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Am J Physiol Cell Physiol 277: C693-C700, 1999;
0363-6143/99 $5.00
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Vol. 277, Issue 4, C693-C700, October 1999

Cloning, expression, and characterization of the trout cardiac Na+/Ca2+ exchanger

Xiao-Hua Xue1, Larry V. Hryshko2, Debora A. Nicoll3, Kenneth D. Philipson3, and Glen F. Tibbits1

1 Cardiac Membrane Research Laboratory, Simon Fraser University, Burnaby, British Columbia V5A 1S6; and 2 Institute of Cardiovascular Sciences, St. Boniface General Hospital Research Centre, The University of Manitoba, Winnipeg, Manitoba R2H 2A6, Canada; and 3 Cardiovascular Research Laboratories, School of Medicine, University of California, Los Angeles, Los Angeles, California 90095-1760

Isoform 1 of the cardiac Na+/Ca2+ exchanger (NCX1) is an important regulator of cytosolic Ca2+ concentration in contraction and relaxation. Studies with trout heart sarcolemmal vesicles have shown NCX to have a high level of activity at 7°C, and this unique property is likely due to differences in protein structure. In this study, we describe the cloning of an NCX (NCX-TR1) from a Lambda ZAP II cDNA library constructed from rainbow trout (Oncorhynchus mykiss) heart RNA. The NCX-TR1 cDNA has an open reading frame that codes for a protein of 968 amino acids with a deduced molecular mass of 108 kDa. A hydropathy plot indicates the protein contains 12 hydrophobic segments (of which the first is predicted to be a cleaved leader peptide) and a large cytoplasmic loop. By analogy to NCX1, NCX-TR1 is predicted to have nine transmembrane segments. The sequences demonstrated to be the exchanger inhibitory peptide site and the regulatory Ca2+ binding site in the cytoplasmic loop of mammalian NCX1 are almost completely conserved in NCX-TR1. NCX-TR1 cRNA was injected into Xenopus oocytes, and after 3-4 days currents were measured by the giant excised patch technique. NCX-TR1 currents measured at ~23°C demonstrated Na+-dependent inactivation and Ca2+-dependent activation in a manner qualitatively similar to that for NCX1 currents.

teleosts; myocardium; contractility; sodium/calcium exchange


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