BIOMAT Database Logo BIOMAT Database Logo

Inhibition of Na+/K+- and Ca2+-ATPase activities by phosphotetradecavanadate. 2019

Gil Fraqueza, and Juan Fuentes, and Lukáš Krivosudský, and Saikat Dutta, and Sib Sankar Mal, and Alexander Roller, and Gerald Giester, and Annette Rompel, and Manuel Aureliano
ISE, University of Algarve, 8005-139 Faro, Portugal; CCMar, University of Algarve, 8005-139 Faro, Portugal.

Polyoxometalates (POMs) are promising inorganic inhibitors for P-type ATPases. The experimental models used to study the effects of POMs on these ATPases are usually in vitro models using vesicles from several membrane sources. Very recently, some polyoxotungstates, such as the Dawson anion [P2W18O62]6-, were shown to be potent P-type ATPase inhibitors; being active in vitro as well as in ex-vivo. In the present study we broaden the spectrum of highly active inhibitors of Na+/K+-ATPase from basal membrane of epithelial skin to the bi-capped Keggin-type anion phosphotetradecavanadate Cs5.6H3.4PV14O42 (PV14) and we confront the data with activity of other commonly encountered polyoxovanadates, decavanadate (V10) and monovanadate (V1). The X-ray crystal structure of PV14 was solved and contains two trans-bicapped α-Keggin anions HxPV14O42(9-x)-. The anion is built up from the classical Keggin structure [(PO4)@(V12O36)] capped by two [VO] units. PV14 (10 μM) exhibited higher ex-vivo inhibitory effect on Na+/K+-ATPase (78%) than was observed at the same concentrations of V10 (66%) or V1 (33%). Moreover, PV14 is also a potent in vitro inhibitor of the Ca2+-ATPase activity (IC50 5 μM) exhibiting stronger inhibition than the previously reported activities for V10 (15 μM) and V1 (80 μM). Putting it all together, when compared both P-typye ATPases it is suggested that PV14 exibited a high potential to act as an in vivo inhibitor of the Na+/K+-ATPase associated with chloride secretion.

UI MeSH Term Description Entries
D004791 Enzyme Inhibitors Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction. Enzyme Inhibitor,Inhibitor, Enzyme,Inhibitors, Enzyme
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000252 Calcium-Transporting ATPases Cation-transporting proteins that utilize the energy of ATP hydrolysis for the transport of CALCIUM. They differ from CALCIUM CHANNELS which allow calcium to pass through a membrane without the use of energy. ATPase, Calcium,Adenosinetriphosphatase, Calcium,Ca(2+)-Transporting ATPase,Calcium ATPase,Calcium Adenosinetriphosphatase,Adenosine Triphosphatase, Calcium,Ca2+ ATPase,Calcium-ATPase,ATPase, Ca2+,ATPases, Calcium-Transporting,Calcium Adenosine Triphosphatase,Calcium Transporting ATPases,Triphosphatase, Calcium Adenosine
D000254 Sodium-Potassium-Exchanging ATPase An enzyme that catalyzes the active transport system of sodium and potassium ions across the cell wall. Sodium and potassium ions are closely coupled with membrane ATPase which undergoes phosphorylation and dephosphorylation, thereby providing energy for transport of these ions against concentration gradients. ATPase, Sodium, Potassium,Adenosinetriphosphatase, Sodium, Potassium,Na(+)-K(+)-Exchanging ATPase,Na(+)-K(+)-Transporting ATPase,Potassium Pump,Sodium Pump,Sodium, Potassium ATPase,Sodium, Potassium Adenosinetriphosphatase,Sodium-Potassium Pump,Adenosine Triphosphatase, Sodium, Potassium,Na(+) K(+)-Transporting ATPase,Sodium, Potassium Adenosine Triphosphatase,ATPase Sodium, Potassium,ATPase, Sodium-Potassium-Exchanging,Adenosinetriphosphatase Sodium, Potassium,Pump, Potassium,Pump, Sodium,Pump, Sodium-Potassium,Sodium Potassium Exchanging ATPase,Sodium Potassium Pump
D014638 Vanadates Oxyvanadium ions in various states of oxidation. They act primarily as ion transport inhibitors due to their inhibition of Na(+)-, K(+)-, and Ca(+)-ATPase transport systems. They also have insulin-like action, positive inotropic action on cardiac ventricular muscle, and other metabolic effects. Decavanadate,Metavanadate,Orthovanadate,Oxyvanadium,Vanadyl,Monovanadate,Sodium Vanadate,Vanadate,Vanadate, Sodium
D018360 Crystallography, X-Ray The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) X-Ray Crystallography,Crystallography, X Ray,Crystallography, Xray,X Ray Crystallography,Xray Crystallography,Crystallographies, X Ray,X Ray Crystallographies

Related Publications

Gil Fraqueza, and Juan Fuentes, and Lukáš Krivosudský, and Saikat Dutta, and Sib Sankar Mal, and Alexander Roller, and Gerald Giester, and Annette Rompel, and Manuel Aureliano
Ca2+-Dependent activities of (Na+ + K+)-ATPase.
July 1982, Archives of biochemistry and biophysics,
Gil Fraqueza, and Juan Fuentes, and Lukáš Krivosudský, and Saikat Dutta, and Sib Sankar Mal, and Alexander Roller, and Gerald Giester, and Annette Rompel, and Manuel Aureliano
Activities of Ca2+-ATPase and Na+ + K+-ATPase in human placenta.
October 1980, Nihon Sanka Fujinka Gakkai zasshi,
Gil Fraqueza, and Juan Fuentes, and Lukáš Krivosudský, and Saikat Dutta, and Sib Sankar Mal, and Alexander Roller, and Gerald Giester, and Annette Rompel, and Manuel Aureliano
Ca2+-dependent inhibition of (Na+ + K+)-dependent ATPase by hydroxylamine.
July 1967, Biochimica et biophysica acta,
Gil Fraqueza, and Juan Fuentes, and Lukáš Krivosudský, and Saikat Dutta, and Sib Sankar Mal, and Alexander Roller, and Gerald Giester, and Annette Rompel, and Manuel Aureliano
Calcium inhibition of the ATPase and phosphatase activities of (Na+ + K+)-ATPase.
March 1983, Biochimica et biophysica acta,
Gil Fraqueza, and Juan Fuentes, and Lukáš Krivosudský, and Saikat Dutta, and Sib Sankar Mal, and Alexander Roller, and Gerald Giester, and Annette Rompel, and Manuel Aureliano
Kinetic studies on Na+/K+-ATPase and inhibition of Na+/K+-ATPase by ATP.
August 2004, Journal of enzyme inhibition and medicinal chemistry,
Gil Fraqueza, and Juan Fuentes, and Lukáš Krivosudský, and Saikat Dutta, and Sib Sankar Mal, and Alexander Roller, and Gerald Giester, and Annette Rompel, and Manuel Aureliano
Na+-K+-ATPase and Na+/Ca2+ exchange activities in gills of hyperregulating Carcinus maenas.
February 1999, The American journal of physiology,
Gil Fraqueza, and Juan Fuentes, and Lukáš Krivosudský, and Saikat Dutta, and Sib Sankar Mal, and Alexander Roller, and Gerald Giester, and Annette Rompel, and Manuel Aureliano
Hypertension, Na+/Ca2+ exchanger, and Na+, K+-ATPase.
June 2006, Kidney international,
Gil Fraqueza, and Juan Fuentes, and Lukáš Krivosudský, and Saikat Dutta, and Sib Sankar Mal, and Alexander Roller, and Gerald Giester, and Annette Rompel, and Manuel Aureliano
Increased intracellular calcium and decreased activities of leucocyte Na+,K+-ATPase and Ca2+-ATPase in asthma.
November 1999, Clinical science (London, England : 1979),
Gil Fraqueza, and Juan Fuentes, and Lukáš Krivosudský, and Saikat Dutta, and Sib Sankar Mal, and Alexander Roller, and Gerald Giester, and Annette Rompel, and Manuel Aureliano
Effects of calcium antagonists on (Na+ + K+)-ATPase, Mg2+-ATPase and Ca2+-ATPase activities of rat cortical synaptosomes.
January 1987, General pharmacology,
Gil Fraqueza, and Juan Fuentes, and Lukáš Krivosudský, and Saikat Dutta, and Sib Sankar Mal, and Alexander Roller, and Gerald Giester, and Annette Rompel, and Manuel Aureliano
Na+, K+-ATPase: (Ca2+ + ouabain)-dependent phosphorylation by Pi.
April 1981, FEBS letters,
Copied contents to your clipboard!