Weber HC (February 2009). “Regulation and signaling of human bombesin receptors and their biological effects”. Current Opinion in Endocrinology, Diabetes and Obesity. 16 (1): 66–71. doi:10.1097/med.0b013e32831cf5aa. PMID19115523. S2CID45482442.
It also activates these receptors in the brain. Together with cholecystokinin, it is the second major source of negative feedback signals that stop eating behaviour.
Yamada K, Wada E, Wada K (November 2000). “Bombesin-like peptides: studies on food intake and social behaviour with receptor knock-out mice”. Annals of Medicine. 32 (8): 519–29. doi:10.3109/07853890008998831. PMID11127929. S2CID24431961.
Bombesin is also a tumor marker for small cell carcinoma of lung, gastric cancer, pancreatic cancer, and neuroblastoma.
Ohlsson B, Fredäng N, Axelson J (December 1999). “The effect of bombesin, cholecystokinin, gastrin, and their antagonists on proliferation of pancreatic cancer cell lines”. Scandinavian Journal of Gastroenterology. 34 (12): 1224–9. doi:10.1080/003655299750024742. PMID10636070.
Receptors
The anuran BB4 receptor homologue is termed frog BB4 (fBB4). Iwabuchi et al. 2003 discovered a chicken (Gallus domesticus) receptor which is homologous to both the mammalian BB3 and fBB4 and so they named it chBRS-3.5.
Unfortunately, Wikipedia does not have a ranatensin page and I think it probably should. Spellcheck doesn’t like the word so maybe it is called something else. For now, I’ve had to scoot over to Science Direct where I found this article (There is lots more at the article itself. There is talk of chapters so maybe it is a book or something in between an article and a book. We shall find out.):
The structure of ranatensin, a vasoactive undecapeptide isolated from extracts of amphibian skin, was described by Nakajima et al. (1970), and shortly thereafter Erspamer and colleagues (Erspamer et al., 1970; Anastasi et al., 1971) reported the structures of bombesin and alytesin, tetradecapeptides isolated from extracts of the skin of two European frogs. Bombesin and alytesin differed in only 2 of their 14 amino acid residues, and both peptides had marked carboxy-terminal sequence homology with ranatensin. A number of amphibian skin peptides structurally related to bombesin and ranatensin have since been characterized, and these are commonly referred to as the bombesin family of peptides (Erspamer, 1980). Intense interest in this peptide family was initiated by the demonstrations by Erspamer and colleagues that administration of bombesin to mammals resulted in elevation of plasma gastrin levels (Bertaccini et al., 1974a), increased gastric acid secretion (Bertaccini et al., 1973), stimulated gallbladder contraction, and increased exocrine pancreas secretion (Erspamer et al., 1974; Erspamer and Melchiorri, 1975). From these studies the question arose as to whether or not bombesinlike peptides were present in mammals. Erspamer and Melchiorri (1975) reported that tissue extracts from the mammalian gastrointestinal tract did indeed contain bombesinlike immunoreactivity (BLI), a finding rapidly confirmed by others (Polak et al., 1976; Brown et al., 1978; Dockray et al., 1979; Walsh et al., 1979). The presence of BLI was also demonstrated in the mammalian central nervous system (Brown et al., 1978; Villarreal and Brown, 1978). Robberecht et al. (1975) and Deschodt-Lanckman et al. (1976) reported that bombesin stimulated amylase release from the mammalian pancreas in vitro, and subsequent studies demonstrated the presence of receptors for bombesin on mammalian pancreatic acinar cells (Iwatsuki and Petersen, 1978; Jensen et al., 1978) and in the mammalian central nervous system (Moody et al., 1978). These and other studies provided strong evidence for the existence of mammalian bombesinlike peptides.
Thomas J. McDonald, The Gastrin-Releasing Polypeptide (GRP), part of volume Gastrointestinal Hormones edited by Victor Mutt- The Gastrin-Releasing Polypeptide (GRP) in Advances in Metabolic Disorders, 1988 doi.org/10.1016/B978-0-12-027311-9.50011-1.
Weber HC (February 2009). “Regulation and signaling of human bombesin receptors and their biological effects”. Current Opinion in Endocrinology, Diabetes and Obesity. 16 (1): 66–71. doi:10.1097/med.0b013e32831cf5aa. PMID19115523. S2CID45482442.
Yamada K, Wada E, Wada K (November 2000). “Bombesin-like peptides: studies on food intake and social behaviour with receptor knock-out mice”. Annals of Medicine. 32 (8): 519–29. doi:10.3109/07853890008998831. PMID11127929. S2CID24431961.
Ohlsson B, Fredäng N, Axelson J (December 1999). “The effect of bombesin, cholecystokinin, gastrin, and their antagonists on proliferation of pancreatic cancer cell lines”. Scandinavian Journal of Gastroenterology. 34 (12): 1224–9. doi:10.1080/003655299750024742. PMID10636070.
Thomas J. McDonald, The Gastrin-Releasing Polypeptide (GRP), part of volume Gastrointestinal Hormones edited by Victor Mutt- The Gastrin-Releasing Polypeptide (GRP) in Advances in Metabolic Disorders, 1988 doi.org/10.1016/B978-0-12-027311-9.50011-1.
