Mammalian bombesin (Bn) receptors comprise 3 subtypes: BB₁, BB₂, BB₃ (nomenclature recommended by the NC-IUPHAR Subcommittee on bombesin receptors, [1,14]). BB₁ and BB₂ are activated by the endogenous ligands neuromedin B (NMB, P08949) (NMB), gastrin-releasing peptide (GRP, P07492) (GRP), and GRP-(18-27) (GRP, P07492). Bombesin is a tetra-decapeptide, originally derived from amphibians and structurally closely related to GRP. The three Bn receptor subtypes couple primarily to the G_q/11 and G_12/13 family of G proteins [14]. Each of these receptors is widely distributed in the CNS and peripheral tissues [9,13-14,22-23,43,47,51,60]. Activation of BB₁ and BB₂ receptors causes a wide range of physiological/pathophysiogical actions, including the stimulation of normal and neoplastic tissue growth, smooth-muscle contraction, respiration, gastrointestinal motility, feeding behavior, secretion and many central nervous system effects including regulation of circadian rhythm, body temperature control, sighing, behavioral disorders and mediation of pruritus [4-5,7,14,20,35,38-39,44,47,53,58]. BB₃ is an orphan receptor, although some propose it is constitutively active [54]. BB₃ receptor knockout studies show it has important roles in glucose and insulin regulation, metabolic homeostasis, feeding, regulation of body temperature, obesity, diabetes mellitus and growth of normal/neoplastic tissues [9,19,25,36,41,59]. Bn receptors are one of the most frequently overexpressed receptors in cancers and are receiving increased attention for their roles in tumor growth, as well as for tumour imaging and for receptor-targeted cytotoxicity [2,16,24,26-27,33,38,50]. Bn receptors are also receiving attention because they are one of the primary neurotransmitters for pruritus [4-5,15,53].

All three human subtypes may be activated by [D-Phe⁶,β-Ala¹¹,Phe¹³,Nle¹⁴]bombesin-(6-14) [30]. The Agonist [D-Tyr⁶,Apa-4Cl11,Phe¹³,Nle1⁴]bombesin-(6-14) has more than 200-fold selectivity for BB₃ receptors over BB₁ and BB₂ [29-30,47,47-48]. A recent study [45] shows MK-5046 is functioning as an allosteric agonist for hBRS-3 (the first for any BnR). A further recent study reports for the first time, the inactive crystal structure of hGRPR (BB₂) as well as two active state GRPR structures bound to GRP or [D-Phe6,β-Ala11,Phe13,Nle14]bombesin-(6-14) [42].

* Key recommended reading is highlighted with an asterisk

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Subcommittee members: Robert T. Jensen (Chairperson) National Institute of Diabetes & Kidney Diseases National Institutes of Health Building 10 Room 9C-103 NIH Bethesda MD 20892 USA Jim Battey National Institute on Deafness and Other Communication Disorders Building 31 Room 3C02 NIH Bethesda MD 20892 USA Richard V. Benya University of Illinois Section of Digestive Diseases and Nutrition 840 South Wood Street (M/C 716) Chicago Illinois 60612 USA Terry W. Moody National Institutes of Health Center for Cancer Research Bethesda MD USA