Functional and structural properties of Na+/K+-ATPase enzyme in neonatal erythrocytes

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Abstract

Background - The Na+/K+-pump is the main regulator enzyme of intracellular monovalent cation concentration. There are only limited data available concerning its structure and function in healthy neonates, in comparison with data available regarding its structure and function in children. Patients and methods - Samples of 100 μL of anticoagulated blood were taken from 53 healthy neonates (age under 6th postnatal day, median age 3.5 days) and 61 healthy children (median age 12.4 months, range 6-36 months). The Na+/K+-ATPase activity, its sensitivity to ouabain (a digoxin-analogue substance) and the expression of Na+/K+-ATPase subunit isoforms were determined. Results - The enzyme activity (429.2 ± 17.1 versus 295.5 ± 10.2 U, P <0.001) and I50 value for ouabain inhibition (1.50 ± 0.10 versus 0.96 ± 0.10 μmol L-1, P <0.05) was higher in neonates. More α1 subunits (relative density: 1.16 ± 0.10 versus 0.75 ± 0.03, P <0.001) and higher α12 ratio (4.14 ± 0.21 versus 2.02 ± 0.16, P <0.01) were detected. Conclusion - This is the first study demonstrating changes of Na+/K+-ATPase molecules not only in enzyme activity, but also on protein level. Our results might contribute to the understanding of the resistance of neonatal cell membranes toward the pharmacodynamic actions of cardiac glycosides.

Original languageEnglish
Pages (from-to)543-545
Number of pages3
JournalEuropean Journal of Clinical Investigation
Volume28
Issue number7
DOIs
Publication statusPublished - 1998

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Adenosine Triphosphatases
Structural properties
Erythrocytes
Enzyme activity
Newborn Infant
Ouabain
Enzymes
Pharmacodynamics
Monovalent Cations
Cardiac Glycosides
Specific Gravity
Digoxin
Cell membranes
Protein Isoforms
Blood
Cell Membrane
Pumps
Molecules
sodium-translocating ATPase
Proteins

Keywords

  • Alpha subunit
  • Digoxin resistance
  • Erythrocyte
  • Isoform
  • Na/K-ATPase
  • Neonates

ASJC Scopus subject areas

  • Medicine(all)

Cite this

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title = "Functional and structural properties of Na+/K+-ATPase enzyme in neonatal erythrocytes",
abstract = "Background - The Na+/K+-pump is the main regulator enzyme of intracellular monovalent cation concentration. There are only limited data available concerning its structure and function in healthy neonates, in comparison with data available regarding its structure and function in children. Patients and methods - Samples of 100 μL of anticoagulated blood were taken from 53 healthy neonates (age under 6th postnatal day, median age 3.5 days) and 61 healthy children (median age 12.4 months, range 6-36 months). The Na+/K+-ATPase activity, its sensitivity to ouabain (a digoxin-analogue substance) and the expression of Na+/K+-ATPase subunit isoforms were determined. Results - The enzyme activity (429.2 ± 17.1 versus 295.5 ± 10.2 U, P <0.001) and I50 value for ouabain inhibition (1.50 ± 0.10 versus 0.96 ± 0.10 μmol L-1, P <0.05) was higher in neonates. More α1 subunits (relative density: 1.16 ± 0.10 versus 0.75 ± 0.03, P <0.001) and higher α1/α2 ratio (4.14 ± 0.21 versus 2.02 ± 0.16, P <0.01) were detected. Conclusion - This is the first study demonstrating changes of Na+/K+-ATPase molecules not only in enzyme activity, but also on protein level. Our results might contribute to the understanding of the resistance of neonatal cell membranes toward the pharmacodynamic actions of cardiac glycosides.",
keywords = "Alpha subunit, Digoxin resistance, Erythrocyte, Isoform, Na/K-ATPase, Neonates",
author = "B. V{\'a}s{\'a}rhelyi and A. V{\'e}r and A. Nobilis and T. Szab{\'o} and T. Tulassay",
year = "1998",
doi = "10.1046/j.1365-2362.1998.00337.x",
language = "English",
volume = "28",
pages = "543--545",
journal = "European Journal of Clinical Investigation",
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T1 - Functional and structural properties of Na+/K+-ATPase enzyme in neonatal erythrocytes

AU - Vásárhelyi, B.

AU - Vér, A.

AU - Nobilis, A.

AU - Szabó, T.

AU - Tulassay, T.

PY - 1998

Y1 - 1998

N2 - Background - The Na+/K+-pump is the main regulator enzyme of intracellular monovalent cation concentration. There are only limited data available concerning its structure and function in healthy neonates, in comparison with data available regarding its structure and function in children. Patients and methods - Samples of 100 μL of anticoagulated blood were taken from 53 healthy neonates (age under 6th postnatal day, median age 3.5 days) and 61 healthy children (median age 12.4 months, range 6-36 months). The Na+/K+-ATPase activity, its sensitivity to ouabain (a digoxin-analogue substance) and the expression of Na+/K+-ATPase subunit isoforms were determined. Results - The enzyme activity (429.2 ± 17.1 versus 295.5 ± 10.2 U, P <0.001) and I50 value for ouabain inhibition (1.50 ± 0.10 versus 0.96 ± 0.10 μmol L-1, P <0.05) was higher in neonates. More α1 subunits (relative density: 1.16 ± 0.10 versus 0.75 ± 0.03, P <0.001) and higher α1/α2 ratio (4.14 ± 0.21 versus 2.02 ± 0.16, P <0.01) were detected. Conclusion - This is the first study demonstrating changes of Na+/K+-ATPase molecules not only in enzyme activity, but also on protein level. Our results might contribute to the understanding of the resistance of neonatal cell membranes toward the pharmacodynamic actions of cardiac glycosides.

AB - Background - The Na+/K+-pump is the main regulator enzyme of intracellular monovalent cation concentration. There are only limited data available concerning its structure and function in healthy neonates, in comparison with data available regarding its structure and function in children. Patients and methods - Samples of 100 μL of anticoagulated blood were taken from 53 healthy neonates (age under 6th postnatal day, median age 3.5 days) and 61 healthy children (median age 12.4 months, range 6-36 months). The Na+/K+-ATPase activity, its sensitivity to ouabain (a digoxin-analogue substance) and the expression of Na+/K+-ATPase subunit isoforms were determined. Results - The enzyme activity (429.2 ± 17.1 versus 295.5 ± 10.2 U, P <0.001) and I50 value for ouabain inhibition (1.50 ± 0.10 versus 0.96 ± 0.10 μmol L-1, P <0.05) was higher in neonates. More α1 subunits (relative density: 1.16 ± 0.10 versus 0.75 ± 0.03, P <0.001) and higher α1/α2 ratio (4.14 ± 0.21 versus 2.02 ± 0.16, P <0.01) were detected. Conclusion - This is the first study demonstrating changes of Na+/K+-ATPase molecules not only in enzyme activity, but also on protein level. Our results might contribute to the understanding of the resistance of neonatal cell membranes toward the pharmacodynamic actions of cardiac glycosides.

KW - Alpha subunit

KW - Digoxin resistance

KW - Erythrocyte

KW - Isoform

KW - Na/K-ATPase

KW - Neonates

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DO - 10.1046/j.1365-2362.1998.00337.x

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