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Bombesin (and a wee bit of ranatensin)

Bombesin is a 14-amino acid peptide originally isolated from the skin of the European fire-bellied toad (Bombina bombina) by Vittorio Erspamer et al. and named after its source.

It has two known homologs in mammals called neuromedin B and gastrin-releasing peptide. It stimulates gastrin release from G cells. It activates three different G-protein-coupled receptors known as BBR1, -2, and -3.

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.

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 Gastroenterology34 (12): 1224–9. doi:10.1080/003655299750024742PMID 10636070.

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.

Effects

Erspamer 1988 finds bombesin has a similar effect on the chicken to ranatensin, unreliably increasing or decreasing blood pressure.

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.

See also

References

  1. Gonzalez N, Moody TW, Igarashi H, Ito T, Jensen RT (February 2008). “Bombesin-related peptides and their receptors: recent advances in their role in physiology and disease states”Current Opinion in Endocrinology, Diabetes and Obesity15 (1): 58–64. doi:10.1097/MED.0b013e3282f3709bPMC 2631407PMID 18185064.
  2. Anastasi, A.; Erspamer, Vittorio; Bucci, M. (1971). “Isolation and structure of bombesin and alytesin, two analogous active peptides from the skin of the european amphibians Bombina and Alytes“. ExperientiaSpringer27 (2): 166–167. doi:10.1007/bf02145873ISSN 0014-4754S2CID 30779940.
  3. Verkhratsky, Alexei; Nedergaard, Maiken (2018-01-01). “Physiology of Astroglia”Physiological ReviewsAmerican Physiological Society98 (1): 239–389. doi:10.1152/physrev.00042.2016ISSN 0031-9333.
  4. M., H. (1972). “Toxicon Reviews”. ToxiconInternational Society on Toxinology + Brazilian Society of Toxinology + North American Society of Toxinology (Elsevier). 10 (2): 189. doi:10.1016/0041-0101(72)90248-6ISSN 0041-0101PMID 5544731S2CID 32711539.
  5. Daniel, Edwin E., ed. (2019-08-15). Neuropeptide Function in the Gastrointestinal Tract. CRC Press. ISBN 978-0-429-28576-9OCLC 1112671803.
  6. Jensen, R. T.; Battey, J. F.; Spindel, E. R.; Benya, R. V. (2007-11-30). “International Union of Pharmacology. LXVIII. Mammalian Bombesin Receptors: Nomenclature, Distribution, Pharmacology, Signaling, and Functions in Normal and Disease States”Pharmacological ReviewsAmerican Society for Pharmacology & Experimental Therapeutics (ASPET). 60 (1): 1–42. doi:10.1124/pr.107.07108ISSN 0031-6997PMC 2517428PMID 18055507NIHMSID 45053.
  7. Weber HC (February 2009). “Regulation and signaling of human bombesin receptors and their biological effects”. Current Opinion in Endocrinology, Diabetes and Obesity16 (1): 66–71. doi:10.1097/med.0b013e32831cf5aaPMID 19115523S2CID 45482442.
  8. 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 Medicine32 (8): 519–29. doi:10.3109/07853890008998831PMID 11127929S2CID 24431961.
  9. 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 Gastroenterology34 (12): 1224–9. doi:10.1080/003655299750024742PMID 10636070.
  10. Erspamer, Vittorio (1988). “Discovery, Isolation, and Characterization of Bombesin-like Peptides”. Part I. Chemistry and Molecular Biology of Bombesin-like Peptides. Annals of the New York Academy of SciencesNYAS (WB). 547 (1 Bombesin-Like): 3–9. doi:10.1111/j.1749-6632.1988.tb23870.xISSN 0077-8923.
  11. Moreno, Paola; Mantey, Samuel A.; Nakamura, Taichi; Nuche-Berenguer, Bernardo; Moody, Terry W.; Coy, David H.; Jensen, Robert T. (2001-09-06). “Insights into Bombesin receptors and ligands: Highlighting recent advances”PeptidesElsevier72doi:10.1016/j.peptides.2015.04.026PMC 4641779PMID 25976083NIHMSID 697823.
  12. Daniel, Edwin E., ed. (2019-08-15). Neuropeptide Function in the Gastrointestinal Tract. CRC Press. ISBN 978-0-429-28576-9OCLC 1112671803.
  13. Jensen, R. T.; Battey, J. F.; Spindel, E. R.; Benya, R. V. (2007-11-30). “International Union of Pharmacology. LXVIII. Mammalian Bombesin Receptors: Nomenclature, Distribution, Pharmacology, Signaling, and Functions in Normal and Disease States”Pharmacological ReviewsAmerican Society for Pharmacology & Experimental Therapeutics (ASPET). 60 (1): 1–42. doi:10.1124/pr.107.07108ISSN 0031-6997PMC 2517428PMID 18055507NIHMSID 45053.
  14. 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.
  15. https://www.sciencedirect.com/topics/neuroscience/ranatensin
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