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This Article Accepted manuscript (PDF) All Versions of this Article: JOE-09-0119v1 202/1/77    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Qin, H. Articles by Bollag, W. Search for Related Content PubMed PubMed Citation Articles by Qin, H. Articles by Bollag, W.

H Qin, Institute of Molecular Medicine and Genetics, Medical College of Georgia, Augusta, United States
P Kent, Institute of Molecular Medicine and Genetics, Medical College of Georgia, Augusta, United States
C Isales, Institute of Molecular Medicine and Genetics, Medical College of Georgia, Augusta, United States
P Parker, Institute of Molecular Medicine and Genetics, Medical College of Georgia, Augusta, United States
M Wilson, Institute of Molecular Medicine and Genetics, Medical College of Georgia, Augusta, United States
W Bollag, Inst. of Mol. Med. & Genetics, Medical College of Georgia, Augusta, 30912, United States

Correspondence: Wendy Bollag, Email: wbollag{at}mail.mcg.edu

The steroid hormone aldosterone maintains sodium homeostasis and is therefore important in control of blood volume and pressure. Angiotensin II (AngII) and elevated extracellular potassium concentrations ([K+4]e), the prime physiologic regulators of aldosterone secretion from adrenal glomerulosa cells, activate phospholipase D (PLD) in these cells. The role of Ca2+ in the activation by these agents, is unknown, although nitrendipine, a voltage-dependent Ca2+ channel antagonist, does not inhibit AngII-elicited PLD activation, despite the fact that this compound blocked elevated ([K+4]e) -stimulated PLD activity. PLD activation triggered by AngII was also unaffected by the T-type calcium channel inhibitor nickel. Nevertheless, Ca2+ influx was also required for AngII-induced PLD activation in both primary cultures of bovine adrenal glomerulosa cells and a glomerulosa cell model, the NCI H295R adrenocortical carcinoma cell line. The involvement of store-operated Ca2+ (SOC) influx and Ca2+ release-activated Ca2+ (CRAC) influx pathways in PLD activation was investigated using thapsigargin, an endoplasmic reticulum Ca2+ pump inhibitor that empties the store to induce SOC influx, and the SOC inhibitor YM-58483 (BTP2), as well as a CRAC inhibitor, tyrphostin A9. In bovine glomerulosa cells tyrphostin A9 inhibited AngII-induced PLD activation without affecting elevated [([K+4]e) -stimulated enzyme activity. On the other hand, differences were observed between the bovine adrenal glomerulosa and H295R cells in the involvement of Ca2+ influx in PLD activation, with the involvement of the SOC pathway suggested in the H295R cells. In summary, our results indicate that Ca2+ entry only through certain Ca2+ influx pathways is linked to PLD activation.