Evidence that mammalian lignans show endogenous digitalis-like activities

Biochem Biophys Res Commun. 1986 Feb 13;134(3):1064-70. doi: 10.1016/0006-291x(86)90359-1.

Abstract

Enterolactone, a lignan that has been identified in biological samples from man and several mammals, shares with ascorbic acid and cardiac glycosides a gamma-butyrolactone. It displaces 3H-ouabain from its binding sites on cardiac digitalis receptor and inhibits, dose dependently, the Na+, K+-ATPase activity of human and guinea-pig heart. The time dependence of this inhibition resembles that of dihydroouabain, a cardiac glycoside in which the lactone ring does not contain conjugated double bonds. The active concentrations of enterolactone as inhibitor of Na+,K+-ATPase are in the 10(-4) M range and, at those concentrations, the cross-reactivity with antidigoxin antibodies is low. Lignans may contribute to the putative digitalis-like activity found in tissues, blood and urine of several mammals including man.

MeSH terms

  • 4-Butyrolactone / analogs & derivatives
  • 4-Butyrolactone / metabolism
  • 4-Butyrolactone / physiology*
  • Animals
  • Binding, Competitive
  • Cross Reactions
  • Digoxin / immunology
  • Furans / physiology*
  • Guinea Pigs
  • Humans
  • In Vitro Techniques
  • Lignans*
  • Myocardium / enzymology
  • Ouabain / analogs & derivatives
  • Ouabain / metabolism
  • Radioimmunoassay
  • Receptors, Drug / metabolism*
  • Sodium-Potassium-Exchanging ATPase / antagonists & inhibitors*

Substances

  • Furans
  • Lignans
  • Receptors, Drug
  • digitalis receptor
  • dihydroouabain
  • Ouabain
  • Digoxin
  • Sodium-Potassium-Exchanging ATPase
  • 4-Butyrolactone
  • 2,3-bis(3'-hydroxybenzyl)butyrolactone