Mouse Nmbr

Figure. Concentration-dependent activation of Nmbr by NMB

Reporter cells were transfected with either the expression plasmid for mouse neuromedin B receptor (Nmbr) or the mock plasmid and treated with various concentrations of the reference agonist. Data points shown are the mean ± SEM of an experiment (n = 4).

neuromedin B receptor
Available assay modes
Agonist, Inverse agonist, Antagonist, PAM, NAM
à la carte, Mouse non-orphan GPCRs

Bombesin receptors

Mammalian bombesin (Bn) receptors comprise 3 subtypes: BB1, BB2, BB3. BB1 and BB2 are activated by the endogenous ligands neuromedin B (NMB), gastrin-releasing peptide (GRP), and GRP-(18-27). bombesin is a tetra-decapeptide, originally derived from amphibians. The three Bn receptor subtypes couple primarily to the Gq/11 and G12/13 family of G proteins [1]. Each of these receptors is widely distributed in the CNS and peripheral tissues [1,2,3,4,5,6]. 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, gastrointestinal motility, feeding behavior, secretion and many central nervous system effects including regulation of circadian rhythm, body temperature control, sighing and mediation of pruritus [1,3,7,8,9,10,11,12,13,14]. A physiological role for the BB3 receptor has yet to be fully defined although recently studies suggest an important role in glucose and insulin regulation, metabolic homeostasis, feeding, regulation of body temperature, obesity, diabetes mellitus and growth of normal/neoplastic tissues [2,15,16,17,18,19]. 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 [8,20,21,22].


  1. Jensen RT, Battey JF, Spindel ER, et al. International Union of Pharmacology. LXVIII. Mammalian bombesin receptors: nomenclature, distribution, pharmacology, signaling, and functions in normal and disease states. Pharmacol Rev 2008;60:1-42.
  2. González N, Moreno P, Jensen RT. Bombesin receptor subtype 3 as a potential target for obesity and diabetes. Expert Opin Ther Targets 2015;19:1153-70.
  3. Ramos-Álvarez I, Moreno P, Mantey SA, et al. Insights into bombesin receptors and ligands: Highlighting recent advances. Peptides 2015;72:128-44.
  4. Sano H, Feighner SD, Hreniuk DL, et al. Characterization of the bombesin-like peptide receptor family in primates. Genomics 2004;84:139-46.
  5. Porcher C, Juhem A, Peinnequin A, et al. Bombesin receptor subtype-3 is expressed by the enteric nervous system and by interstitial cells of Cajal in the rat gastrointestinal tract. Cell Tissue Res 2005;320:21-31.
  6. Zhang L, Parks GS, Wang Z, et al. Anatomical characterization of bombesin receptor subtype-3 mRNA expression in the rodent central nervous system. J Comp Neurol 2013;521:1020-39.
  7. Li P, Janczewski WA, Yackle K, et al. The peptidergic control circuit for sighing. Nature 2016;530:293-297.
  8. Moreno P, Ramos-Álvarez I, Moody TW, et al. Bombesin related peptides/receptors and their promising therapeutic roles in cancer imaging, targeting and treatment. Expert Opin Ther Targets 2016;20:1055-73.
  9. Qu X, Wang H, Liu R. Recent insights into biological functions of mammalian bombesin-like peptides and their receptors. Curr Opin Endocrinol Diabetes Obes 2018;25:36-41.
  10. Moody TW, Merali Z. Bombesin-like peptides and associated receptors within the brain: distribution and behavioral implications. Peptides 2004;25:511-520.
  11. Sun YG, Chen ZF. A gastrin-releasing peptide receptor mediates the itch sensation in the spinal cord. Nature 2007;448:700-3.
  12. Gajjar S, Patel BM. Neuromedin: An insight into its types, receptors and therapeutic opportunities. Pharmacol Rep 2017;69:438-447.
  13. Chen XJ, Sun YG. Central circuit mechanisms of itch. Nat Commun 2020;11:3052.
  14. Wan L, Jin H, Liu XY, et al. Distinct roles of NMB and GRP in itch transmission. Sci Rep 2017;7:15466.
  15. Li M, Liang P, Liu D, et al. Bombesin Receptor Subtype-3 in Human Diseases. Arch Med Res 2019;50:463-467.
  16. Majumdar ID, Weber HC. Biology and pharmacology of bombesin receptor subtype-3. Curr Opin Endocrinol Diabetes Obes 2012;19:3-7.
  17. Ohki-Hamazaki H, Watase K, Yamamoto K, et al. Mice lacking bombesin receptor subtype-3 develop metabolic defects and obesity. Nature 1997;390:165-9.
  18. Xiao C, Reitman ML. Bombesin-Like Receptor 3: Physiology of a Functional Orphan. Trends Endocrinol Metab 2016;27:603-5.
  19. Moreno P, Mantey SA, Lee SH, et al. A possible new target in lung-cancer cells: The orphan receptor, bombesin receptor subtype-3. Peptides 2018;101:213-226.
  20. Sancho V, Di Florio A, Moody TW, et al. Bombesin receptor-mediated imaging and cytotoxicity: review and current status. Curr Drug Deliv 2011;8:79-134.
  21. Baratto L, Duan H, Mäcke H, et al. Imaging the Distribution of Gastrin-Releasing Peptide Receptors in Cancer. J Nucl Med 2020;61:792-798.
  22. Maina T, Nock BA. From Bench to Bed: New Gastrin-Releasing Peptide Receptor-Directed Radioligands and Their Use in Prostate Cancer. PET Clin 2017;12:205-217.


NMB is a decapeptide which was originally isolated from porcine spinal cord [1] and is the mammalian equivalent of the frog peptide ranatensin, to which it has an almost identical COOH terminus with six of seven amino acid identities [2]. The location of the human NMB gene is chromosome 15q11 [3,4]. NMB is encoded as a prepro-NMB, a 76 amino acid precursor that consists of a 24 amino acid signal peptide, NMB-32 and a 17 amino acid carboxyl terminal extension peptide [3]. The predicted amino acid sequence for NMB-32 is highly conserved in human, rat and pig with only differences of four amino acids [2,5]. The NMB gene is encoded in three exons and studies on rat and human genomic DNA are consistent with only a single NMB gene present. In the human Northern blot analysis reveals high expression in the hypothalamus, colon, stomach and low levels in the pancreas, cerebellum and adrenals [2]. By in situ hybridization studies NMB mRNA was found in rat brain in the greatest amounts in the olfactory bulb, dentate gyrus and dorsal root ganglion [5]. NMB has a wide range of physiological and pharmacological effects and these will be discussed later.


  1. Minamino N, Kangawa K, Matsuo H. Neuromedin B: a novel bombesin-like peptide identified in porcine spinal cord. Biochem Biophys Res Commun 1983;114:541-548.
  2. Ohki-Hamazaki H. Neuromedin B. Prog Neurobiol 2000;62:297-312.
  3. Krane IM, Naylor SL, Helin-Davis D, et al. Molecular cloning of cDNAs encoding the human bombesin-like peptide neuromedin B. Chromosomal localization and comparison to cDNAs encoding its amphibian homolog ranatensin. J Biol Chem 1988;263:13317-23.
  4. Gregory CA, Schwartz JS. The cDNA of the human neuromedin B gene (NMB) mapped to 15q11-qter recognizes an XbaI RFLP. Nucleic Acids Res 1991;19:1167.
  5. Wada E, Way J, Lebacq-Verheyden AM, et al. Neuromedin B and gastrin-releasing peptide mRNAs are differentially distributed in the rat nervous system. J Neurosci 1990;10:2917-2930.
Excerpt from IUPHAR/BPS Guide to Pharmacology

Related Receptors

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