Evidence for cardiac sodium-calcium exchanger association with caveolin-3.
The interaction of cardiac Na+-Ca2+ exchange (NCX1) with caveolin proteins was investigated in sarcolemmal vesicles. Western blots of sarcolemmal vesicles revealed the presence of caveolin-1, -2, and -3. NCX1 co-fractionated more closely with caveolin-3 than caveolin-1 on sucrose density gradients. NCX1 has five possible caveolin-binding motifs and NCX1 co-precipitated specifically ... with caveolin-3. Molecular sieve column chromatography indicated that this co-precipitation was not due to incomplete solubilization of lipid raft microdomains. Cholesterol chelation in vesicles decreased NCX1 transport activity and caveolin-3 co-precipitation. NCX1 may play a role in caveolar transmembrane signaling in addition to its role in excitation-contraction coupling.
Mesh Terms:
Amino Acid Motifs, Animals, Binding Sites, Blotting, Western, Cattle, Caveolae, Caveolin 3, Caveolins, Centrifugation, Density Gradient, Cholesterol, Chromatography, Gel, Cyclodextrins, Myocardium, Precipitin Tests, Protein Binding, Sarcolemma, Sodium-Calcium Exchanger
Amino Acid Motifs, Animals, Binding Sites, Blotting, Western, Cattle, Caveolae, Caveolin 3, Caveolins, Centrifugation, Density Gradient, Cholesterol, Chromatography, Gel, Cyclodextrins, Myocardium, Precipitin Tests, Protein Binding, Sarcolemma, Sodium-Calcium Exchanger
FEBS Lett.
Date: Jan. 30, 2002
PubMed ID: 11821059
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