Document Detail


Fatty acid-induced modulation of ouabain responsiveness of rat Na, K-ATPase isoforms.
MedLine Citation:
PMID:  10051686     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Membrane phospholipids represent a potential influence on the enzymatic properties of the Na,K-ATPase. Little is known concerning the effects of the fatty acid environment surrounding the enzyme on the kinetic properties of the Na,K-ATPase. We used the most obvious difference among the alpha isoforms of rat, their affinities for digitalis glycosides, to examine the relationship between the lipid environment and the Na,K-ATPase. Specific membrane environments that differ in their fatty acid composition were produced by drug-induced diabetes, as well as variations in diet. The alpha1 isoforms in various tissues were then characterized by their resistance to ouabain in Na,K-ATPase-enriched membrane microsomal fractions. The Na,K-ATPase activity in nerves and hearts were altered by diabetes and partially restored in nerves after a fish oil diet. Evaluation of enzyme kinetics (dose-response curves for ouabain) in membrane preparations allowed us to correlate the ouabain affinity of alpha1 isoform with fatty acid composition. The affinity of the alpha1 isoform for ouabain was significantly increased with accretions in the total amount of fatty acids of the n-6 series (P < 0.0001). Our observations provide a partial explanation for the observed difference in isoform properties among tissues. Moreover, these results underline the interaction between membrane fatty acids and the glycoside binding site of the Na,K-ATPase alpha1 subunit.
Authors:
A Gerbi; J M Maixent
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Publication Detail:
Type:  Comparative Study; Journal Article    
Journal Detail:
Title:  The Journal of membrane biology     Volume:  168     ISSN:  0022-2631     ISO Abbreviation:  J. Membr. Biol.     Publication Date:  1999 Mar 
Date Detail:
Created Date:  1999-04-22     Completed Date:  1999-04-22     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  0211301     Medline TA:  J Membr Biol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  19-27     Citation Subset:  IM    
Affiliation:
Laboratoire de Recherche Cardiologique, Faculté de Médecine, 15 Bd Pierre Dramard 13015, Marseille, France.
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MeSH Terms
Descriptor/Qualifier:
Animals
Cell Membrane / chemistry
Diabetes Mellitus, Experimental / enzymology
Dietary Fats / pharmacology
Docosahexaenoic Acids / pharmacology
Eicosapentaenoic Acid / pharmacology
Enzyme Inhibitors / pharmacology*
Fatty Acids / analysis,  pharmacology*
Fatty Acids, Omega-6
Fatty Acids, Unsaturated / pharmacology
Fish Oils / pharmacology
Male
Membrane Lipids / analysis,  physiology*
Nerve Tissue Proteins / antagonists & inhibitors
Organ Specificity
Ouabain / pharmacology*
Plant Oils / pharmacology
Protein Isoforms / antagonists & inhibitors*
Rats
Rats, Sprague-Dawley
Sodium-Potassium-Exchanging ATPase / antagonists & inhibitors*
Streptozocin
Chemical
Reg. No./Substance:
0/Dietary Fats; 0/Enzyme Inhibitors; 0/Fatty Acids; 0/Fatty Acids, Omega-6; 0/Fatty Acids, Unsaturated; 0/Fish Oils; 0/Membrane Lipids; 0/Nerve Tissue Proteins; 0/Plant Oils; 0/Protein Isoforms; 1553-41-9/Eicosapentaenoic Acid; 18883-66-4/Streptozocin; 25167-62-8/Docosahexaenoic Acids; 630-60-4/Ouabain; 8001-25-0/olive oil; EC 3.6.3.9/Sodium-Potassium-Exchanging ATPase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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