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http://purl.uniprot.org/citations/8021246http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8021246http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8021246http://www.w3.org/2000/01/rdf-schema#comment"The Na(+)-Ca2+ exchanger is an important regulator of cellular Ca2+ levels, and one isoform of this transporter, NCX1, has been cloned previously (Nicoll, D.A., Longoni, S., and Philipson, K.D. (1990) Science 250, 562-565). We now report the cloning of a second isoform (NCX2) of the Na(+)-Ca2+ exchanger which was present in a rat brain cDNA library. NCX2 is predicted to code for a protein of 921 amino acids. NCX1 and NCX2 are 61 and 65% identical at the nucleotide and amino acid levels, respectively, and are the products of different genes. The genes for NCX1 and NCX2 are located on human chromosomes 2 and 14, respectively. Hydropathy profiles of the two exchangers are very similar. Transcripts of NCX2 are detected in brain and skeletal muscle. NCX2 was expressed in Xenopus oocytes and Na(+)-Ca2+ exchange activity was analyzed electrophysiologically by the giant inside-out, excised patch technique. Outward currents were evoked by the application of Na+ with the exchanger operating in the reversed mode (extracellular Ca2+ exchanging for intracellular Na+). The affinity for Na+ (30 mM) and the current-voltage relationship of NCX2 are similar to those for NCX1. Like NCX1, NCX2 is secondarily regulated by intracellular Ca2+, but the affinity of NCX2 for regulatory Ca2+ (1.5 microM) upon initial application of Na+ is lower than that of NCX1 (0.3 microM). The existence of multiple Na(+)-Ca2+ exchanger isoforms may provide flexibility for regulation and expression."xsd:string
http://purl.uniprot.org/citations/8021246http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(17)32458-4"xsd:string
http://purl.uniprot.org/citations/8021246http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(17)32458-4"xsd:string
http://purl.uniprot.org/citations/8021246http://purl.uniprot.org/core/author"Li Z."xsd:string
http://purl.uniprot.org/citations/8021246http://purl.uniprot.org/core/author"Li Z."xsd:string
http://purl.uniprot.org/citations/8021246http://purl.uniprot.org/core/author"Matsuoka S."xsd:string
http://purl.uniprot.org/citations/8021246http://purl.uniprot.org/core/author"Matsuoka S."xsd:string
http://purl.uniprot.org/citations/8021246http://purl.uniprot.org/core/author"Lifton R.P."xsd:string
http://purl.uniprot.org/citations/8021246http://purl.uniprot.org/core/author"Lifton R.P."xsd:string
http://purl.uniprot.org/citations/8021246http://purl.uniprot.org/core/author"Nicoll D.A."xsd:string
http://purl.uniprot.org/citations/8021246http://purl.uniprot.org/core/author"Nicoll D.A."xsd:string
http://purl.uniprot.org/citations/8021246http://purl.uniprot.org/core/author"Philipson K.D."xsd:string
http://purl.uniprot.org/citations/8021246http://purl.uniprot.org/core/author"Philipson K.D."xsd:string
http://purl.uniprot.org/citations/8021246http://purl.uniprot.org/core/author"Bershon M.M."xsd:string
http://purl.uniprot.org/citations/8021246http://purl.uniprot.org/core/author"Bershon M.M."xsd:string
http://purl.uniprot.org/citations/8021246http://purl.uniprot.org/core/author"Burke E.P."xsd:string
http://purl.uniprot.org/citations/8021246http://purl.uniprot.org/core/author"Burke E.P."xsd:string
http://purl.uniprot.org/citations/8021246http://purl.uniprot.org/core/author"Hryshko L.V."xsd:string
http://purl.uniprot.org/citations/8021246http://purl.uniprot.org/core/author"Hryshko L.V."xsd:string
http://purl.uniprot.org/citations/8021246http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/8021246http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/8021246http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/8021246http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string