ArticleMolecular pharmacology2010
Antagonist selective modulation of adenosine A1 and A3 receptor pharmacology by the food dye Brilliant Black BN: evidence for allosteric interactions.
Article in Molecular pharmacology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 33 citations in OpenAlex.
- Review
- Assay-Dependent Inverse Agonism at the AACS pharmacology & translational science · 2023Article
- Species dependence of APurinergic signalling · 2023Review
- Chemical Probes for the Adenosine Receptors.Pharmaceuticals (Basel, Switzerland) · 2019Review
- Article
- New paradigms in adenosine receptor pharmacology: allostery, oligomerization and biased agonism.British journal of pharmacology · 2018Review
- Article
- Negative cooperativity across β1-adrenoceptor homodimers provides insights into the nature of the secondary low-affinity CGP 12177 β1-adrenoceptor binding conformation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015Article
- Kinetic analysis of antagonist-occupied adenosine-A3 receptors within membrane microdomains of individual cells provides evidence of receptor dimerization and allosterism.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014Article
- Allosteric interactions at adenosine A(1) and A(3) receptors: new insights into the role of small molecules and receptor dimerization.British journal of pharmacology · 2014Review
- Synthesis of BODIPY derivatives substituted with various bioconjugatable linker groups: a construction kit for fluorescent labeling of receptor ligands.Journal of fluorescence · 2014Article
- Biophysical Detection of Diversity and Bias in GPCR Function.Frontiers in endocrinology · 2014Review
- Synthesis and characterization of high-affinity 4,4-difluoro-4-bora-3a,4a-diaza-s-indacene-labeled fluorescent ligands for human β-adrenoceptors.Journal of medicinal chemistry · 2011Article
- Allosteric interactions across native adenosine-A3 receptor homodimers: quantification using single-cell ligand-binding kinetics.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2011Article
- Allosteric modulation of purine and pyrimidine receptors.Advances in pharmacology (San Diego, Calif.) · 2011Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Allosteric binding sites on the adenosine receptor family represent potential therapeutic targets for a number of conditions involving metabolic stress. This study has identified Brilliant Black BN as a novel allosteric modulator of the adenosine A(1) and A(3) receptors. In addition to being a food dye and pharmaceutical excipient, Brilliant Black BN is commonly used within calcium mobilization assays to quench extracellular fluorescence. Brilliant Black BN (5-500 microM) had no significant effect on the calcium mobilization stimulated by the nonselective adenosine receptor agonist 5'-(N-ethylcarboxamido)adenosine in Chinese hamster ovary cells stably transfected with the human adenosine A(1) or A(3) receptor. Likewise, calcium mobilization and radioligand binding assays found that Brilliant Black BN (5-500 microM) did not significantly influence the antagonism mediated by 8-cyclopentyl-1,3-dipropylxanthine (100 nM) at the A(1) receptor. In contrast, the affinity of N-[9-chloro-2-(2-furanyl)[1,2,4]-triazolo[1,5-c]quinazolin-5-yl]benzene acetamide (MRS1220) at the A(3) receptor and xanthine amine congener (XAC) and XAC-X-BY630 at the A(1) and A(3) receptors was significantly decreased in the presence of 500 muM Brilliant Black BN. A reduction in XAC potency at the A(1) and A(3) receptor was achieved within 1 min of Brilliant Black BN addition, despite receptors having been pre-equilibrated with antagonist. Dissociation kinetics of the fluorescent XAC derivative, XAC-X-BY630, revealed that the decrease in affinity is probably due to a significant increase in dissociation rate of the antagonist in the presence of Brilliant Black BN. Taken together, these results suggest that Brilliant Black BN can act allosterically to modify ligand affinity at A(1) and A(3) receptors.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.