Na+-K+-ATPase properties in rat heart and skeletal muscle 3 mo after coronary artery ligation.

Abstract

This study was designed to determine whether chronic heart failure (CHF) results in changes in Na(+)-K(+)-ATPase properties in heart and skeletal muscles of different fiber-type composition. Adult rats were randomly assigned to a control (Con; n = 8) or CHF (n = 8) group. CHF was induced by ligation of the left main coronary artery. Examination of Na(+)-K(+)-ATPase activity (means +/- SE) 12 wk after the ligation measured, using the 3-O-methylfluorescein phosphatase assay (3-O-MFPase), indicated higher (P < 0.05) levels in soleus (Sol) (250 +/- 13 vs. 179 +/- 18 nmol.mg protein(-1).h(-1)) and lower (P < 0.05) levels in diaphragm (Dia) (200 +/- 12 vs. 272 +/- 27 nmol.mg protein(-1).h(-1)) and left ventricle (LV) (760 +/- 62 vs. 992 +/- 16 nmol.mg protein(-1).h(-1)) in CHF compared with Con, respectively. Na(+)-K(+)-ATPase protein content, measured by the [(3)H]ouabain binding technique, was higher (P < 0.05) in white gastrocnemius (WG) (166 +/- 12 vs. 135 +/- 7.6 pmol/g wet wt) and lower (P < 0.05) in Sol (193 +/- 20 vs. 260 +/- 8.6 pmol/g wet wt) and LV (159 +/- 10 vs. 221 +/- 10 pmol/g wet wt) in CHF compared with Con, respectively. Isoform content in CHF, measured by Western blot techniques, showed both increases (WG; P < 0.05) and decreases (Sol; P < 0.05) in alpha(1). For alpha(2), only increases [red gastrocnemius (RG), Sol, and Dia; P < 0.05] occurred. The beta(2)-isoform was decreased (LV, Sol, RG, and WG; P < 0.05) in CHF, whereas the beta(1) was both increased (WG and Dia; P < 0.05) and decreased (Sol and LV; P < 0.05). For beta(3), decreases (P < 0.05) in RG were observed in CHF, whereas no differences were found in Sol and WG between CHF and Con. It is concluded that CHF results in alterations in Na(+)-K(+)-ATPase that are muscle specific and property specific. Although decreases in Na(+)-K(+)-ATPase content would appear to explain the lower 3-O-MFPase in the LV, such does not appear to be the case in skeletal muscles where a dissociation between these properties was observed.

• Authors: D J Barr, H J Green, D S Lounsbury, J W E Rush, J Ouyang
• Journal: Journal of applied physiology (Bethesda, Md. : 1985) (J Appl Physiol (1985)) Vol. 99 Issue 2 Pg. 656-64 (Aug 2005) ISSN: 8750-7587 [Print] United States
• PMID: 15817721 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Sodium-Potassium-Exchanging ATPase

Topics

• Adaptation, Physiological
• Animals
• Chronic Disease
• Coronary Artery Disease (complications, enzymology)
• Coronary Vessels (surgery)
• Enzyme Activation
• Heart Failure (enzymology, etiology)
• Ligation
• Male
• Muscle, Skeletal (enzymology)
• Myocardium (enzymology)
• Rats
• Rats, Sprague-Dawley
• Sodium-Potassium-Exchanging ATPase (metabolism)