Tyrosine kinase is involved in angiotensin II-stimulated phospholipase D activation in aortic smooth muscle cells: Function of Ca2+ influx

Atsushi Suzuki, Junji Shinoda, Yutaka Oiso, Osamu Kozawa

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

In the present study, we examined the effect of angiotensin II (Ang II) on phosphatidylcholine-hydrolyzing phospholipase D activity in subcultured rat aortic smooth muscle cells (SMC). Ang II dose-dependently stimulated the formation of choline and inositol phosphates. The effect of Ang II on the formation of inositol phosphates (EC50 was 0.249 ± 0.091 nM) was more potent than that on the formation of choline (EC50 was 2.39 ± 1.29 nM). A combination of Ang II and 12-O-tetradecanoylphorbol-13-acetate (TPA), an activator of protein kinase C, additively stimulated the formation of choline. Staurosporine, an inhibitor of protein kinases, inhibited the TPA-induced formation of choline, but had little effect on the Ang II-induced choline formation. Ang II stimulated Ca2+ influx from extracellular space time- and dose-dependently. The depletion of extracellular Ca2+ by (ethylenebis(oxyethylenenitrilo))tetraacetic acid (EGTA) significantly reduced the Ang II-induced formation of choline. Genistein and tyrphostin, protein tyrosine kinase inhibitors, significantly suppressed the Ang II-induced Ca2+ influx. Genistein and tyrphostin also suppressed the Ang II-induced formation of choline. These results suggest that Ang II stimulates phosphatidylcholine-hydrolyzing phospholipase D due to Ca2+ influx from the extracellular space in rat aortic SMC, and that protein tyrosine kinase is involved in the Ang II-induced Ca2+ influx, resulting in the promotion of phosphatidylcholine hydrolysis.

Original languageEnglish
Pages (from-to)119-127
Number of pages9
JournalAtherosclerosis
Volume121
Issue number1
DOIs
Publication statusPublished - 01-03-1996
Externally publishedYes

Fingerprint

Phospholipase D
Angiotensin II
Protein-Tyrosine Kinases
Smooth Muscle Myocytes
Choline
Phosphatidylcholines
Tyrphostins
Inositol Phosphates
Genistein
Extracellular Space
Tetradecanoylphorbol Acetate
Protein Kinase Inhibitors
Staurosporine
Phosphorylcholine
Muscle Proteins
Egtazic Acid
Protein Kinase C
Hydrolysis

All Science Journal Classification (ASJC) codes

  • Cardiology and Cardiovascular Medicine

Cite this

@article{f8431ec2732d4ea39320f6be3d55f3ce,
title = "Tyrosine kinase is involved in angiotensin II-stimulated phospholipase D activation in aortic smooth muscle cells: Function of Ca2+ influx",
abstract = "In the present study, we examined the effect of angiotensin II (Ang II) on phosphatidylcholine-hydrolyzing phospholipase D activity in subcultured rat aortic smooth muscle cells (SMC). Ang II dose-dependently stimulated the formation of choline and inositol phosphates. The effect of Ang II on the formation of inositol phosphates (EC50 was 0.249 ± 0.091 nM) was more potent than that on the formation of choline (EC50 was 2.39 ± 1.29 nM). A combination of Ang II and 12-O-tetradecanoylphorbol-13-acetate (TPA), an activator of protein kinase C, additively stimulated the formation of choline. Staurosporine, an inhibitor of protein kinases, inhibited the TPA-induced formation of choline, but had little effect on the Ang II-induced choline formation. Ang II stimulated Ca2+ influx from extracellular space time- and dose-dependently. The depletion of extracellular Ca2+ by (ethylenebis(oxyethylenenitrilo))tetraacetic acid (EGTA) significantly reduced the Ang II-induced formation of choline. Genistein and tyrphostin, protein tyrosine kinase inhibitors, significantly suppressed the Ang II-induced Ca2+ influx. Genistein and tyrphostin also suppressed the Ang II-induced formation of choline. These results suggest that Ang II stimulates phosphatidylcholine-hydrolyzing phospholipase D due to Ca2+ influx from the extracellular space in rat aortic SMC, and that protein tyrosine kinase is involved in the Ang II-induced Ca2+ influx, resulting in the promotion of phosphatidylcholine hydrolysis.",
author = "Atsushi Suzuki and Junji Shinoda and Yutaka Oiso and Osamu Kozawa",
year = "1996",
month = "3",
day = "1",
doi = "10.1016/0021-9150(95)05708-0",
language = "English",
volume = "121",
pages = "119--127",
journal = "Atherosclerosis",
issn = "0021-9150",
publisher = "Elsevier Ireland Ltd",
number = "1",

}

Tyrosine kinase is involved in angiotensin II-stimulated phospholipase D activation in aortic smooth muscle cells : Function of Ca2+ influx. / Suzuki, Atsushi; Shinoda, Junji; Oiso, Yutaka; Kozawa, Osamu.

In: Atherosclerosis, Vol. 121, No. 1, 01.03.1996, p. 119-127.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Tyrosine kinase is involved in angiotensin II-stimulated phospholipase D activation in aortic smooth muscle cells

T2 - Function of Ca2+ influx

AU - Suzuki, Atsushi

AU - Shinoda, Junji

AU - Oiso, Yutaka

AU - Kozawa, Osamu

PY - 1996/3/1

Y1 - 1996/3/1

N2 - In the present study, we examined the effect of angiotensin II (Ang II) on phosphatidylcholine-hydrolyzing phospholipase D activity in subcultured rat aortic smooth muscle cells (SMC). Ang II dose-dependently stimulated the formation of choline and inositol phosphates. The effect of Ang II on the formation of inositol phosphates (EC50 was 0.249 ± 0.091 nM) was more potent than that on the formation of choline (EC50 was 2.39 ± 1.29 nM). A combination of Ang II and 12-O-tetradecanoylphorbol-13-acetate (TPA), an activator of protein kinase C, additively stimulated the formation of choline. Staurosporine, an inhibitor of protein kinases, inhibited the TPA-induced formation of choline, but had little effect on the Ang II-induced choline formation. Ang II stimulated Ca2+ influx from extracellular space time- and dose-dependently. The depletion of extracellular Ca2+ by (ethylenebis(oxyethylenenitrilo))tetraacetic acid (EGTA) significantly reduced the Ang II-induced formation of choline. Genistein and tyrphostin, protein tyrosine kinase inhibitors, significantly suppressed the Ang II-induced Ca2+ influx. Genistein and tyrphostin also suppressed the Ang II-induced formation of choline. These results suggest that Ang II stimulates phosphatidylcholine-hydrolyzing phospholipase D due to Ca2+ influx from the extracellular space in rat aortic SMC, and that protein tyrosine kinase is involved in the Ang II-induced Ca2+ influx, resulting in the promotion of phosphatidylcholine hydrolysis.

AB - In the present study, we examined the effect of angiotensin II (Ang II) on phosphatidylcholine-hydrolyzing phospholipase D activity in subcultured rat aortic smooth muscle cells (SMC). Ang II dose-dependently stimulated the formation of choline and inositol phosphates. The effect of Ang II on the formation of inositol phosphates (EC50 was 0.249 ± 0.091 nM) was more potent than that on the formation of choline (EC50 was 2.39 ± 1.29 nM). A combination of Ang II and 12-O-tetradecanoylphorbol-13-acetate (TPA), an activator of protein kinase C, additively stimulated the formation of choline. Staurosporine, an inhibitor of protein kinases, inhibited the TPA-induced formation of choline, but had little effect on the Ang II-induced choline formation. Ang II stimulated Ca2+ influx from extracellular space time- and dose-dependently. The depletion of extracellular Ca2+ by (ethylenebis(oxyethylenenitrilo))tetraacetic acid (EGTA) significantly reduced the Ang II-induced formation of choline. Genistein and tyrphostin, protein tyrosine kinase inhibitors, significantly suppressed the Ang II-induced Ca2+ influx. Genistein and tyrphostin also suppressed the Ang II-induced formation of choline. These results suggest that Ang II stimulates phosphatidylcholine-hydrolyzing phospholipase D due to Ca2+ influx from the extracellular space in rat aortic SMC, and that protein tyrosine kinase is involved in the Ang II-induced Ca2+ influx, resulting in the promotion of phosphatidylcholine hydrolysis.

UR - http://www.scopus.com/inward/record.url?scp=0030025752&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030025752&partnerID=8YFLogxK

U2 - 10.1016/0021-9150(95)05708-0

DO - 10.1016/0021-9150(95)05708-0

M3 - Article

C2 - 8678916

AN - SCOPUS:0030025752

VL - 121

SP - 119

EP - 127

JO - Atherosclerosis

JF - Atherosclerosis

SN - 0021-9150

IS - 1

ER -