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General Physiology and Biophysics 2009 General Physiology and Biophysics Vol.28, No.3, p.302-306, 2009
General Physiology and Biophysics 2009 General Physiology and Biophysics Vol.28, No.3, p.302-306, 2009
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General Physiology and Biophysics Vol.28, No.3, p.302-306, 2009 |
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| Title: Influence of decavanadate on rat synaptic plasma membrane ATPases activity | ||
| Author: Danijela Krstić, Mirjana Čolović, Nada Bošnjaković-Pavlović, Anne Spasojević-De Bire and Vesna Vasić | ||
| Abstract: The in vitro influence of decameric vanadate species on Na+/K+-ATPase, plasma membrane Ca2+-ATPase (PMCA)-calcium pump and ecto-ATPase activity, using rat synaptic plasma membrane (SPM) as model system was investigated, whereas the commercial porcine cerebral cortex Na+/K+-ATPase served as a reference. The thermal behaviour of the synthesized decavanadate (V10) has been studied by differential scanning calorimetry and thermogravimetric analysis, while the type of polyvanadate anion was identified using the IR spectroscopy. The concentration-dependent responses to V10 of all enzymes were obtained. The half-maximum inhibitory concentration (IC50) of the enzyme activity was achieved at (4.74 ± 1.15) × 10–7 mol/l for SPM Na+/K+-ATPase, (1.30 ± 0.10) × 10–6 mol/l for commercial Na+/K+-ATPase and (3.13 ± 1.70) × 10–8 mol/l for Ca2+-ATPase, while ecto-ATPase is significantly less sensitive toward V10 (IC50 = (1.05 ± 0.10) × 10–4 mol/l) than investigated P-type ATPases. Kinetic analysis showed that V10 inhibited Na+/K+-ATPase by reducing the maximum enzymatic velocity and apparent affinity for ATP (increasing Km value), implying a mixed mode of interaction between V10 and P-type ATPases. |
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| Keywords: Decavanadate — Na+/K+-ATPase — Plasma membrane Ca2+-ATPase — ecto-ATPase | ||
| Year: 2009, Volume: 28, Issue: 3 | Page From: 302, Page To: 306 | |
| doi:10.4149/gpb_2009_03_302 |
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