Inhibition of Na<sup>+</sup>/K<sup>+</sup> - and Ca<sup>2+</sup> -ATPase activities by phosphotetradecavanadate
- Autor(en)
- Gil Fraqueza, Juan Fuentes, Lukáš Krivosudský, Saikat Dutta, Sib Sankar Mal, Alexander Roller, Gerald Giester, Annette Rompel, Manuel Aureliano
- Abstrakt
-
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 [P
2
W
18
O
62
]
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 Cs
5.6
H
3.4
PV
14
O
42
(PV
14
)and we confront the data with activity of other commonly encountered polyoxovanadates, decavanadate (V
10
)and monovanadate (V
1
). The X-ray crystal structure of PV
14
was solved and contains two trans-bicapped α-Keggin anions H
x
PV
14
O
42
(9-x)-
. The anion is built up from the classical Keggin structure [(PO
4
)@(V
12
O
36
)]capped by two [VO]units. PV
14
(10 μM)exhibited higher ex-vivo inhibitory effect on Na
+
/K
+
-ATPase (78%)than was observed at the same concentrations of V
10
(66%)or V
1
(33%). Moreover, PV
14
is also a potent in vitro inhibitor of the Ca
2+
-ATPase activity (IC
50
5 μM)exhibiting stronger inhibition than the previously reported activities for V
10
(15 μM)and V
1
(80 μM). Putting it all together, when compared both P-typye ATPases it is suggested that PV
14
exibited a high potential to act as an in vivo inhibitor of the Na
+
/K
+
-ATPase associated with chloride secretion.
- Organisation(en)
- Zentrum für Röntgenstrukturanalyse, Institut für Anorganische Chemie, Institut für Mineralogie und Kristallographie, Institut für Biophysikalische Chemie
- Journal
- Journal of Inorganic Biochemistry
- Band
- 197
- Anzahl der Seiten
- 7
- ISSN
- 0162-0134
- DOI
- https://doi.org/10.1016/j.jinorgbio.2019.110700
- Publikationsdatum
- 04-2019
- Publikationsstatus
- Elektronische Veröffentlichung vor Drucklegung
- Peer-reviewed
- Ja
- ÖFOS 2012
- 104004 Chemische Biologie, 104003 Anorganische Chemie, 104024 Röntgenstrukturanalyse, 105113 Kristallographie
- ASJC Scopus Sachgebiete
- Biochemistry, Inorganic Chemistry
- Link zum Portal
- https://ucris.univie.ac.at/portal/de/publications/inhibition-of-nak--and-ca2-atpase-activities-by-phosphotetradecavanadate(0d97b7c5-e299-42be-9400-27d790aa9a0b).html