Elsevier

Genomics

Volume 84, Issue 1, July 2004, Pages 139-146
Genomics

Characterization of the bombesin-like peptide receptor family in primates

https://doi.org/10.1016/j.ygeno.2004.01.008Get rights and content

Abstract

In mammals, bombesin-like peptides mediate a broad range of physiological functions through binding to three highly conserved G-protein-coupled receptors: the neuromedin B-preferring, the gastrin-releasing peptide-preferring, and the bombesin-receptor subtype 3. Selective modulation of these receptors presents opportunities for the development of novel therapeutics. To ascertain if rhesus monkey could serve as a surrogate animal model for the development of modulators of bombesin-like receptor function, we undertook a search for additional receptor family members and studied the expression profiles of the three known bombesin-related receptors. We found no evidence for additional receptor family members in mammals, suggesting that the expression of the previously described bombesin-receptor subtype 4 is limited to amphibians. We studied the distribution of the three receptors in a broad array of human and rhesus monkey tissues. Based on the similarity between the human and the rhesus expression profiles, we conclude that the rhesus monkey may be a suitable animal model to evaluate the clinical efficacy and potential side effects of bombesin-like peptide ligands.

Section snippets

Search for mammalian BB4R

RT-PCR and genomic PCR were conducted on rhesus, Xenopus, and human brain cDNA or genomic DNA using primers for the reported rhesus BB4R DNA fragment [10]. The primers were almost perfectly conserved with the Bombina BB4R DNA sequence. Unexpectedly, an amplified fragment from Xenopus cDNA and genomic DNA that perfectly matched the partial rhesus BB4R sequence [10] was found. Attempts to detect the partial rhesus BB4R by RT-PCR using human and rhesus mRNA samples were not successful. These

Poly(A)+ mRNA and genomic DNA isolation

Poly(A)+ mRNAs were isolated from rhesus hypothalamus, cerebellum, pituitary gland, pons, medulla oblongata, liver, brain (except for hypothalamus, cerebellum, pituitary gland, pons, medulla oblongata), liver, and testis using FastTrack 2.0 (Invitrogen, Carlsbad, CA, USA). Genomic DNA was purified from rhesus liver and Xenopus laevis brain. Human poly(A)+ RNAs and genomic DNA were purchased from Clontech (Palo Alto, CA, USA).

Genomic and RT-PCR for BB4R

Primers were based on a rhesus BB4 partial sequence [10] and had high

References (42)

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    Mammalian BRS-3 may be conserved during evolution because it can modify the response pattern of other GPCRs or contribute to basal signaling [11]. Brs3 mRNA and BRS-3 binding activity are located in restricted regions of the brain, including portions of the hypothalamus, amygdala, and thalamus [12–19]. BRS-3 is also reported to be present at low levels in peripheral sites including pancreatic islets, developing testis, female reproductive tract, lung, and muscle, and in certain cancers [5,20–22] (https://gtexportal.org/home/gene/BRS3).

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    There is a possible reason that NMB and GRP are differentially distributed in the rat nervous system which suggests that these 2 structurally related peptides may have very distinct functions as neuropeptides in the rat nervous system (Moody et al., 1986). In addition, it has been recognized that NMBR has greater than a 100-food higher affinity for NMB than GRP, whereas the GRPR has a greater than 50-fold higher affinity for GRP than NMB (Jensen et al., 2008; Sano et al., 2004) which might be an explanation of more effective in improving learning and memory of NMB than GRP. And other studies also found that GRP and NMB could exert not exactly the same physiological action in anxiety and fear-related behavior (Bedard et al., 2007).

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