PortalPublikationenCalreticulin enhances B2 bradykinin receptor maturation and ...

Calreticulin enhances B2 bradykinin receptor maturation and heterodimerization.

Standard

Calreticulin enhances B2 bradykinin receptor maturation and heterodimerization. / Joshua, Abd Alla; Reeck, Kristin; Langer, Andreas; Streichert, Thomas; Quitterer, Ursula.

in: BIOCHEM BIOPH RES CO, Jahrgang 387, Nr. 1, 1, 2009, S. 186-190.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Joshua, AA, Reeck, K, Langer, A, Streichert, T & Quitterer, U 2009, 'Calreticulin enhances B2 bradykinin receptor maturation and heterodimerization.', BIOCHEM BIOPH RES CO, Jg. 387, Nr. 1, 1, S. 186-190. <http://www.ncbi.nlm.nih.gov/pubmed/19580784?dopt=Citation>

APA

Joshua, A. A., Reeck, K., Langer, A., Streichert, T., & Quitterer, U. (2009). Calreticulin enhances B2 bradykinin receptor maturation and heterodimerization. BIOCHEM BIOPH RES CO, 387(1), 186-190. [1]. http://www.ncbi.nlm.nih.gov/pubmed/19580784?dopt=Citation

Vancouver

Joshua AA, Reeck K, Langer A, Streichert T, Quitterer U. Calreticulin enhances B2 bradykinin receptor maturation and heterodimerization. BIOCHEM BIOPH RES CO. 2009;387(1):186-190. 1.

Bibtex

@article{f81766592a23436ab0a8534416e1087d,
title = "Calreticulin enhances B2 bradykinin receptor maturation and heterodimerization.",
abstract = "In different native tissues and cells the receptor for the vasodepressor bradykinin, B(2), forms dimers with the receptor for the vasopressor angiotensin II, AT(1). Because AT(1)/B(2) heterodimers may contribute to enhanced angiotensin II-stimulated signaling under pathophysiological conditions, we analyzed mechanisms of AT(1)/B(2) heterodimerization. We found that efficient B(2) receptor maturation was a prerequisite for heterodimerization because only the fully mature B(2) receptor was capable to interact with AT(1). To identify chaperones involved in B(2) receptor maturation and heterodimerization we performed microarray gene expression profiling of human embryonic kidney (HEK293) cells. The expression of the chaperone calreticulin was up-regulated in cells with efficient B(2) receptor maturation. Vice versa, upon down regulation of calreticulin expression by RNA interference, B(2) receptor maturation and AT(1)/B(2) receptor heterodimerization were significantly impaired. Concomitantly, the B(2) receptor-mediated enhancement of AT(1)-stimulated signaling was reduced. Thus, calreticulin enhances B(2) receptor maturation and heterodimerization with AT(1).",
author = "Joshua, {Abd Alla} and Kristin Reeck and Andreas Langer and Thomas Streichert and Ursula Quitterer",
year = "2009",
language = "Deutsch",
volume = "387",
pages = "186--190",
journal = "BIOCHEM BIOPH RES CO",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "1",

}

RIS

TY - JOUR

T1 - Calreticulin enhances B2 bradykinin receptor maturation and heterodimerization.

AU - Joshua, Abd Alla

AU - Reeck, Kristin

AU - Langer, Andreas

AU - Streichert, Thomas

AU - Quitterer, Ursula

PY - 2009

Y1 - 2009

N2 - In different native tissues and cells the receptor for the vasodepressor bradykinin, B(2), forms dimers with the receptor for the vasopressor angiotensin II, AT(1). Because AT(1)/B(2) heterodimers may contribute to enhanced angiotensin II-stimulated signaling under pathophysiological conditions, we analyzed mechanisms of AT(1)/B(2) heterodimerization. We found that efficient B(2) receptor maturation was a prerequisite for heterodimerization because only the fully mature B(2) receptor was capable to interact with AT(1). To identify chaperones involved in B(2) receptor maturation and heterodimerization we performed microarray gene expression profiling of human embryonic kidney (HEK293) cells. The expression of the chaperone calreticulin was up-regulated in cells with efficient B(2) receptor maturation. Vice versa, upon down regulation of calreticulin expression by RNA interference, B(2) receptor maturation and AT(1)/B(2) receptor heterodimerization were significantly impaired. Concomitantly, the B(2) receptor-mediated enhancement of AT(1)-stimulated signaling was reduced. Thus, calreticulin enhances B(2) receptor maturation and heterodimerization with AT(1).

AB - In different native tissues and cells the receptor for the vasodepressor bradykinin, B(2), forms dimers with the receptor for the vasopressor angiotensin II, AT(1). Because AT(1)/B(2) heterodimers may contribute to enhanced angiotensin II-stimulated signaling under pathophysiological conditions, we analyzed mechanisms of AT(1)/B(2) heterodimerization. We found that efficient B(2) receptor maturation was a prerequisite for heterodimerization because only the fully mature B(2) receptor was capable to interact with AT(1). To identify chaperones involved in B(2) receptor maturation and heterodimerization we performed microarray gene expression profiling of human embryonic kidney (HEK293) cells. The expression of the chaperone calreticulin was up-regulated in cells with efficient B(2) receptor maturation. Vice versa, upon down regulation of calreticulin expression by RNA interference, B(2) receptor maturation and AT(1)/B(2) receptor heterodimerization were significantly impaired. Concomitantly, the B(2) receptor-mediated enhancement of AT(1)-stimulated signaling was reduced. Thus, calreticulin enhances B(2) receptor maturation and heterodimerization with AT(1).

M3 - SCORING: Zeitschriftenaufsatz

VL - 387

SP - 186

EP - 190

JO - BIOCHEM BIOPH RES CO

JF - BIOCHEM BIOPH RES CO

SN - 0006-291X

IS - 1

M1 - 1

ER -