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J. Biol. Chem., Vol. 263, Issue 17, 8078-8083, Jun, 1988
P Vigne, JP Breittmayer, D Duval, C Frelin and M Lazdunski
The Na+/Ca2+ antiporter is present in aortic smooth muscle cells of the
A7r5 cell line. Imposing an outward Na+ gradient to the cells promoted a
45Ca2+ uptake component which was sensitive to amiloride derivatives and
insensitive to blockers of the voltage-dependent Ca2+ channel. The Ca2+
uptake system was dependent on intracellular Na+ concentration; it was
inactive when Li+ replaced intracellular Na+ and it was electrogenic. Flow
cytometric analysis of cells that had been loaded with the Ca2+ indicator
indo-1 showed that all conditions that promoted Ca2+ influx led to
corresponding increases in the free cytoplasmic Ca2+ concentration.
Treatment of the A7r5 cells with phorbol myristate acetate, a known
activator of protein kinase C (Ca2+/phospholipid- dependent enzyme), led to
a two-fold activation of the system and to larger intracellular Ca2+
transients when cells were shifted to Na+- free solutions. Activation was
observed at all intracellular Na+ concentrations. Changing the activity of
the Na+/Ca2+ system did not affect the size and duration of intracellular
Ca2+ transients elicited by the Ca2+ mobilizing hormone vasopressin. It is
concluded that the Na+/Ca2+ antiporter in smooth muscle cells is a target
for protein kinase C but that the system is not involved in the regulation
of Ca2+ transients induced by vasopressin.
The Na+/Ca2+ antiporter in aortic smooth muscle cells. Characterization and demonstration of an activation by phorbol esters
Centre de Biochimie du Centre National de La Recherche Scientifique, Parc Valrose, Nice, France.
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