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

Title:

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

Creator:

Vrbjar, N., Monika Ivanová, Oľga Pecháňová, and Mária Gerová

Identifier:

https://cdk.lib.cas.cz/client/handle/uuid:b0f26d5b-c332-49e0-a999-556ec93eda99
uuid:b0f26d5b-c332-49e0-a999-556ec93eda99
issn:0862-8408

Subject:

Fyziologie člověka a srovnávací fyziologie, fyziologie člověka, human physiology, Sodium pump, Heart, Pressure overload, Nitric oxide, L-NAME, 14, and 612

Type:

article, studie, model:article, and TEXT

Format:

print, bez média, and svazek

Description:

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., N. Vrbjar, M. Strnisková, O. Pecháňová, M. Gerová., and Obsahuje bibliografii

Language:

English

Rights:

http://creativecommons.org/licenses/by-nc-sa/4.0/
policy:public

Source:

Physiological research | 2002 Volume:51 | Number:6

Harvested from:

CDK

Metadata only:

false