Abstract
The interaction of cardiac Na$^+$-Ca$^2+$ 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.
- 3;
- acid
- amino
- animals;
- binding
- binding;
- blotting,
- cattle;
- caveolae,
- caveolin
- caveolins,
- centrifugation,
- chemistry/drug
- chemistry/metabolism
- cholesterol,
- chromatography,
- cyclodextrins,
- density
- effects/metabolism;
- exchanger,
- gel;
- gradient;
- metabolism;
- motifs;
- myocardium,
- pharmacology;
- precipitin
- protein
- sarcolemma,
- sites;
- sodium-calcium
- tests;
- western;
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