Role of intracellular calcium in the angiotensin II-mediated tyrosine phosphorylation and dephosphorylation of PLC-γl

J. B. Harp; P. P. Sayeski; M. Scanlon; K. E. Bernstein; M. B. Marrero

doi:10.1006/bbrc.1997.6322

Role of intracellular calcium in the angiotensin II-mediated tyrosine phosphorylation and dephosphorylation of PLC-γl

J. B. Harp, P. P. Sayeski, M. Scanlon, K. E. Bernstein, M. B. Marrero

Graduate Studies

Research output: Contribution to journal › Article › peer-review

5 Scopus citations

Abstract

Angiotensin II induces the rapid temporal tyrosine phosphorylation and activation of phospholipase C-γ1 (PLC-γl) and the elevation of intracellular calcium levels. To investigate the relationship of these intracellular signaling events, rat aortic smooth muscle cells were treated with the calcium chelator BAPTA-AM, the calcium channel blocker verapamil, the intracellular calcium antagonist TMB-8, and the calcium ionophore ionomycin. The effects of these agents on PLC-γl tyrosine phosphorylation were then measured. We found that treatment of these cells with the calcium inhibitors augmented the basal level of PLC-γl tyrosine phosphorylation, without changing the peak level of tyrosine phosphorylation induced by angiotensin II. The rapid dephosphorylation of PLC-γ1 that follows angiotensin II stimulation was prevented by these calcium antagonists. In contrast, angiotensin II-induced tyrosine phosphorylation of PLC-γl was inhibited by ionomycin. These results suggest that the angiotensin II-induced tyrosine phosphorylation of PLC-γ1 is calcium-independent, while the dephosphorylation is calcium-dependent.

Original language	English (US)
Pages (from-to)	540-544
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	232
Issue number	2
DOIs	https://doi.org/10.1006/bbrc.1997.6322
State	Published - Mar 17 1997

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1006/bbrc.1997.6322

Cite this

@article{d3079b36a1ba4fa49f11af4cb0d28135,

title = "Role of intracellular calcium in the angiotensin II-mediated tyrosine phosphorylation and dephosphorylation of PLC-γl",

abstract = "Angiotensin II induces the rapid temporal tyrosine phosphorylation and activation of phospholipase C-γ1 (PLC-γl) and the elevation of intracellular calcium levels. To investigate the relationship of these intracellular signaling events, rat aortic smooth muscle cells were treated with the calcium chelator BAPTA-AM, the calcium channel blocker verapamil, the intracellular calcium antagonist TMB-8, and the calcium ionophore ionomycin. The effects of these agents on PLC-γl tyrosine phosphorylation were then measured. We found that treatment of these cells with the calcium inhibitors augmented the basal level of PLC-γl tyrosine phosphorylation, without changing the peak level of tyrosine phosphorylation induced by angiotensin II. The rapid dephosphorylation of PLC-γ1 that follows angiotensin II stimulation was prevented by these calcium antagonists. In contrast, angiotensin II-induced tyrosine phosphorylation of PLC-γl was inhibited by ionomycin. These results suggest that the angiotensin II-induced tyrosine phosphorylation of PLC-γ1 is calcium-independent, while the dephosphorylation is calcium-dependent.",

author = "Harp, {J. B.} and Sayeski, {P. P.} and M. Scanlon and Bernstein, {K. E.} and Marrero, {M. B.}",

note = "Funding Information: This study was supported by grants from the National Institutes of Health, DK44280, DK45215, and DK39777. Dr. Marrero is a Minority Developmental Award Investigator from the American Heart Association. We are grateful to Dr. Brian Ling for his review of the manuscript and helpful comments.",

year = "1997",

month = mar,

day = "17",

doi = "10.1006/bbrc.1997.6322",

language = "English (US)",

volume = "232",

pages = "540--544",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "2",

}

TY - JOUR

T1 - Role of intracellular calcium in the angiotensin II-mediated tyrosine phosphorylation and dephosphorylation of PLC-γl

AU - Harp, J. B.

AU - Sayeski, P. P.

AU - Scanlon, M.

AU - Bernstein, K. E.

AU - Marrero, M. B.

N1 - Funding Information: This study was supported by grants from the National Institutes of Health, DK44280, DK45215, and DK39777. Dr. Marrero is a Minority Developmental Award Investigator from the American Heart Association. We are grateful to Dr. Brian Ling for his review of the manuscript and helpful comments.

PY - 1997/3/17

Y1 - 1997/3/17

N2 - Angiotensin II induces the rapid temporal tyrosine phosphorylation and activation of phospholipase C-γ1 (PLC-γl) and the elevation of intracellular calcium levels. To investigate the relationship of these intracellular signaling events, rat aortic smooth muscle cells were treated with the calcium chelator BAPTA-AM, the calcium channel blocker verapamil, the intracellular calcium antagonist TMB-8, and the calcium ionophore ionomycin. The effects of these agents on PLC-γl tyrosine phosphorylation were then measured. We found that treatment of these cells with the calcium inhibitors augmented the basal level of PLC-γl tyrosine phosphorylation, without changing the peak level of tyrosine phosphorylation induced by angiotensin II. The rapid dephosphorylation of PLC-γ1 that follows angiotensin II stimulation was prevented by these calcium antagonists. In contrast, angiotensin II-induced tyrosine phosphorylation of PLC-γl was inhibited by ionomycin. These results suggest that the angiotensin II-induced tyrosine phosphorylation of PLC-γ1 is calcium-independent, while the dephosphorylation is calcium-dependent.

AB - Angiotensin II induces the rapid temporal tyrosine phosphorylation and activation of phospholipase C-γ1 (PLC-γl) and the elevation of intracellular calcium levels. To investigate the relationship of these intracellular signaling events, rat aortic smooth muscle cells were treated with the calcium chelator BAPTA-AM, the calcium channel blocker verapamil, the intracellular calcium antagonist TMB-8, and the calcium ionophore ionomycin. The effects of these agents on PLC-γl tyrosine phosphorylation were then measured. We found that treatment of these cells with the calcium inhibitors augmented the basal level of PLC-γl tyrosine phosphorylation, without changing the peak level of tyrosine phosphorylation induced by angiotensin II. The rapid dephosphorylation of PLC-γ1 that follows angiotensin II stimulation was prevented by these calcium antagonists. In contrast, angiotensin II-induced tyrosine phosphorylation of PLC-γl was inhibited by ionomycin. These results suggest that the angiotensin II-induced tyrosine phosphorylation of PLC-γ1 is calcium-independent, while the dephosphorylation is calcium-dependent.

UR - http://www.scopus.com/inward/record.url?scp=0031575847&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031575847&partnerID=8YFLogxK

U2 - 10.1006/bbrc.1997.6322

DO - 10.1006/bbrc.1997.6322

M3 - Article

C2 - 9125218

AN - SCOPUS:0031575847

SN - 0006-291X

VL - 232

SP - 540

EP - 544

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 2

ER -

Role of intracellular calcium in the angiotensin II-mediated tyrosine phosphorylation and dephosphorylation of PLC-γl

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this