Key result
All human Na+-K+-ATPase α-subunit isoforms have a similar affinity for ouabain (mean Kd 18 ± 6 nM), with failing hearts showing approximately 50% fewer binding sites than nonfailing hearts.
Population
Membranes from a panel of different human tissues, cell lines derived from human tissues, and nonfailing and…
Comparison
Ouabain (cardiac glycoside) binding assay vs Nonfailing vs failing human heart samples
Design
Preclinical
Authors
Loading...
Reduced pump density may drive glycoside sensitivity in failing hearts; animal data leave isoform-selective targeting untested in humans.
All human Na+-K+-ATPase alpha-subunit isoforms have similar affinity for ouabain, suggesting that the increased sensitivity of failing hearts to cardiac glycosides is due to a reduction in total pump number rather than altered affinity.
Wang et al. (2001) studied Heart failure. Ouabain binding to Na+-K+-ATPase α-subunit isoforms vs. Nonfailing vs failing human heart samples was evaluated on Equilibrium dissociation constant (Kd) for ouabain binding. All human Na+-K+-ATPase α-subunit isoforms have a similar affinity for ouabain (mean Kd 18 ± 6 nM), with failing hearts showing approximately 50% fewer binding sites than nonfailing hearts.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: