TY - JOUR
T1 - Angiotensin II priming of aldosterone secretion with agents that enhance Ca2+ influx
AU - Betancourt-Calle, Soraya
AU - Mann-Blakeney, Ra Shawn
AU - Isales, Carlos M.
AU - Calle, Roberto A.
AU - Bollinger Bollag, Wendy
N1 - Funding Information:
We gratefully acknowlege Dr Roni Bollag for his analysis of the bovine StAR sequence, EunMi Jung for her expert technical assistance and William Brown for his aid in obtaining adrenal glands. This work was supported by an American Heart Association/Southeast Affiliate Grant-in-Aid (to WBB), a Veteran's Administration Merit Review Award (to RAC) and a National Institutes of Health grant DK19813-22 (CMI). Portions of the data in this paper are from a thesis submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy in the Department of Cellular Biology and Anatomy, Medical College of Georgia (SB-C). This work has been presented in part at the 80th Annual Meeting of the Endocrine Society, June, 1998 in New Orleans, LA.
PY - 2001/5/25
Y1 - 2001/5/25
N2 - We have previously shown that angiotensin II (AngII) is able to prime, or sensitize, the secretory response of cultured bovine adrenal glomerulosa cells to the Ca2+ channel agonist, BAY K8644. We examined the ability of AngII to prime glomerulosa cells to an elevated extracellular K+ level, a physiological agonist that also triggers Ca2+ influx. K+ (9 mM) elicited enhanced secretion in AngII-primed cells compared to those with no prior exposure to the hormone, suggesting that AngII can sensitize glomerulosa cells to respond to increases in extracellular K+. The potential involvement of protein kinase C (PKC) in priming was investigated by determining whether enhanced Ca2+ influx could maintain the AngII-induced phosphorylation of the endogenous PKC substrate, myristoylated, alanine-rich C kinase substrate (MARCKS). Incubation with the AngII antagonist, saralasin, for 30 min following an AngII exposure reduced the AngII-induced increase in MARCKS phosphorylation. 100 nM BAY K8644 together with saralasin was unable to maintain AngII-stimulated MARCKS phosphorylation. On the other hand, phosphorylation of the steroidogenic acute regulatory (StAR) protein was sustained with saralasin exposure, both in the presence and absence of BAY K8644. This observation suggests that persistent StAR phosphorylation/activation may play a role in priming.
AB - We have previously shown that angiotensin II (AngII) is able to prime, or sensitize, the secretory response of cultured bovine adrenal glomerulosa cells to the Ca2+ channel agonist, BAY K8644. We examined the ability of AngII to prime glomerulosa cells to an elevated extracellular K+ level, a physiological agonist that also triggers Ca2+ influx. K+ (9 mM) elicited enhanced secretion in AngII-primed cells compared to those with no prior exposure to the hormone, suggesting that AngII can sensitize glomerulosa cells to respond to increases in extracellular K+. The potential involvement of protein kinase C (PKC) in priming was investigated by determining whether enhanced Ca2+ influx could maintain the AngII-induced phosphorylation of the endogenous PKC substrate, myristoylated, alanine-rich C kinase substrate (MARCKS). Incubation with the AngII antagonist, saralasin, for 30 min following an AngII exposure reduced the AngII-induced increase in MARCKS phosphorylation. 100 nM BAY K8644 together with saralasin was unable to maintain AngII-stimulated MARCKS phosphorylation. On the other hand, phosphorylation of the steroidogenic acute regulatory (StAR) protein was sustained with saralasin exposure, both in the presence and absence of BAY K8644. This observation suggests that persistent StAR phosphorylation/activation may play a role in priming.
KW - Adrenal glomerulosa
KW - Angiotensin II
KW - MARCKS
KW - Phosphorylation
KW - Protein kinase C
KW - StAR
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U2 - 10.1016/S0303-7207(01)00421-X
DO - 10.1016/S0303-7207(01)00421-X
M3 - Article
C2 - 11377821
AN - SCOPUS:0035947063
SN - 0303-7207
VL - 177
SP - 61
EP - 70
JO - Molecular and Cellular Endocrinology
JF - Molecular and Cellular Endocrinology
IS - 1-2
ER -