Ultrastructural and cytochemical analysis of Na+, K+, ATPase and H+, K+, ATPase in parietal cells of gastric mucosa in the rabbit
| Autor: | G. Pradal, N. H. Vo, Gérard Lefranc, B. Pouyet, P. Piloquet |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Histology
Hydrogen potassium ATPase ATPase Ouabain chemistry.chemical_compound Parietal Cells Gastric Proton transport Sodium fluoride Gastric mucosa medicine Animals Vanadate Na+/K+-ATPase Molecular Biology biology Apyrase Cell Biology General Medicine Medical Laboratory Technology Microscopy Electron Proton-Translocating ATPases medicine.anatomical_structure chemistry Biochemistry biology.protein Ca(2+) Mg(2+)-ATPase Rabbits Anatomy Sodium-Potassium-Exchanging ATPase General Agricultural and Biological Sciences medicine.drug |
| Zdroj: | Histochemistry. 97(3) |
| ISSN: | 0301-5564 |
| Popis: | Rabbit gastric secretion has the physiological peculiarity of being continuous and uninfluenced by food intake. In this respect, ultrastructural analysis of rabbit parietal cells has revealed morphofunctional features situated between states of rest and very active acid secretion. Our cytochemical study shows that Mg2+ ATPase and ADPase activities vary from cell to cell and can even be totally absent. These activities concern either microcanaliculi or laterobasal folds or both, but never tubulovesicles. Application of the technique of Mayahara to K+ pNPP, associated or not with inhibitors (ouabain, vanadate, N-ethyl-maleimide, sodium fluoride), enabled us to confirm the coexistence of H+, K+, ATPase and Na+, K+, ATPase activities in the rabbit and to determine that these activities concern basolateral folds, microcanaliculi, hyaloplasm and tubulovesicles. The global activity of K+, pNPPase varied considerably in intensity. The results of using inhibitors suggest that proton transport ceases completely in certain cells. The signs of functional alternation found in this study are in agreement with physiological data relative to this animal. |
| Databáze: | OpenAIRE |
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