| Literature DB >> 6331372 |
L G Lelievre, P Mansier, D Charlemagne, B Swynghedauw.
Abstract
The sensitivity of the Na+, K+-ATPase to ouabain has been studied in sarcolemma vesicles isolated from normal rat heart. Two enzyme forms exhibiting high and low sensitivities to ouabain have been observed in Ca2+-free perfused heart. The half-maximal inhibitory effects occurred with 1-2 X 10(-8) M ouabain. The high sensitivity form undetectable in hearts maintained at a physiological Ca2+ level might represent altered low affinity sites or latent enzyme forms unmasked by low calcium concentrations. The heterogeneity of the Na+, K+-ATPase forms was found to be also modulated by the K+/ouabain antagonism, addition of K+ accentuating the heterogeneity. These in vitro results associated with in vivo experiments on isolated rat heart working under isovolumic conditions suggested that lowering Ca2+ has qualitative and quantitative effects. Low Ca2+ concentrations increased the sensitivities to ouabain and the amplitudes of both the enzyme inhibition and the positive inotropic effects.Entities:
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Year: 1984 PMID: 6331372 DOI: 10.1007/978-3-642-72376-6_17
Source DB: PubMed Journal: Basic Res Cardiol ISSN: 0300-8428 Impact factor: 17.165