Modifications induced by plasma of gestational hypertensive women on the Na+/K+-ATPase obtained from human placenta

N. Cester, R. A. Rabini, A. L. Tranquilli, G. Lucarelli, E. Salvolini, R. Staffolani, E. Amler, G. Zolese, L. Mazzanti

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

In order to investigate the molecular mechanisms of the inhibition of Na+/K+-ATPase in Gestational Hypertension (GH), we incubated Na+K+-ATPase purified from human placenta of 6 healthy normotensive women with plasma from 6 GH women and 6 healthy controls. We determined the enzyme activity by the method of Esman, and the anthroyl-ouabain-binding capacity, dissociation constant (K(d)) and average lifetime values (τ) by the static and dynamic fluorescence of anthroyl-ouabain. The lipid annulus of the enzyme was studied by static and dynamic fluorescence of 1-(4-trimethylaminophenyl)-6-phenyl-1,3,5-hexatriene (TMA-DPH). The addition of total and protein-free GH plasma to normal Na+/K+-ATPase significantly inhibited the enzymatic activity even at the lowest concentration studied (1:100), as well as the ouabain-binding capacity, K(d) and τ. GH plasma significantly decreased the fluorescence polarization and lifetime values of TMA-DPH. These observations indicate that the inhibition caused by GH plasma on Na+/K+-ATPase might be due to a reduction of the number of active molecules or a modification of the ouabain-binding site suggesting the existence of digitalis-like factor. A link between the modification of the lipid moiety of the enzyme and the Na+/K+-ATPase inhibition might be hypothesized.

Original languageEnglish
Pages (from-to)125-129
Number of pages5
JournalMolecular and Cellular Biochemistry
Volume170
Issue number1-2
DOIs
Publication statusPublished - 1997

Fingerprint

Pregnancy Induced Hypertension
Placenta
Adenosine Triphosphatases
Ouabain
Plasmas
Fluorescence
Enzymes
Lipids
Fluorescence Polarization
Enzyme activity
Binding Sites
sodium-translocating ATPase
Polarization
Molecules
Proteins

Keywords

  • Activity
  • Fluorescence
  • Gestational hypertension
  • Ouabain
  • Plasma

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Modifications induced by plasma of gestational hypertensive women on the Na+/K+-ATPase obtained from human placenta. / Cester, N.; Rabini, R. A.; Tranquilli, A. L.; Lucarelli, G.; Salvolini, E.; Staffolani, R.; Amler, E.; Zolese, G.; Mazzanti, L.

In: Molecular and Cellular Biochemistry, Vol. 170, No. 1-2, 1997, p. 125-129.

Research output: Contribution to journalArticle

Cester, N, Rabini, RA, Tranquilli, AL, Lucarelli, G, Salvolini, E, Staffolani, R, Amler, E, Zolese, G & Mazzanti, L 1997, 'Modifications induced by plasma of gestational hypertensive women on the Na+/K+-ATPase obtained from human placenta', Molecular and Cellular Biochemistry, vol. 170, no. 1-2, pp. 125-129. https://doi.org/10.1023/A:1006849318305
Cester, N. ; Rabini, R. A. ; Tranquilli, A. L. ; Lucarelli, G. ; Salvolini, E. ; Staffolani, R. ; Amler, E. ; Zolese, G. ; Mazzanti, L. / Modifications induced by plasma of gestational hypertensive women on the Na+/K+-ATPase obtained from human placenta. In: Molecular and Cellular Biochemistry. 1997 ; Vol. 170, No. 1-2. pp. 125-129.
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