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Molecular Studies of the Cardiac Sarcolemmal Sodium‐Calcium Exchanger
Author(s) -
NICOLL D. A.,
PHILIPSON K. D.
Publication year - 1991
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1991.tb17305.x
Subject(s) - annals , gerontology , medicine , library science , research center , center (category theory) , health science , history , archaeology , medical education , chemistry , pathology , computer science , crystallography
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.