Molecular Studies of the Cardiac Sarcolemmal Sodium‐Calcium Exchanger
- 17 December 1991
- journal article
- review article
- Published by Wiley in Annals of the New York Academy of Sciences
- Vol. 639 (1), 181-188
- https://doi.org/10.1111/j.1749-6632.1991.tb17305.x
Abstract
The molecular nature of the canine cardiac sarcolemmal Na(+)-Ca2+ exchanger has been investigated by purification of the protein and by sequencing and expression of an exchanger cDNA clone. The mature exchanger protein is apparently 120 kDa, with glycosylation at a single asparagine residue near the amino terminus. A proposed model for the exchanger protein includes 11 transmembrane segments, a large cytoplasmic domain that is not involved in ion translocation, an exchanger inhibitory site, two Ca2+ interaction sites and an ion-translocation pathway. Experiments are now under way to test the proposed model.This publication has 8 references indexed in Scilit:
- Identification of a peptide inhibitor of the cardiac sarcolemmal Na(+)-Ca2+ exchanger.Journal of Biological Chemistry, 1991
- Molecular Cloning and Functional Expression of the Cardiac Sarcolemmal Na + -Ca 2+ ExchangerScience, 1990
- The role of charged amino acids in the localization of secreted and membrane proteinsCell, 1990
- The Calmodulin Binding Domain of the Plasma Membrane Ca2+ Pump Interacts Both with Calmodulin and with Another Part of the PumpJournal of Biological Chemistry, 1989
- Sodium-calcium exchange current. Dependence on internal Ca and Na and competitive binding of external Na and Ca.The Journal of general physiology, 1989
- Location of high affinity Ca2 +-binding sites within the predicted transmembrahe domain of the sarco-plasmic reticulum Ca2+-ATPaseNature, 1989
- Purification of the cardiac Na+Ca2+ exchange proteinBiochimica et Biophysica Acta (BBA) - Biomembranes, 1988
- A new method for predicting signal sequence cleavage sitesNucleic Acids Research, 1986