The tissue distribution of the human b b 3 -adrenoceptor studied using a monoclonal antibody: Direct evidence of the b b 3 -adrenoceptor in human adipose tissue, atrium and skeletal muscle 2,3 The human b 3 -adrenoceptor was later cloned by Emorine et al. 4 The pharmacology of the cloned b 3 -adrenoceptor agreed with the pharmacological data previously obtained in rodent adipose tissue, gut, and skeletal muscle in that the badrenoceptors in these tissues were insensitive to classical b-adrenoceptor antagonists such as propranolol.5 ± 8 Aryloxypropanolamine b 1 ab 2 adrenoceptor antagonists, exempli®ed by CGP12177, evoke a lipolytic response in rat adipose tissue through agonism at b 3 -adrenoceptors. 9 Similarly, selective b 3 -adrenoceptor agonists, such as BRL-37344, showed similar or greater potency than isoproterenol in stimulating lipolysis, but were much less potent than isoproterenol in stimulating responses mediated by b 1 -or b 2 -adrenoceptors. 10 The assessment of the pharmacological role of b 3 -adrenoceptors in human tissues has proved more controversial. For example, lipolysis in human white adipocytes induced by isoproterenol is sensitive to propranolol.11 Also, CGP12177-induced lipolytic responses have been demonstrated by some 12 ± 14 but not others. 9,15 It is now evident from comparisons of cloned human and rat b 3 -adrenoceptors that there are signi®cant species differences in pharmacology. 16 Attempts to detect b 3 -mRNA in human tissues using reverse-transcription PCR have also given conicting results. Krief et al 17 detected b 3 -adrenoceptor mRNA in several tissues, including gall bladder, adipose tissue and colon, while Thomas and Liggett 18 failed to detect a b 3 -adrenoceptor signal. Recently, RNAase protection assays, that do not rely on ampli®cation techniques, were used to identify b 3 -adrenoceptor mRNA in a variety of human tissues, including
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