Inhibition of SERCA and PMCA Ca2+-ATPase activities by polyoxotungstates

Manuel Aureliano (Korresp. Autor*in), Gil Fraqueza, Maria Berrocal, Juan J. Cordoba-Granados, Nadiia I. Gumerova, Annette Rompel (Korresp. Autor*in), Carlos Gutierrez-Merino, Ana M. Mata

Veröffentlichungen: Beitrag in FachzeitschriftArtikelPeer Reviewed


Plasma membrane calcium ATPases (PMCA) and sarco(endo) reticulum calcium ATPases (SERCA) are key proteins in the maintenance of calcium homeostasis. Herein, we compare for the first time the inhibition of SERCA and PMCA calcium pumps by several polyoxotungstates (POTs), namely by Wells-Dawson phosphotungstate anions [P 2W 18O 62] 6− (intact, {P 2W 18}), [P 2W 17O 61] 10− (monolacunary, {P 2W 17}), [P 2W 15O 56] 12− (trilacunary, {P 2W 15}), [H 2P 2W 12O 48] 12− (hexalacunary, {P 2W 12}), [H 3P 2W 15V 3O 62] 6− (trivanadium-substituted, {P 2W 15V 3}) and by Preyssler-type anion [NaP 5W 30O 110] 14− ({P 5W 30}). The speciation in the solutions of tested POTs was investigated by 31P and 51V NMR spectroscopy. The tested POTs inhibited SERCA Ca 2+-ATPase activity, whereby the Preyssler POT showed the strongest effect, with an IC 50 value of 0.37 μM. For {P 2W 17} and {P 2W 15V 3} higher IC 50 values were determined: 0.72 and 0.95 μM, respectively. The studied POTs showed to be more potent inhibitors of PMCA Ca 2+-ATPase activity, with lower IC 50 values for {P 2W 17}, {P 5W 30} and {P 2W 15V 3}.
FachzeitschriftJournal of Inorganic Biochemistry
PublikationsstatusVeröffentlicht - Nov. 2022

ÖFOS 2012

  • 106006 Biophysik
  • 106002 Biochemie
  • 106023 Molekularbiologie