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Bombesin
Chemical compound

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.

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Receptors

The anuran BB4 receptor homologue is termed frog BB4 (fBB4).7 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-3.5.8

Effects

Erspamer 1988 finds bombesin has a similar effect on the chicken to ranatensin, unreliably increasing or decreasing blood pressure.9

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 Obesity. 15 (1): 58–64. doi:10.1097/MED.0b013e3282f3709b. PMC 2631407. PMID 18185064. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2631407

  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". Experientia. 27 (2). Springer: 166–167. doi:10.1007/bf02145873. ISSN 0014-4754. PMID 5544731. S2CID 30779940.Verkhratsky, Alexei; Nedergaard, Maiken (2018-01-01). "Physiology of Astroglia". Physiological Reviews. 98 (1). American Physiological Society: 239–389. doi:10.1152/physrev.00042.2016. ISSN 0031-9333. PMC 6050349. PMID 29351512.M., H. (1972). "Toxicon Reviews". Toxicon. 10 (2). International Society on Toxinology + Brazilian Society of Toxinology + North American Society of Toxinology (Elsevier): 189. doi:10.1016/0041-0101(72)90248-6. ISSN 0041-0101. PMID 5544731. S2CID 32711539.Daniel, Edwin E., ed. (2019-08-15). Neuropeptide Function in the Gastrointestinal Tract. CRC Press. ISBN 978-0-429-28576-9. OCLC 1112671803. 978-0-429-28576-9

  3. 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 Reviews. 60 (1). American Society for Pharmacology & Experimental Therapeutics (ASPET): 1–42. doi:10.1124/pr.107.07108. ISSN 0031-6997. PMC 2517428. PMID 18055507. NIHMSID 45053. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2517428

  4. 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. PMID 19115523. S2CID 45482442. /wiki/Doi_(identifier)

  5. 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. PMID 11127929. S2CID 24431961. /wiki/Doi_(identifier)

  6. 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. PMID 10636070. /wiki/Doi_(identifier)

  7. 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 Reviews. 60 (1). American Society for Pharmacology & Experimental Therapeutics (ASPET): 1–42. doi:10.1124/pr.107.07108. ISSN 0031-6997. PMC 2517428. PMID 18055507. NIHMSID 45053. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2517428

  8. 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 Reviews. 60 (1). American Society for Pharmacology & Experimental Therapeutics (ASPET): 1–42. doi:10.1124/pr.107.07108. ISSN 0031-6997. PMC 2517428. PMID 18055507. NIHMSID 45053. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2517428

  9. 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 Sciences. 547 (1 Bombesin-Like). NYAS (WB): 3–9. Bibcode:1988NYASA.547....3E. doi:10.1111/j.1749-6632.1988.tb23870.x. ISSN 0077-8923. PMID 3071223. S2CID 83974453.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". Peptides. 72. Elsevier: 128–144. doi:10.1016/j.peptides.2015.04.026. PMC 4641779. PMID 25976083. NIHMSID 697823.Daniel, Edwin E., ed. (2019-08-15). Neuropeptide Function in the Gastrointestinal Tract. CRC Press. ISBN 978-0-429-28576-9. OCLC 1112671803.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 Reviews. 60 (1). American Society for Pharmacology & Experimental Therapeutics (ASPET): 1–42. doi:10.1124/pr.107.07108. ISSN 0031-6997. PMC 2517428. PMID 18055507. NIHMSID 45053. 978-0-429-28576-9