Key result
Specific amino acid substitutions in the alpha-1 and alpha-2 repeats of Na+/Ca2+ exchangers account for the differential sensitivity of NCX1 and NCX3 isoforms to external Ni2+ and Li+.
Population
CCL39 cells stably expressing NCX1/NCX3 chimeras or mutants
Comparison
Chimeric analysis and site-directed mutagenesis… vs Wild-type NCX1 and NCX3
Design
Preclinical
Authors
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Highlights potential for isoform-selective NCX modulation; leaves open translation to cardiovascular therapeutics.
Specific amino acid residues in the alpha-1 and alpha-2 repeats of Na+/Ca2+ exchangers form an ion interaction domain that determines differential sensitivity to Ni2+ and Li+.
Iwamoto et al. (1999) studied this question. NCX1/NCX3 chimeras or mutants vs. Wild-type NCX1 and NCX3 was evaluated on Intracellular Na+-dependent 45Ca2+ uptake (Ni2+ or Li+ sensitivity). Specific amino acid substitutions in the alpha-1 and alpha-2 repeats of Na+/Ca2+ exchangers account for the differential sensitivity of NCX1 and NCX3 isoforms to external Ni2+ and Li+.
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