Characterization of [3H]ouabain binding sites in human brain, platelet, and erythrocyte

J Neurochem. 1985 Jun;44(6):1704-8. doi: 10.1111/j.1471-4159.1985.tb07157.x.

Abstract

[3H]Ouabain binding was investigated in membranes prepared from human brain, erythrocyte, and platelet. Scatchard analysis of [3H]ouabain binding to human hypothalamic membranes revealed a single class of noninteracting binding sites with an apparent affinity constant (KD) of 21 nM. Though the number of [3H]ouabain binding sites was lower in human platelets than in erythrocytes, both tissues exhibited a single class of high-affinity binding sites with an apparent KD similar to that found in human brain. Specific [3H]ouabain binding in basal ganglia tissue from patients with Huntington's disease was more than 50% lower than in tissue from age- and sex-matched controls. These results, along with previous findings in rat brain, suggest that high-affinity [3H]ouabain binding labels the neuronal form of Na, K-ATPase in human brain, and may prove useful in quantitating this enzyme in postmortem brain samples.

MeSH terms

  • Basal Ganglia / analysis
  • Blood Platelets / analysis*
  • Brain Chemistry*
  • Erythrocytes / analysis*
  • Humans
  • Huntington Disease / metabolism
  • In Vitro Techniques
  • Ouabain / metabolism
  • Receptors, Drug / analysis*
  • Sodium-Potassium-Exchanging ATPase*
  • Tritium

Substances

  • Receptors, Drug
  • cardiac glycoside receptors
  • Tritium
  • Ouabain
  • Sodium-Potassium-Exchanging ATPase