Adrenoceptors: Introduction

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Adrenoceptors are 7-transmembrane receptors which mediate the central and peripheral actions of the neurotransmitter, noradrenaline (norepinephrine), and the hormone and neurotransmitter, adrenaline (epinephrine). Adrenoceptors are found in nearly all peripheral tissues and on many neuronal populations within the central nervous system. Both noradrenaline and adrenaline play important roles in the control of blood pressure, myocardial contractile rate and force, airway reactivity, and a variety of metabolic and central nervous system functions.

Agonists and antagonists interacting with adrenoceptors have proved useful in the treatment of a variety of diseases, including hypertension, angina pectoris, congestive heart failure, asthma, depression, benign prostatic hypertrophy, and glaucoma. These drugs are also useful in several other therapeutic situations including shock, premature labour and opioid withdrawal, and as adjuncts to general anaesthetics.

In 1948, adrenoceptors were first divided into two major types, α and β, based on their pharmacological characteristics (i.e., rank order of potency of agonists) [1]. Subsequently, both the α and β types were subdivided into α1, α2, β1 and β2 subtypes (for a more complete historical perspective, see ref. [10]). Based on both pharmacological and molecular evidence, it is now clear that a more useful classification scheme is based on three major types - α1, α2 and β - each of which is further divided into at least three subtypes (Figure) [7].


Building on an initial report that both phentolamine and WB4101 inhibited [3H]prazosin binding in rat frontal cortex in a manner consistent with more than a single type of receptor [4], Morrow and Creese [44] formally proposed a definition of α1A and α1B receptors based on the differential affinities of WB4101 and phentolamine. At about the same time Johnson and Minneman [30] observed that the alkylating agent chloroethylclonidine selectively inactivated only half of the [125I]-HEAT binding to α1-adrenoceptors in rat cerebral cortex. The inactivated sites corresponded to the α1B-adrenoceptor subtype, because they had low affinity for WB4101 [26,43].

Three α1-adrenoceptor subtypes have been identified by cloning. The α1B-adrenoceptor from the DDT cell line (hamster smooth muscle) was cloned first [15], followed by what was thought to be a novel α1-adrenoceptor from a bovine brain cDNA library identified as the α1C subtype [55]. Subsequently, it was shown that this clone corresponded to the pharmacologically defined α1A subtype [22,28]. A third α1-adrenoceptor was cloned from rat cortex and designated as the α1A-adrenoceptor [41]. However, an identical recombinant rat α1-adrenoceptor subtype was independently identified by Perez et al. [49] and denoted the α1D-adrenoceptor. This α1D-subtype was subsequently characterized functionally in tissues [33,50]. It appears that the α1D-adrenoceptor signals less effectively upon agonist stimulation as compared to the other subtypes, perhaps because it exhibits spontaneous internalization [27].

Four isoforms of the α1A-adrenoceptor have been reported. In addition to the originally reported sequence (α1A-1), two C-terminal variants (α1A-2 and α1A-3) produced by alterative splicing were reported in 1995 [29]. An additional splice variant (α1A-4) was reported subsequently [12]. No functional differences among these splice variants have been reported to date.

A fourth α1-adrenoceptor subtype has been postulated and is designated as α1L based on its low affinity for prazosin [48]. The evidence for the existence of the α1L-adrenoceptor is supported by pharmacological data in several tissues, including human prostate, bladder neck and periurethra longitudinal muscle [20,45-46]. It has been suggested that the α1L subtype may represent a particular conformational state of the α1A-adrenoceptor [21].The α1L-adrenoceptor mediated responses in the mouse prostate are essentially abolished in α1A-adrenoceptor knockout mice [25].


The evidence for α2-adrenoceptor subtypes has come from binding and functional studies in various tissues and cell lines, and more recently in cells transfected with the cDNA for the receptors [8]. On the basis of these studies, three genetic and four pharmacologically distinct α2-adrenoceptor subtypes have been defined. The α2A-adrenoceptor subtype, for which prazosin has a relatively low affinity and oxymetazoline a relatively high affinity, is found in human platelets and HT29 cells [7] and has been cloned from man [36]. The second subtype, the α2B, was identified in neonatal rat lung and in NG108 cells [11]. This subtype has relatively high affinity for prazosin and a low affinity for oxymetazoline, and has been cloned from man [61]. A third subtype, α2C, has been identified in an opossum kidney (OK) cell line and cloned from human kidney [47,52]. Although this subtype has relatively high affinity for prazosin and a low affinity for oxymetazoline, it is pharmacologically distinct from the α2B subtype [5]. A fourth pharmacological subtype, the α2D, has been identified in the rat salivary gland [42] and in the bovine pineal [57]. This pharmacological subtype has been cloned from the rat [40]. On the basis of the predicted amino acid sequence, the α2D is a species orthologue of the human α2A subtype, and thus is not considered to be a separate subtype.

Additional α2 subtypes have been identified in lower species, including five receptor genes in the zebrafish and as many as eight in the pufferfish [53]. In the zebrafish, three of the subtypes are similar to those found in mammals (orthologs, the same gene in different species), whereas the other two are not found in mammals, but are paralogs (duplicated genes in the same species). The significance of many receptor subtypes in a species is not well understood [9]


In 1967, Lands and coworkers [39], comparing rank orders of potency of agonists in a manner similar to that of Ahlquist, concluded that there were two subtypes of the β-adrenoceptor. The β1-adrenoceptor, the dominant receptor in heart and adipose tissue, was equally sensitive to noradrenaline and adrenaline, whereas the β2-adrenoceptor, responsible for relaxation of vascular, uterine, and airway smooth muscle, was much less sensitive to noradrenaline vis-a-vis adrenaline. Highly selective antagonists for both β1- and β2-adrenoceptors have been developed, as well as many potent and selective β2-adrenoceptor agonists.

Subsequently it has become apparent that not all of the β-adrenoceptor-mediated responses can be classified as either β1 or β2, suggesting the existence of at least one additional β-adrenoceptor subtype [3,6]. This β3 receptor is insensitive to the commonly used β-antagonists and has often been referred to as the 'atypical' β-adrenoceptor. It is unlikely that all of the atypical β-adrenoceptor responses observed have characteristics consistent with those of the β3-adrenoceptor, and hence, the possibility of additional subtypes cannot be excluded. Alternatively, agents may have atypical pharmacologies as the result of allosteric interactions at β-adrenoceptors [59]. Pharmacological evidence has been accumulating for a fourth β-adrenoceptor localized in cardiac tissues of various species [31]. This β4-adrenoceptor is activated with low potency by noradrenaline and adrenaline, and is blocked by β-adrenoceptor antagonists such as bupranolol and CGP20712A [24,54]. Although some of the pharmacology overlaps with the β3-adrenoceptor, the receptor-mediated response has recently been demonstrated in β3-adrenoceptor 'knock-out' mice [32]. However, definitive evidence for this putative β4-adrenoceptor is still lacking [58], and there is some evidence that it may be a 'state' of the β1-adrenoceptor [37-38]. It has been suggested that the β2-adrenoceptor may form homodimers [2] as well as oligomers with other receptors [56].

The β2-adrenoceptor was cloned from man [14,34] using probes derived from the hamster β2 receptor [16]. It proved difficult to clone the β1-adrenoceptor, because the human β2-adrenoceptor cDNA did not cross-hybridize with the β1-adrenoceptor. A related receptor was isolated using the β2-adrenoceptor cDNA as a probe [35], which proved to be the 5-HT1A receptor [19]. Using the coding region of the 5-HT1A receptor DNA to probe a human placental cDNA library, Frielle et al. [23] finally identified the β1-adrenoceptor clone. The β3-adrenoceptor was subsequently cloned from man [17]. Splice variants of the β3-adrenoceptor have been reported [18].

Recently the structure of the human β2-adrenoceptor has been solved by X-ray crystallography: a 3.4 Å structure of the wild type β2-adrenoceptor in complex with a conformationally sensitive Fab [51]; and a 2.4 Å structure of a β2-adrenoceptor engineered to facilitate crystal formation [13]. As this was the first 7-transmembrane receptor for a hormone or neurotransmitter to have its crystal structure solved, it provided a relevant template for homology models of closely related monoamine and other 7-transmembrane receptors. The crystal structure of the human β1-adrenoceptor has been recently published [60].


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Katrin Altosaar, Poornima Balaji, Richard A. Bond, David B. Bylund, Susanna Cotecchia, Dominic Devost, Van A. Doze, Douglas C. Eikenburg, Sarah Gora, Eugénie Goupil, Robert M. Graham, Terry Hébert, J. Paul Hieble, Rebecca Hills, Shahriar Kan, Gayane Machkalyan, Martin C. Michel, Kenneth P. Minneman, Sergio Parra, Dianne Perez, Rory Sleno, Roger Summers, Peter Zylbergold.
Adrenoceptors, introduction. Last modified on 01/02/2018. Accessed on 20/08/2019. IUPHAR/BPS Guide to PHARMACOLOGY,