Different oxidant sensitivities of the alpha 1 and alpha 2 isoforms of Na+/K(+)-ATPase expressed in baculovirus-infected insect cells

Biochem Biophys Res Commun. 1995 Feb 6;207(1):155-9. doi: 10.1006/bbrc.1995.1166.

Abstract

Inhibition of Na+/K(+)-ATPase by partially reduced oxygen metabolites is an early event in the course of cell injury caused by oxidative stress. We showed before that isoforms of the enzyme obtained from different sources have different oxidant sensitivities. To evaluate the role of tissue-specific impurities in this difference, cDNAs of alpha 1 and alpha 2 isoforms were expressed in Sf-9 insect cells, and the effects of H2O2 on the resulting isolated enzymes were studied. The expressed alpha 2 was significantly more sensitive than alpha 1 to H2O2. These findings, together with our previous data showing different oxidant sensitivities of alpha 1 and alpha 3 in a cardiac enzyme preparation, indicate that differential oxidant sensitivities of Na+/K(+)-ATPase isoforms of various tissues are dictated by the primary sequences of alpha 1, alpha 2, and alpha 3 subunits.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Baculoviridae
  • Brain Stem / enzymology
  • Cell Line
  • Dogs
  • Hydrogen Peroxide / pharmacology*
  • Isoenzymes / biosynthesis
  • Isoenzymes / metabolism*
  • Kidney / enzymology
  • Kinetics
  • Oxidants / pharmacology*
  • Oxidative Stress*
  • Rats
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / metabolism
  • Rodentia
  • Sodium-Potassium-Exchanging ATPase / biosynthesis
  • Sodium-Potassium-Exchanging ATPase / metabolism*
  • Spodoptera
  • Transfection

Substances

  • Isoenzymes
  • Oxidants
  • Recombinant Proteins
  • Hydrogen Peroxide
  • Sodium-Potassium-Exchanging ATPase