Abstract P099: Angiotensin Type I Receptor (AT1R) and (Pro)renin Receptor (PRR) Functional Heterodimer Mediates ERK Phosphorylation

Abstract only Receptor dimerization was shown to enhance the receptor efficacy, trafficking and signal transduction. Angiotensin II type 1 receptor (AT1R) and (Pro)renin receptor (PRR) are expressed in the kidney. Studies demonstrated that these two receptors have some similarities in their signalin...

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Published in:Hypertension (Dallas, Tex. 1979) Tex. 1979), 2015-09, Vol.66 (suppl_1)
Main Authors: Quadri, Syed Siraj Ahmed, Li, Caixia, Culver, Silas, Siragy, Helmy M
Format: Article
Language:English
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Summary:Abstract only Receptor dimerization was shown to enhance the receptor efficacy, trafficking and signal transduction. Angiotensin II type 1 receptor (AT1R) and (Pro)renin receptor (PRR) are expressed in the kidney. Studies demonstrated that these two receptors have some similarities in their signaling mechanisms and effects. In the present study we hypothesized that the AT1R and PRR form functional heterodimer to enhance cellular ERK phosphorylation. Using Immunoprecipitation technique, confocal immunofluorescence staining (IF), and fluorescence resonance energy transfer (FRET), we evaluated the presence of AT1R and PRR heterodimer in rat renal mesangial (RMC) and PC12W cells transfected with AT1R. These two receptors coimmunoprecipitated at 80kD band. IF demonstrated AT1R and PRR co-localization as shown in figure below and FRET demonstrated the physical distance between them to be less than 10nm (
ISSN:0194-911X
1524-4563
DOI:10.1161/hyp.66.suppl_1.p099