Mercury weakens membrane anchoring of Na-K-ATPase
| Autor: | M. Moosmayer, Beatrice M. Anner, E. Imesch |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Proteases
Physiology ATPase Molecular Conformation Permeability Extracellular medicine Animals Trypsin Na+/K+-ATPase chemistry.chemical_classification Kidney Membranes biology Unithiol Mercury Enzyme medicine.anatomical_structure chemistry Biochemistry Enzyme inhibitor biology.protein Electrophoresis Polyacrylamide Gel Rabbits Sodium-Potassium-Exchanging ATPase Intracellular |
| Zdroj: | American Journal of Physiology-Renal Physiology. 263:F984-F984 |
| ISSN: | 1522-1466 1931-857X |
| DOI: | 10.1152/ajprenal.1992.263.5.f984-r |
| Popis: | The presence of circulating inhibitors able to decrease the renal Na-K-adenosinetriphosphatase (ATPase) activity (natriuretic hormones) was postulated some 30 years ago. In the present work, the natriuretic inhibitor HgCl2 was selected as a model compound for the structural characterization of a possible natriuretic pathway for Na-K-ATPase modification. The structural effects of Na-K-ATPase inhibition by HgCl2 were assessed by trypsinolysis of the blocked enzyme in comparison with untreated preparations. The results show that inactivation of Na-K-ATPase by HgCl2 leads to the release of the alpha-subunit from the membrane preferentially in the E2 conformation but also in the E1 conformation. Apparently, HgCl2 weakens the membrane anchoring of the alpha-subunit, presumably by loosening the alpha-beta-subunit interaction. By this mechanism, the sensitivity of the Na-K-ATPase to extracellular drugs, hormones, and antibodies, as well as to intracellular proteases and other regulatory factors, could be altered. |
| Databáze: | OpenAIRE |
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