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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Classical and atypical binding sites for beta-adrenoceptor ligands and activation of adenylyl cyclase in bovine skeletal muscle and adipose tissue membranes.

1. The radioligand [125I]-iodocyanopindolol ([125I]-ICYP) was used under standard ligand binding conditions, to detect beta 1- and beta 2-adrenoceptors in membrane preparations from bovine skeletal muscle and adipose tissue. High concentrations of [125I]-ICYP were also used, to identify an 'atypical' binding site in skeletal muscle. Finally, adenosine 3':5'-cyclic monophosphate (cyclic AMP) production was measured in the same membrane preparations, to determine the relationship between the beta-adrenoceptor sub-types present and the production of this second-messenger. 2. According to the results of radioligand binding studies, both skeletal muscle and adipose tissue membranes have beta 2-adrenoceptors, characterized by a high affinity for the beta 2-selective antagonist, ICI 118551 (pK 8.3 and 8.6 respectively); and a low affinity for the beta 1-selective antagonist CGP 20712A (pK 5.2 in both tissues). Antagonism of (-)-isoprenaline-stimulated cyclic AMP production by low concentrations of ICI 118551, yielded pseudo pA2 values in muscle and adipose tissue of 7.6 and 8.7 respectively, confirming that beta 2-adrenoceptors in these tissues are linked to the production of the second-messenger. 3. Although beta 1-adrenoceptors could not be detected in either skeletal muscle or adipose tissue membranes by use of ligand binding techniques, high pseudo pA2 values were obtained (8.0 and 8.2 respectively), when CGP 20712A was used to block the stimulation of cyclic AMP production by (-)-isoprenaline. This finding is consistent with the presence in both tissues of a population of beta 1-adrenoceptors which is small, but efficiently coupled to the second-messenger.(ABSTRACT TRUNCATED AT 250 WORDS)[1]


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