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Pharmacological characterization of new @b-agonists using Hu@b"1- and Hu@b"2-adrenergic receptor binding assay in transfected HEK-293 cells [An article from: Analytica Chimica Acta]
Book Details
PublisherElsevier
ISBN / ASINB000RR3G48
ISBN-13978B000RR3G41
AvailabilityAvailable for download now
MarketplaceUnited States 🇺🇸
Description
This digital document is a journal article from Analytica Chimica Acta, published by Elsevier in 2005. The article is delivered in HTML format and is available in your Amazon.com Media Library immediately after purchase. You can view it with any web browser.
Description:
The continuous turn over of @b-agonists molecules, may affect the reliability of screening tests. To overcome possible false negative results, a bioassay is under development to detect the presence of new @b-agonists in feeds and biological matrices and so to provide a valid tool for a multi-analyte screening method. Preliminary study were focused on the pharmacological characterisation of new @b-agonists, with the aim to combine both the screening results with a toxicological evaluation about the potential health risk for consumers. The interaction of G4, G5, G6, G8 adrenergic drugs with human @b"1- and @b"2-adrenergic receptors expressed separately in membranes of human embryonic kidney cells in culture (HEK-293-Hu@b"1 and HEK-293-Hu@b"2), were studied by a receptor binding assay and results compared with those from a well-known @b-adrenergic agonist (clenbuterol). The specificity of the test was assured by the use of a specific radiolabel tracer ligand ([^1^2^5I]iodopindolol) as competitor. For compounds G4, G5 and G6 the affinity (IC"5"0) for @b"1-adrenergic binding sites was of the same magnitude of that from clenbuterol. By contrast, G8 showed a 100-fold higher affinity. On @b"2-adrenergic receptors the binding affinity was similar for G4 and G6, but about 10-fold higher for G5 and G8 with respect to that from clenbuterol.
Description:
The continuous turn over of @b-agonists molecules, may affect the reliability of screening tests. To overcome possible false negative results, a bioassay is under development to detect the presence of new @b-agonists in feeds and biological matrices and so to provide a valid tool for a multi-analyte screening method. Preliminary study were focused on the pharmacological characterisation of new @b-agonists, with the aim to combine both the screening results with a toxicological evaluation about the potential health risk for consumers. The interaction of G4, G5, G6, G8 adrenergic drugs with human @b"1- and @b"2-adrenergic receptors expressed separately in membranes of human embryonic kidney cells in culture (HEK-293-Hu@b"1 and HEK-293-Hu@b"2), were studied by a receptor binding assay and results compared with those from a well-known @b-adrenergic agonist (clenbuterol). The specificity of the test was assured by the use of a specific radiolabel tracer ligand ([^1^2^5I]iodopindolol) as competitor. For compounds G4, G5 and G6 the affinity (IC"5"0) for @b"1-adrenergic binding sites was of the same magnitude of that from clenbuterol. By contrast, G8 showed a 100-fold higher affinity. On @b"2-adrenergic receptors the binding affinity was similar for G4 and G6, but about 10-fold higher for G5 and G8 with respect to that from clenbuterol.
