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In vivo model with targeted cAMP biosensor reveals changes in receptor–microdomain communication in cardiac disease
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In vivo model with targeted cAMP biosensor reveals changes in receptor–microdomain communication in cardiac disease
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Journal Article
In vivo model with targeted cAMP biosensor reveals changes in receptor–microdomain communication in cardiac disease
2015
Overview
3′,5′-cyclic adenosine monophosphate (cAMP) is an ubiquitous second messenger that regulates physiological functions by acting in distinct subcellular microdomains. Although several targeted cAMP biosensors are developed and used in single cells, it is unclear whether such biosensors can be successfully applied
in vivo
, especially in the context of disease. Here, we describe a transgenic mouse model expressing a targeted cAMP sensor and analyse microdomain-specific second messenger dynamics in the vicinity of the sarcoplasmic/endoplasmic reticulum calcium ATPase (SERCA). We demonstrate the biocompatibility of this targeted sensor and its potential for real-time monitoring of compartmentalized cAMP signalling in adult cardiomyocytes isolated from a healthy mouse heart and from an
in vivo
cardiac disease model. In particular, we uncover the existence of a phosphodiesterase-dependent receptor–microdomain communication, which is affected in hypertrophy, resulting in reduced β-adrenergic receptor-cAMP signalling to SERCA.
cAMP is a second messenger that acts in distinct intracellular locations regulating diverse cellular functions. Here the authors design a FRET-based cAMP biosensor and use it to measure
in vivo
dynamics of cAMP concentration changes in the sarcoplasmatic reticulum of mouse cardiomyocytes in health and disease.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 64/110
/ 9/10
/ Animals
/ Female
/ Fluorescence Resonance Energy Transfer
/ Guanine Nucleotide Exchange Factors
/ Humanities and Social Sciences
/ Myocytes, Cardiac - metabolism
/ Phosphoric Diester Hydrolases - metabolism
/ Sarcoplasmic Reticulum Calcium-Transporting ATPases - metabolism
/ Science
