Visualization of the G-protein coupled receptor (GPCR) is of great importance for studying its function in a native cell. We have synthesized a series of red-emitting fluorescent probes targeting β-adrenergic receptor (βAR) that are compatible with confocal and Stimulated Emission Depletion (STED) microscopy as well as with Time-Resolved Fluorescence Resonance Energy Transfer (TR-FRET) binding assay in living cells. The probe based on the agonist BI-167107 and fluorescent dye KK114 demonstrates nanomolar binding affinity and up to nine-fold β2AR selectivity over β1AR. Carazolol-derived probes are fluorogenic and allow no-wash imaging experiments. STED microscopy of β2ARs stained at the native expression level on pancreatic CAPAN cells provides two-fold improvement in lateral optical resolution over confocal mode and reveals the formation of receptor microdomains. These probes retain their functional (agonist or antagonist) properties, allowing simultaneous modulation of cyclic adenosine monophosphate (cAMP) levels and receptor internalization as well as imaging receptor localization.
Characterization of [3H](+/-)carazolol binding to beta-adrenergic receptors. Application to study of beta-adrenergic receptor subtypes in canine ventricular myocardium and lung
A comparison of the selectivity of carazolol with that of other beta 2-selective adrenoceptor antagonists
Competitive and non-competitive interactions between specific ligands and beta-adrenoceptors in living cardiac cells
Visualization of agonist-induced sequestration and down-regulation of a green fluorescent protein-tagged beta2-adrenergic receptor.
Live cell imaging of Gs and the beta2-adrenergic receptor demonstrates that both alphas and beta1gamma7 internalize upon stimulation and exhibit similar trafficking patterns that differ from that of the beta2-adrenergic receptor
beta2-adrenergic receptor signaling and desensitization elucidated by quantitative modeling of real time cAMP dynamics
Cell-surface protein-protein interaction analysis with time-resolved FRET and snap-tag technologies: application to GPCR oligomerization
Breaking the diffraction resolution limit by stimulated emission: stimulated-emission-depletion fluorescence microscopy
Influence of fluorophore and linker composition on the pharmacology of fluorescent adenosine A1 receptor ligands
Expression of G protein-coupled receptors and related proteins in HEK293, AtT20, BV2, and N18 cell lines as revealed by microarray analysis
Synthesis and characterization of high-affinity 4,4-difluoro-4-bora-3a,4a-diaza-s-indacene-labeled fluorescent ligands for human β-adrenoceptors
A novel fluorescent histamine H(1) receptor antagonist demonstrates the advantage of using fluorescence correlation spectroscopy to study the binding of lipophilic ligands
Activatable optical imaging with a silica-rhodamine based near infrared (SiR700) fluorophore: a comparison with cyanine based dyes
Highly potent and selective fluorescent antagonists of the human adenosine A₃ receptor based on the 1,2,4-triazolo[4,3-a]quinoxalin-1-one scaffold
Polar red-emitting rhodamine dyes with reactive groups: synthesis, photophysical properties, and two-color STED nanoscopy applications
Fluorescent Rhodamines and Fluorogenic Carbopyronines for Super-Resolution STED Microscopy in Living Cells
Allosteric nanobodies reveal the dynamic range and diverse mechanisms of G-protein-coupled receptor activation
Development of novel fluorescent histamine H1 -receptor antagonists to study ligand-binding kinetics in living cells
Adrenergic Receptors: Trafficking
Adrenergic receptor trafficking is an active physiological process where adrenergic receptors are relocated from one region of the cell to another or from one type of cell to another. Discover the latest research on adrenergic receptor trafficking here.