lignans and dihydroouabain

lignans has been researched along with dihydroouabain* in 1 studies

Other Studies

1 other study(ies) available for lignans and dihydroouabain

Article	Year
Evidence that mammalian lignans show endogenous digitalis-like activities. Biochemical and biophysical research communications, 1986, Feb-13, Volume: 134, Issue:3 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. Topics: 4-Butyrolactone; Animals; Binding, Competitive; Cross Reactions; Digoxin; Furans; Guinea Pigs; Humans; In Vitro Techniques; Lignans; Myocardium; Ouabain; Radioimmunoassay; Receptors, Drug; Sodium-Potassium-Exchanging ATPase	1986

Article

Year

Evidence that mammalian lignans show endogenous digitalis-like activities.

Biochemical and biophysical research communications, 1986, Feb-13, Volume: 134, Issue:3

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.

Topics: 4-Butyrolactone; Animals; Binding, Competitive; Cross Reactions; Digoxin; Furans; Guinea Pigs; Humans; In Vitro Techniques; Lignans; Myocardium; Ouabain; Radioimmunoassay; Receptors, Drug; Sodium-Potassium-Exchanging ATPase

1986