Effects of angiotensin II and adrenocorticotropic hormone on myristoylated alanine-rich C-kinase substrate phosphorylation in glomerulosa cells

S. Betancourt-Calle, W. B. Bollag, E. M. Jung, R. A. Calle, H. Rasmussen

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

Angiotensin II (AngII) is thought to stimulate aldosterone secretion from bovine adrenal glomerulosa cells in part via activation of protein kinase C (PKC), while adrenocorticotropic hormone (ACTH) functions through increases in intracellular cAMP levels and calcium influx. Rather than using invasive homogenization techniques as in previous studies, we chose to monitor PKC activity in intact glomerulosa cells in situ by measuring the phosphorylation of the endogenous PKC substrate, myristoylated alanine-rich C-kinase substrate (MARCKS). AngII enhanced MARCKS phosphorylation in a rapid, sustained manner; whereas ACTH induced a rapid and sustained inhibition of MARCKS phosphorylation. Studies using pharmacological agents to mimic various signals indicated that the AngII-induced MARCKS phosphorylation was due to PKC activation, and the ACTH-elicited decrease was mediated by increases in calcium influx rather than cAMP production. We propose that changes in the phosphorylation state of MARCKS, an actin-binding protein, may contribute to cytoskeletal rearrangements involved in steroidogenesis. Copyright (C) 1999 Elsevier Science Ireland Ltd.

Original languageEnglish (US)
Pages (from-to)1-9
Number of pages9
JournalMolecular and Cellular Endocrinology
Volume154
Issue number1-2
DOIs
StatePublished - Aug 20 1999

Fingerprint

Phosphorylation
Angiotensin II
Adrenocorticotropic Hormone
Protein Kinase C
Chemical activation
Calcium
Zona Glomerulosa
Microfilament Proteins
Aldosterone
myristoylated alanine-rich C kinase substrate
Pharmacology
Substrates

Keywords

  • ACTH
  • Aldosterone secretion
  • Angiotensin II
  • Bovine adrenal
  • MARCKS
  • Protein kinase C

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Endocrinology

Cite this

Effects of angiotensin II and adrenocorticotropic hormone on myristoylated alanine-rich C-kinase substrate phosphorylation in glomerulosa cells. / Betancourt-Calle, S.; Bollag, W. B.; Jung, E. M.; Calle, R. A.; Rasmussen, H.

In: Molecular and Cellular Endocrinology, Vol. 154, No. 1-2, 20.08.1999, p. 1-9.

Research output: Contribution to journalArticle

@article{7d4a064fc6c144a0864d92815fc80e2f,
title = "Effects of angiotensin II and adrenocorticotropic hormone on myristoylated alanine-rich C-kinase substrate phosphorylation in glomerulosa cells",
abstract = "Angiotensin II (AngII) is thought to stimulate aldosterone secretion from bovine adrenal glomerulosa cells in part via activation of protein kinase C (PKC), while adrenocorticotropic hormone (ACTH) functions through increases in intracellular cAMP levels and calcium influx. Rather than using invasive homogenization techniques as in previous studies, we chose to monitor PKC activity in intact glomerulosa cells in situ by measuring the phosphorylation of the endogenous PKC substrate, myristoylated alanine-rich C-kinase substrate (MARCKS). AngII enhanced MARCKS phosphorylation in a rapid, sustained manner; whereas ACTH induced a rapid and sustained inhibition of MARCKS phosphorylation. Studies using pharmacological agents to mimic various signals indicated that the AngII-induced MARCKS phosphorylation was due to PKC activation, and the ACTH-elicited decrease was mediated by increases in calcium influx rather than cAMP production. We propose that changes in the phosphorylation state of MARCKS, an actin-binding protein, may contribute to cytoskeletal rearrangements involved in steroidogenesis. Copyright (C) 1999 Elsevier Science Ireland Ltd.",
keywords = "ACTH, Aldosterone secretion, Angiotensin II, Bovine adrenal, MARCKS, Protein kinase C",
author = "S. Betancourt-Calle and Bollag, {W. B.} and Jung, {E. M.} and Calle, {R. A.} and H. Rasmussen",
year = "1999",
month = "8",
day = "20",
doi = "10.1016/S0303-7207(99)00111-2",
language = "English (US)",
volume = "154",
pages = "1--9",
journal = "Molecular and Cellular Endocrinology",
issn = "0303-7207",
publisher = "Elsevier Ireland Ltd",
number = "1-2",

}

TY - JOUR

T1 - Effects of angiotensin II and adrenocorticotropic hormone on myristoylated alanine-rich C-kinase substrate phosphorylation in glomerulosa cells

AU - Betancourt-Calle, S.

AU - Bollag, W. B.

AU - Jung, E. M.

AU - Calle, R. A.

AU - Rasmussen, H.

PY - 1999/8/20

Y1 - 1999/8/20

N2 - Angiotensin II (AngII) is thought to stimulate aldosterone secretion from bovine adrenal glomerulosa cells in part via activation of protein kinase C (PKC), while adrenocorticotropic hormone (ACTH) functions through increases in intracellular cAMP levels and calcium influx. Rather than using invasive homogenization techniques as in previous studies, we chose to monitor PKC activity in intact glomerulosa cells in situ by measuring the phosphorylation of the endogenous PKC substrate, myristoylated alanine-rich C-kinase substrate (MARCKS). AngII enhanced MARCKS phosphorylation in a rapid, sustained manner; whereas ACTH induced a rapid and sustained inhibition of MARCKS phosphorylation. Studies using pharmacological agents to mimic various signals indicated that the AngII-induced MARCKS phosphorylation was due to PKC activation, and the ACTH-elicited decrease was mediated by increases in calcium influx rather than cAMP production. We propose that changes in the phosphorylation state of MARCKS, an actin-binding protein, may contribute to cytoskeletal rearrangements involved in steroidogenesis. Copyright (C) 1999 Elsevier Science Ireland Ltd.

AB - Angiotensin II (AngII) is thought to stimulate aldosterone secretion from bovine adrenal glomerulosa cells in part via activation of protein kinase C (PKC), while adrenocorticotropic hormone (ACTH) functions through increases in intracellular cAMP levels and calcium influx. Rather than using invasive homogenization techniques as in previous studies, we chose to monitor PKC activity in intact glomerulosa cells in situ by measuring the phosphorylation of the endogenous PKC substrate, myristoylated alanine-rich C-kinase substrate (MARCKS). AngII enhanced MARCKS phosphorylation in a rapid, sustained manner; whereas ACTH induced a rapid and sustained inhibition of MARCKS phosphorylation. Studies using pharmacological agents to mimic various signals indicated that the AngII-induced MARCKS phosphorylation was due to PKC activation, and the ACTH-elicited decrease was mediated by increases in calcium influx rather than cAMP production. We propose that changes in the phosphorylation state of MARCKS, an actin-binding protein, may contribute to cytoskeletal rearrangements involved in steroidogenesis. Copyright (C) 1999 Elsevier Science Ireland Ltd.

KW - ACTH

KW - Aldosterone secretion

KW - Angiotensin II

KW - Bovine adrenal

KW - MARCKS

KW - Protein kinase C

UR - http://www.scopus.com/inward/record.url?scp=0032782502&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032782502&partnerID=8YFLogxK

U2 - 10.1016/S0303-7207(99)00111-2

DO - 10.1016/S0303-7207(99)00111-2

M3 - Article

C2 - 10509794

AN - SCOPUS:0032782502

VL - 154

SP - 1

EP - 9

JO - Molecular and Cellular Endocrinology

JF - Molecular and Cellular Endocrinology

SN - 0303-7207

IS - 1-2

ER -