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- W2103703426 abstract "We examined inhibitory effects of external multivalent cations Ni2+, Co2+, Cd2+, La3+, Mg2+, and Mn2+ on reverse-mode exchange of the K+-dependent Na+/Ca2+ exchanger NCKX2 and the K+-independent exchanger NCX1 expressed in CCL-39 cells by measuring the rate of Ca2+ uptake with radioisotope tracer and electrophysiological techniques. The apparent affinities for block of Ca2+ uptake by multivalent cations was higher in NCKX2 than NCX1, and the rank order of inhibitory potencies among these cations was different. Additional experiments also showed that external Li+ stimulated reverse-mode exchange by NCX1, but not NCKX2 in the presence of 5 mM K+. Thus, both exchangers exhibited differential sensitivities to not only K+ but also many other external cations. We attempted to locate the putative binding sites within the α motifs for multivalent cations by site-directed mutagenesis experiments. The cation affinities of NCKX2 were altered by mutations of amino acid residues in the α-1 motif, but not by mutations in the α-2 motif. These results contrast with those for NCX1 where mutations in both α-1 and α-2 motifs have been shown previously to affect cation affinities. Susceptibility tests with sulfhydryl alkylating agents suggested that the α-1 and α-2 motifs are situated extracellularly and intracellularly, respectively, in both exchangers. A topological model is proposed in which the extracellular-facing α-1 motif forms an external cation binding site that includes key residues N203, G207C, and I209 in NCKX2, while both α-1 and α-2 motifs together form the binding sites in NCX1. © 2004 Wiley-Liss, Inc." @default.
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- W2103703426 date "2005-01-01" @default.
- W2103703426 modified "2023-09-27" @default.
- W2103703426 title "Different cation sensitivities and binding site domains of Na+-Ca2+-K+ and Na+-Ca2+ exchangers" @default.
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- W2103703426 doi "https://doi.org/10.1002/jcp.20231" @default.
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