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Biased signaling of the angiotensin II type 1 receptor can be mediated through distinct mechanisms

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Standard

Biased signaling of the angiotensin II type 1 receptor can be mediated through distinct mechanisms. / Bonde, Marie Mi; Hansen, Jonas Tind; Sanni, Samra Joke; Gammeltoft, Steen; Haunsø, Stig; Lyngsø, Christina; Hansen, Jakob Lerche.

I: P L o S One, Bind 5, Nr. 11, 01.01.2010, s. e14135.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Bonde, MM, Hansen, JT, Sanni, SJ, Gammeltoft, S, Haunsø, S, Lyngsø, C & Hansen, JL 2010, 'Biased signaling of the angiotensin II type 1 receptor can be mediated through distinct mechanisms', P L o S One, bind 5, nr. 11, s. e14135. https://doi.org/10.1371/journal.pone.0014135

APA

Bonde, M. M., Hansen, J. T., Sanni, S. J., Gammeltoft, S., Haunsø, S., Lyngsø, C., & Hansen, J. L. (2010). Biased signaling of the angiotensin II type 1 receptor can be mediated through distinct mechanisms. P L o S One, 5(11), e14135. https://doi.org/10.1371/journal.pone.0014135

Vancouver

Bonde MM, Hansen JT, Sanni SJ, Gammeltoft S, Haunsø S, Lyngsø C o.a. Biased signaling of the angiotensin II type 1 receptor can be mediated through distinct mechanisms. P L o S One. 2010 jan 1;5(11):e14135. https://doi.org/10.1371/journal.pone.0014135

Author

Bonde, Marie Mi ; Hansen, Jonas Tind ; Sanni, Samra Joke ; Gammeltoft, Steen ; Haunsø, Stig ; Lyngsø, Christina ; Hansen, Jakob Lerche. / Biased signaling of the angiotensin II type 1 receptor can be mediated through distinct mechanisms. I: P L o S One. 2010 ; Bind 5, Nr. 11. s. e14135.

Bibtex

@article{c318915eb4314a8f82594a4f3e7d4780,
title = "Biased signaling of the angiotensin II type 1 receptor can be mediated through distinct mechanisms",
abstract = "Seven transmembrane receptors (7TMRs) can adopt different active conformations facilitating a selective activation of either G protein or {\ss}-arrestin-dependent signaling pathways. This represents an opportunity for development of novel therapeutics targeting selective biological effects of a given receptor. Several studies on pathway separation have been performed, many of these on the Angiotensin II type 1 receptor (AT1R). It has been shown that certain ligands or mutations facilitate internalization and/or recruitment of {\ss}-arrestins without activation of G proteins. However, the underlying molecular mechanisms remain largely unresolved. For instance, it is unclear whether such selective G protein-uncoupling is caused by a lack of ability to interact with G proteins or rather by an increased ability of the receptor to recruit {\ss}-arrestins. Since uncoupling of G proteins by increased ability to recruit {\ss}-arrestins could lead to different cellular or in vivo outcomes than lack of ability to interact with G proteins, it is essential to distinguish between these two mechanisms.",
author = "Bonde, {Marie Mi} and Hansen, {Jonas Tind} and Sanni, {Samra Joke} and Steen Gammeltoft and Stig Hauns{\o} and Christina Lyngs{\o} and Hansen, {Jakob Lerche}",
year = "2010",
month = jan,
day = "1",
doi = "http://dx.doi.org/10.1371/journal.pone.0014135",
language = "English",
volume = "5",
pages = "e14135",
journal = "P L o S One",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "11",

}

RIS

TY - JOUR

T1 - Biased signaling of the angiotensin II type 1 receptor can be mediated through distinct mechanisms

AU - Bonde, Marie Mi

AU - Hansen, Jonas Tind

AU - Sanni, Samra Joke

AU - Gammeltoft, Steen

AU - Haunsø, Stig

AU - Lyngsø, Christina

AU - Hansen, Jakob Lerche

PY - 2010/1/1

Y1 - 2010/1/1

N2 - Seven transmembrane receptors (7TMRs) can adopt different active conformations facilitating a selective activation of either G protein or ß-arrestin-dependent signaling pathways. This represents an opportunity for development of novel therapeutics targeting selective biological effects of a given receptor. Several studies on pathway separation have been performed, many of these on the Angiotensin II type 1 receptor (AT1R). It has been shown that certain ligands or mutations facilitate internalization and/or recruitment of ß-arrestins without activation of G proteins. However, the underlying molecular mechanisms remain largely unresolved. For instance, it is unclear whether such selective G protein-uncoupling is caused by a lack of ability to interact with G proteins or rather by an increased ability of the receptor to recruit ß-arrestins. Since uncoupling of G proteins by increased ability to recruit ß-arrestins could lead to different cellular or in vivo outcomes than lack of ability to interact with G proteins, it is essential to distinguish between these two mechanisms.

AB - Seven transmembrane receptors (7TMRs) can adopt different active conformations facilitating a selective activation of either G protein or ß-arrestin-dependent signaling pathways. This represents an opportunity for development of novel therapeutics targeting selective biological effects of a given receptor. Several studies on pathway separation have been performed, many of these on the Angiotensin II type 1 receptor (AT1R). It has been shown that certain ligands or mutations facilitate internalization and/or recruitment of ß-arrestins without activation of G proteins. However, the underlying molecular mechanisms remain largely unresolved. For instance, it is unclear whether such selective G protein-uncoupling is caused by a lack of ability to interact with G proteins or rather by an increased ability of the receptor to recruit ß-arrestins. Since uncoupling of G proteins by increased ability to recruit ß-arrestins could lead to different cellular or in vivo outcomes than lack of ability to interact with G proteins, it is essential to distinguish between these two mechanisms.

U2 - http://dx.doi.org/10.1371/journal.pone.0014135

DO - http://dx.doi.org/10.1371/journal.pone.0014135

M3 - Journal article

VL - 5

SP - e14135

JO - P L o S One

JF - P L o S One

SN - 1932-6203

IS - 11

ER -

ID: 34168040