Elevated K+ induces myristoylated alanine-rich C-kinase substrate phosphorylation and phospholipase D activation in glomerulosa cells

Soraya Betancourt-Calle, EunMi Jung, Stephanie White, Sagarika Ray, Xiangjian Zheng, Roberto A. Calle, Wendy B Bollag

Research output: Contribution to journalArticle

14 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)65-76
Number of pages12
JournalMolecular and Cellular Endocrinology
Volume184
Issue number1-2
DOIs
StatePublished - Nov 26 2001

Fingerprint

Phospholipase D
Phosphorylation
Chemical activation
Protein Kinase C
Zona Glomerulosa
Protein C Inhibitor
Depolarization
Calcium Channels
Protein Kinase Inhibitors
Phosphatidylinositols
Aldosterone
Angiotensin II
Hydrolysis
Potassium
myristoylated alanine-rich C kinase substrate
Calcium

Keywords

  • Aldosterone
  • Angiotensin II
  • Calcium channels
  • Protein kinase C

ASJC Scopus subject areas

  • Endocrinology
  • Endocrinology, Diabetes and Metabolism

Cite this

Elevated K+ induces myristoylated alanine-rich C-kinase substrate phosphorylation and phospholipase D activation in glomerulosa cells. / Betancourt-Calle, Soraya; Jung, EunMi; White, Stephanie; Ray, Sagarika; Zheng, Xiangjian; Calle, Roberto A.; Bollag, Wendy B.

In: Molecular and Cellular Endocrinology, Vol. 184, No. 1-2, 26.11.2001, p. 65-76.

Research output: Contribution to journalArticle

Betancourt-Calle, Soraya ; Jung, EunMi ; White, Stephanie ; Ray, Sagarika ; Zheng, Xiangjian ; Calle, Roberto A. ; Bollag, Wendy B. / Elevated K+ induces myristoylated alanine-rich C-kinase substrate phosphorylation and phospholipase D activation in glomerulosa cells. In: Molecular and Cellular Endocrinology. 2001 ; Vol. 184, No. 1-2. pp. 65-76.
@article{9181dab4f66b48f2bb84aeca4a223570,
title = "Elevated K+ induces myristoylated alanine-rich C-kinase substrate phosphorylation and phospholipase D activation in glomerulosa cells",
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.",
keywords = "Aldosterone, Angiotensin II, Calcium channels, Protein kinase C",
author = "Soraya Betancourt-Calle and EunMi Jung and Stephanie White and Sagarika Ray and Xiangjian Zheng and Calle, {Roberto A.} and Bollag, {Wendy B}",
year = "2001",
month = "11",
day = "26",
doi = "10.1016/S0303-7207(01)00642-6",
language = "English (US)",
volume = "184",
pages = "65--76",
journal = "Molecular and Cellular Endocrinology",
issn = "0303-7207",
publisher = "Elsevier Ireland Ltd",
number = "1-2",

}

TY - JOUR

T1 - Elevated K+ induces myristoylated alanine-rich C-kinase substrate phosphorylation and phospholipase D activation in glomerulosa cells

AU - Betancourt-Calle, Soraya

AU - Jung, EunMi

AU - White, Stephanie

AU - Ray, Sagarika

AU - Zheng, Xiangjian

AU - Calle, Roberto A.

AU - Bollag, Wendy B

PY - 2001/11/26

Y1 - 2001/11/26

N2 - 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.

AB - 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.

KW - Aldosterone

KW - Angiotensin II

KW - Calcium channels

KW - Protein kinase C

UR - http://www.scopus.com/inward/record.url?scp=0035955887&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035955887&partnerID=8YFLogxK

U2 - 10.1016/S0303-7207(01)00642-6

DO - 10.1016/S0303-7207(01)00642-6

M3 - Article

VL - 184

SP - 65

EP - 76

JO - Molecular and Cellular Endocrinology

JF - Molecular and Cellular Endocrinology

SN - 0303-7207

IS - 1-2

ER -