valinomycin has been researched along with piretanide* in 2 studies
2 other study(ies) available for valinomycin and piretanide
Article | Year |
---|---|
Ionic control of locomotion and shape of epithelial cells: II. Role of monovalent cations.
The migration of keratocytes isolated from Xenopus tadpole epidermis has been investigated in vitro. In saline the cells move with a mean speed of 5-6 microns/min. Migration is slowed down in saline with diminished sodium content and ceases in media containing not more than 4 mM sodium. Inhibition of the Na+/K+-2Cl- cotransporter by piretanide reduces the speed of migrating cells to about one-third of the control level, the same accounts to inhibition of the Na+/H+ antiport with amiloride at pH 7.2. At pH 6.6, however, amiloride only slightly influences locomotion. Depolarization of the plasma membrane by increased extracellular K+ concentration or by inhibition of the Na+/K+ pump by ouabain is only of minor influence during more than 1 h. Hyperpolarization of the cells using the sodium ionophore monensin impedes locomotion; this inhibition depends on an active Na+/K+ pump. Ionophore-mediated breakdown of the K+ gradient strictly inhibits locomotion. The experiments have shown that a continuous flux of sodium ions is indispensable for the maintenance of cell locomotion. These ions may exert their action primarily by affecting cytosolic free calcium concentration and pH. Topics: Amiloride; Animals; Cations, Monovalent; Cell Movement; Cytoplasm; Epidermal Cells; Epidermis; Epithelial Cells; Epithelium; Hydrogen; Keratins; Membrane Potentials; Monensin; Potassium; Sodium; Sodium-Potassium-Exchanging ATPase; Sulfonamides; Valinomycin; Xenopus laevis | 1988 |
Isolation of protein(s) containing chloride ion transport activity from thylakoid membranes.
Extracts of detergent-treated thylakoids, when reconstituted into azolectin/cholesterol/dicetyl phosphate vesicles, stimulate chloride ion efflux as measured with a Cl--sensitive electrode. This stimulation is inhibited by piretanide, an active chloride ion transport inhibitor in fish intestinal epithelia. This stimulation is also abolished by pretreatment of extracted proteins with trypsin. Antiserum raised to efflux-active proteins inhibits a cation-driven Cl- influx in nonenergized thylakoids, as measured by a flow dialysis technique. Topics: Biological Transport, Active; Chlorides; Chloroplasts; Dialysis; Filtration; Hydrogen-Ion Concentration; Immune Sera; Intracellular Membranes; Membrane Proteins; Membranes, Artificial; Plant Proteins; Sulfonamides; Valinomycin | 1984 |