced increase in basolateral Na+-K+-ATPase could depend on a dephosphorylation process. To this purpose, the effect of protein serine/threonine phosphatase (PP) inhibitors was examined on both the specific 3H-ouabain binding (to evaluate the number of pumps in the basolateral membrane) and the ouabain-dependent 86Rb uptake (to evaluate pump functionality) in the presence or absence of AVP. In addition, the activity of two PP, PP1 and PP2A, was measured and the influence of AVP was examined on both enzymes. Experiments have been performed on mouse CCD isolated by microdissection. Results show that inhibition of PP2A prevents the AVP-induced increase in the number and activity of Na+-K+-ATPases, independent of an effect on the apical cell sodium entry. In addition, AVP rapidly increased the activity of PP2A without effect on PP1. These data suggest that PP2A is implied in the regulation of Na+-K+-ATPase activity by AVP in the CCD and that the AVP-dependent increase in the number of Na+-K+-ATPases is mediated by a PP2A-dependent dephosphorylation process. |
| Databáze: | OpenAIRE |
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