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Am J Physiol Renal Physiol 279: F170-F176, 2000;
0363-6127/00 $5.00
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Vol. 279, Issue 1, F170-F176, July 2000

Store-operated calcium influx inhibits renin secretion

Frank Schweda1, Günter A. J. Riegger2, Armin Kurtz1, and Bernhard K. Krämer2

1 Institut für Physiologie I and 2 Klinik und Poliklinik für Innere Medizin II, Universität Regensburg, D-93040 Regensburg, Germany

On the basis of evidence that changes in the extracellular concentration of calcium effectively modulate renin secretion from renal juxtaglomerular cells, our study aimed to determine the effect of calcium influx activated by depletion of intracellular calcium stores on renin secretion. For this purpose we characterized the effects of the endoplasmatic Ca2+-ATPase inhibitors thapsigargin (300 nM) and cyclopiazonic acid (20 µM) on renin secretion from isolated perfused rat kidneys. We found that Ca2+-ATPase inhibition caused a potent inhibition of basal renin secretion as well as renin secretion activated by isoproterenol, bumetanide, and by a fall in the renal perfusion pressure. The inhibitory effect of Ca2+-ATPase inhibition on renin secretion was reversed within seconds by lowering of the extracellular calcium concentration into the submicromolar range but was not affected by lanthanum, gadolinium, flufenamic acid, or amlodipine. These data suggest that calcium influx triggered by release of calcium from internal stores is a powerful mechanism to inhibit renin secretion from juxtaglomerular cells. The store-triggered calcium influx pathway in juxtaglomerular cells is apparently not sensitive to classic blockers of the capacitative calcium entry pathway.

thapsigargin; cyclopiazonic acid; endoplasmatic calcium-adenosinetriphosphatase; isolated perfused rat kidney


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