Physiol. Res. 51: 565-569, 2002


Short-term NO Synthase Inhibition and the ATP Affinity of Cardiac Na,K-ATPase


Institute for Heart Research and 1Institute of Normal and Pathological Physiology, Slovak Academy of Sciences, Bratislava, Slovak Republic

Received October 17, 2001
Accepted March 20, 2002

It was previously shown that 4 hours´ lasting inhibition of nitric oxide synthesis by administration of an L-arginine analogue, the NG-nitro-L-arginine methyl ester (L-NAME) changed the affinity of the Na-binding site of Na,K-ATPase thus resulting in elevation of enzyme activity especially at higher concentrations of sodium. Using the same experimental model, we focused our attention in the present study to the question of binding of ATP to the enzyme molecule in the left ventricle (LV), ventricular septum (S) and the right ventricle (RV) of the dog heart. Activation of the enzyme by increasing concentrations of ATP revealed a significant increase of the Vmax only in septum (by 38 %). The KM increased significantly in septum (by 40 %) and in left ventricle (by 56 %) indicating an altered sensitivity of the ATP-binding site of Na,K-ATPase in the hearts of NO-deficient animals. The alterations of Na,K-ATPase in its ability to bind and hydrolyze ATP are localized to the tissue surrounding the cavity of the left ventricle

Key words
Sodium pump · Heart · Pressure overload · Nitric oxide · L-NAME

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© 2002 by the Institute of Physiology, Czech Academy of Sciences

ISSN 0862 - 8408

Issue 6