Influence of decavanadate on rat synaptic plasma membrane ATPases activity
2009
Authors
Krstić, Danijela Z.Čolović, Mirjana B.
Bošnjaković-Pavlović, Nada
Spasojević-de Bire, Anne
Vasić, Vesna M.
Article
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The in vitro influence of decameric vanadate species on Na(+)/K(+)-ATPase, plasma membrane Ca(2+)-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 (V(10)) 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 V(10) of all enzymes were obtained. The half-maximum inhibitory concentration (IC(50)) of the enzyme activity was achieved at (4.74 +/- 1.15) x 10(-7) mol/l for SPM Na(+)/K(+)-ATPase, (1.30 +/- 0.10) x 10(-6) mol/l for commercial Na(+)/K(+)-ATPase and (3.13 +/- 1.70) x 10(-8) mol/l for Ca(2+)-ATPase, while ecto-ATPase is significantly less sensitive toward V(10) (IC(50) = (1.05 +/- 0.10) x 10(-4) mol/l) than invest...igated P-type ATPases. Kinetic analysis showed that V(10) inhibited Na(+)/K(+)-ATPase by reducing the maximum enzymatic velocity and apparent affinity for ATP (increasing K(m) value), implying a mixed mode of interaction between V(10) and P-type ATPases.
Keywords:
Decavanadate / Na(+)/K(+)-ATPase / Plasma membrane Ca(2+)-ATPase / ecto-ATPaseSource:
General Physiology and Biophysics, 2009, 28, 3, 302-308Funding / projects:
- Istraživanje mehanizma interakcija biološki aktivnih jedinjenja sa biomolekulima (RS-MESTD-MPN2006-2010-142051)
DOI: 10.4149/gpb_2009_03_302
ISSN: 0231-5882
PubMed: 20037196
WoS: 000272335700011
Scopus: 2-s2.0-72949103321
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VinčaTY - JOUR AU - Krstić, Danijela Z. AU - Čolović, Mirjana B. AU - Bošnjaković-Pavlović, Nada AU - Spasojević-de Bire, Anne AU - Vasić, Vesna M. PY - 2009 UR - https://vinar.vin.bg.ac.rs/handle/123456789/3840 AB - The in vitro influence of decameric vanadate species on Na(+)/K(+)-ATPase, plasma membrane Ca(2+)-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 (V(10)) 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 V(10) of all enzymes were obtained. The half-maximum inhibitory concentration (IC(50)) of the enzyme activity was achieved at (4.74 +/- 1.15) x 10(-7) mol/l for SPM Na(+)/K(+)-ATPase, (1.30 +/- 0.10) x 10(-6) mol/l for commercial Na(+)/K(+)-ATPase and (3.13 +/- 1.70) x 10(-8) mol/l for Ca(2+)-ATPase, while ecto-ATPase is significantly less sensitive toward V(10) (IC(50) = (1.05 +/- 0.10) x 10(-4) mol/l) than investigated P-type ATPases. Kinetic analysis showed that V(10) inhibited Na(+)/K(+)-ATPase by reducing the maximum enzymatic velocity and apparent affinity for ATP (increasing K(m) value), implying a mixed mode of interaction between V(10) and P-type ATPases. T2 - General Physiology and Biophysics T1 - Influence of decavanadate on rat synaptic plasma membrane ATPases activity VL - 28 IS - 3 SP - 302 EP - 308 DO - 10.4149/gpb_2009_03_302 ER -
@article{ author = "Krstić, Danijela Z. and Čolović, Mirjana B. and Bošnjaković-Pavlović, Nada and Spasojević-de Bire, Anne and Vasić, Vesna M.", year = "2009", abstract = "The in vitro influence of decameric vanadate species on Na(+)/K(+)-ATPase, plasma membrane Ca(2+)-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 (V(10)) 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 V(10) of all enzymes were obtained. The half-maximum inhibitory concentration (IC(50)) of the enzyme activity was achieved at (4.74 +/- 1.15) x 10(-7) mol/l for SPM Na(+)/K(+)-ATPase, (1.30 +/- 0.10) x 10(-6) mol/l for commercial Na(+)/K(+)-ATPase and (3.13 +/- 1.70) x 10(-8) mol/l for Ca(2+)-ATPase, while ecto-ATPase is significantly less sensitive toward V(10) (IC(50) = (1.05 +/- 0.10) x 10(-4) mol/l) than investigated P-type ATPases. Kinetic analysis showed that V(10) inhibited Na(+)/K(+)-ATPase by reducing the maximum enzymatic velocity and apparent affinity for ATP (increasing K(m) value), implying a mixed mode of interaction between V(10) and P-type ATPases.", journal = "General Physiology and Biophysics", title = "Influence of decavanadate on rat synaptic plasma membrane ATPases activity", volume = "28", number = "3", pages = "302-308", doi = "10.4149/gpb_2009_03_302" }
Krstić, D. Z., Čolović, M. B., Bošnjaković-Pavlović, N., Spasojević-de Bire, A.,& Vasić, V. M.. (2009). Influence of decavanadate on rat synaptic plasma membrane ATPases activity. in General Physiology and Biophysics, 28(3), 302-308. https://doi.org/10.4149/gpb_2009_03_302
Krstić DZ, Čolović MB, Bošnjaković-Pavlović N, Spasojević-de Bire A, Vasić VM. Influence of decavanadate on rat synaptic plasma membrane ATPases activity. in General Physiology and Biophysics. 2009;28(3):302-308. doi:10.4149/gpb_2009_03_302 .
Krstić, Danijela Z., Čolović, Mirjana B., Bošnjaković-Pavlović, Nada, Spasojević-de Bire, Anne, Vasić, Vesna M., "Influence of decavanadate on rat synaptic plasma membrane ATPases activity" in General Physiology and Biophysics, 28, no. 3 (2009):302-308, https://doi.org/10.4149/gpb_2009_03_302 . .