Direct stimulation of Jak/STAT pathway by the angiotensin II AT1 receptor

Mario B Marrero, Bernhard Schieffer, William G. Paxton, Lauri Heerdt, Bradford C. Berk, Patrick Delafontaine, Kenneth E. Bernstein

Research output: Contribution to journalArticle

613 Citations (Scopus)

Abstract

THE peptide angiotensin II is the effector molecule of the renin-angiotensin system. All the haemodynamic effects of angiotensin II, including vasoconstriction and adrenal aldosterone release, are mediated through a single class of cell-surface receptors known as AT1 (refs 1, 2). These receptors contain the structural features of the G-protein-coupled receptor superfamily3. We show here that angiotensin II induces the rapid phosphorylation of tyrosine in the intracellular kinases Jak2 and Tyk2 in rat aortic smooth-muscle cells and that this phosphorylation is associated with increased activity of Jak2. The Jak family substrates STAT1 and STAT2 (for signal transducers and activators of transcription) are rapidly tyrosine-phosphorylated in response to angiotensin II. We also find that Jak2 co-precipitates with the AT1, receptor, indicating that G-protein-coupled receptors may be able to signal through the intracellular phosphorylation pathways used by cytokine receptors4,5.

Original languageEnglish (US)
Pages (from-to)247-250
Number of pages4
JournalNature
Volume375
Issue number6528
DOIs
StatePublished - May 18 1995

Fingerprint

Angiotensin Type 1 Receptor
Angiotensin Receptors
Angiotensin II
Phosphorylation
G-Protein-Coupled Receptors
Tyrosine
Cell Surface Receptors
Renin-Angiotensin System
Vasoconstriction
Aldosterone
Transducers
Smooth Muscle Myocytes
Phosphotransferases
Hemodynamics
Cytokines
Peptides

ASJC Scopus subject areas

  • General

Cite this

Marrero, M. B., Schieffer, B., Paxton, W. G., Heerdt, L., Berk, B. C., Delafontaine, P., & Bernstein, K. E. (1995). Direct stimulation of Jak/STAT pathway by the angiotensin II AT1 receptor. Nature, 375(6528), 247-250. https://doi.org/10.1038/375247a0

Direct stimulation of Jak/STAT pathway by the angiotensin II AT1 receptor. / Marrero, Mario B; Schieffer, Bernhard; Paxton, William G.; Heerdt, Lauri; Berk, Bradford C.; Delafontaine, Patrick; Bernstein, Kenneth E.

In: Nature, Vol. 375, No. 6528, 18.05.1995, p. 247-250.

Research output: Contribution to journalArticle

Marrero, MB, Schieffer, B, Paxton, WG, Heerdt, L, Berk, BC, Delafontaine, P & Bernstein, KE 1995, 'Direct stimulation of Jak/STAT pathway by the angiotensin II AT1 receptor', Nature, vol. 375, no. 6528, pp. 247-250. https://doi.org/10.1038/375247a0
Marrero MB, Schieffer B, Paxton WG, Heerdt L, Berk BC, Delafontaine P et al. Direct stimulation of Jak/STAT pathway by the angiotensin II AT1 receptor. Nature. 1995 May 18;375(6528):247-250. https://doi.org/10.1038/375247a0
Marrero, Mario B ; Schieffer, Bernhard ; Paxton, William G. ; Heerdt, Lauri ; Berk, Bradford C. ; Delafontaine, Patrick ; Bernstein, Kenneth E. / Direct stimulation of Jak/STAT pathway by the angiotensin II AT1 receptor. In: Nature. 1995 ; Vol. 375, No. 6528. pp. 247-250.
@article{de0943e0604c42829a32eefffe98713a,
title = "Direct stimulation of Jak/STAT pathway by the angiotensin II AT1 receptor",
abstract = "THE peptide angiotensin II is the effector molecule of the renin-angiotensin system. All the haemodynamic effects of angiotensin II, including vasoconstriction and adrenal aldosterone release, are mediated through a single class of cell-surface receptors known as AT1 (refs 1, 2). These receptors contain the structural features of the G-protein-coupled receptor superfamily3. We show here that angiotensin II induces the rapid phosphorylation of tyrosine in the intracellular kinases Jak2 and Tyk2 in rat aortic smooth-muscle cells and that this phosphorylation is associated with increased activity of Jak2. The Jak family substrates STAT1 and STAT2 (for signal transducers and activators of transcription) are rapidly tyrosine-phosphorylated in response to angiotensin II. We also find that Jak2 co-precipitates with the AT1, receptor, indicating that G-protein-coupled receptors may be able to signal through the intracellular phosphorylation pathways used by cytokine receptors4,5.",
author = "Marrero, {Mario B} and Bernhard Schieffer and Paxton, {William G.} and Lauri Heerdt and Berk, {Bradford C.} and Patrick Delafontaine and Bernstein, {Kenneth E.}",
year = "1995",
month = "5",
day = "18",
doi = "10.1038/375247a0",
language = "English (US)",
volume = "375",
pages = "247--250",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Publishing Group",
number = "6528",

}

TY - JOUR

T1 - Direct stimulation of Jak/STAT pathway by the angiotensin II AT1 receptor

AU - Marrero, Mario B

AU - Schieffer, Bernhard

AU - Paxton, William G.

AU - Heerdt, Lauri

AU - Berk, Bradford C.

AU - Delafontaine, Patrick

AU - Bernstein, Kenneth E.

PY - 1995/5/18

Y1 - 1995/5/18

N2 - THE peptide angiotensin II is the effector molecule of the renin-angiotensin system. All the haemodynamic effects of angiotensin II, including vasoconstriction and adrenal aldosterone release, are mediated through a single class of cell-surface receptors known as AT1 (refs 1, 2). These receptors contain the structural features of the G-protein-coupled receptor superfamily3. We show here that angiotensin II induces the rapid phosphorylation of tyrosine in the intracellular kinases Jak2 and Tyk2 in rat aortic smooth-muscle cells and that this phosphorylation is associated with increased activity of Jak2. The Jak family substrates STAT1 and STAT2 (for signal transducers and activators of transcription) are rapidly tyrosine-phosphorylated in response to angiotensin II. We also find that Jak2 co-precipitates with the AT1, receptor, indicating that G-protein-coupled receptors may be able to signal through the intracellular phosphorylation pathways used by cytokine receptors4,5.

AB - THE peptide angiotensin II is the effector molecule of the renin-angiotensin system. All the haemodynamic effects of angiotensin II, including vasoconstriction and adrenal aldosterone release, are mediated through a single class of cell-surface receptors known as AT1 (refs 1, 2). These receptors contain the structural features of the G-protein-coupled receptor superfamily3. We show here that angiotensin II induces the rapid phosphorylation of tyrosine in the intracellular kinases Jak2 and Tyk2 in rat aortic smooth-muscle cells and that this phosphorylation is associated with increased activity of Jak2. The Jak family substrates STAT1 and STAT2 (for signal transducers and activators of transcription) are rapidly tyrosine-phosphorylated in response to angiotensin II. We also find that Jak2 co-precipitates with the AT1, receptor, indicating that G-protein-coupled receptors may be able to signal through the intracellular phosphorylation pathways used by cytokine receptors4,5.

UR - http://www.scopus.com/inward/record.url?scp=0029019246&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029019246&partnerID=8YFLogxK

U2 - 10.1038/375247a0

DO - 10.1038/375247a0

M3 - Article

VL - 375

SP - 247

EP - 250

JO - Nature

JF - Nature

SN - 0028-0836

IS - 6528

ER -