Abstract
Elevated extracellular potassium concentrations ([K+]e) are known to stimulate aldosterone secretion from adrenal glomerulosa cells in vivo and in vitro. The mechanism is thought to involve depolarization-elicited activation of voltage-dependent calcium channels and an increase in calcium influx. Until now protein kinase C (PKC) was thought not to play a role in the steroidogenic response to elevated [K+]e. In this report, we provide evidence in bovine adrenal glomerulosa cells to suggest that elevated [K+]e increases PKC activity, as shown by an enhancement in the phosphorylation of myristoylated alanine-rich C-kinase substrate (MARCKS). Elevated [K+]e-induced MARCKS phosphorylation was delayed and transient and was not the result of a local production of angiotensin II (AngII). MARCKS phosphorylation in response to elevated [K+]e was not accompanied by phosphoinositide hydrolysis but was inhibited by a selective PKC inhibitor. Elevated [K+]e also activated phospholipase D (PLD) in a delayed but sustained manner. We propose that the observed PLD activation mediates the elevated [K+]e-induced MARCKS phosphorylation via PKC, although other factors may modulate this phosphorylation event.
Original language | English (US) |
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Pages (from-to) | 65-76 |
Number of pages | 12 |
Journal | Molecular and Cellular Endocrinology |
Volume | 184 |
Issue number | 1-2 |
DOIs | |
State | Published - Nov 26 2001 |
Keywords
- Aldosterone
- Angiotensin II
- Calcium channels
- Protein kinase C
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Endocrinology