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Revision as of 19:11, 28 January 2023 editOAbot (talk \| contribs)Bots441,761 editsm Open access bot: doi added to citation with #oabot.← Previous edit		Revision as of 18:45, 27 August 2023 edit undoOnel5969 (talk \| contribs)Autopatrolled, Extended confirmed users, Page movers, New page reviewers, Pending changes reviewers, Rollbackers937,225 editsm Disambiguating links to Homology (link changed to Homologous series) using DisamAssist.Next edit →
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	\|{{cite book \| editor-last=Daniel \| editor-first=Edwin E. \| title=Neuropeptide Function in the Gastrointestinal Tract \| publisher=CRC Press \| date=2019-08-15 \| isbn=978-0-429-28576-9 \| oclc=1112671803}}		\|{{cite book \| editor-last=Daniel \| editor-first=Edwin E. \| title=Neuropeptide Function in the Gastrointestinal Tract \| publisher=CRC Press \| date=2019-08-15 \| isbn=978-0-429-28576-9 \| oclc=1112671803}}
	}}		}}
	</ref> by ] ''et al.'' and named after its source.<ref name="Jensen-et-al-2007">{{cite journal \| last1=Jensen \| first1=R. T. \| last2=Battey \| first2=J. F. \| last3=Spindel \| first3=E. R. \| last4=Benya \| first4=R. V. \| title=International Union of Pharmacology. LXVIII. Mammalian Bombesin Receptors: Nomenclature, Distribution, Pharmacology, Signaling, and Functions in Normal and Disease States \| journal=] \| publisher=] (ASPET) \| volume=60 \| issue=1 \| date=2007-11-30 \| issn=0031-6997 \| doi=10.1124/pr.107.07108 \| pages=1–42 \| pmc=2517428 \| pmid=18055507}} ] 45053.</ref> It has two known ] in ] called ] and ]. It stimulates ] release from ]. It activates three different ]-coupled ] known as BBR1, -2, and -3.<ref name="pmid19115523">{{cite journal \| author = Weber HC \| title = Regulation and signaling of human bombesin receptors and their biological effects \| journal = Current Opinion in Endocrinology, Diabetes and Obesity \| volume = 16 \| issue = 1 \| pages = 66–71 \|date=February 2009 \| pmid = 19115523 \| doi = 10.1097/med.0b013e32831cf5aa\| s2cid = 45482442 }}</ref> It also activates these receptors in the ]. Together with ], it is the second major source of ] signals that stop eating behaviour.<ref name="pmid11127929">{{cite journal \| vauthors = Yamada K, Wada E, Wada K \| title = Bombesin-like peptides: studies on food intake and social behaviour with receptor knock-out mice \| journal = Annals of Medicine \| volume = 32 \| issue = 8 \| pages = 519–29 \|date=November 2000 \| pmid = 11127929 \| doi = 10.3109/07853890008998831\| s2cid = 24431961 }}</ref>		</ref> by ] ''et al.'' and named after its source.<ref name="Jensen-et-al-2007">{{cite journal \| last1=Jensen \| first1=R. T. \| last2=Battey \| first2=J. F. \| last3=Spindel \| first3=E. R. \| last4=Benya \| first4=R. V. \| title=International Union of Pharmacology. LXVIII. Mammalian Bombesin Receptors: Nomenclature, Distribution, Pharmacology, Signaling, and Functions in Normal and Disease States \| journal=] \| publisher=] (ASPET) \| volume=60 \| issue=1 \| date=2007-11-30 \| issn=0031-6997 \| doi=10.1124/pr.107.07108 \| pages=1–42 \| pmc=2517428 \| pmid=18055507}} ] 45053.</ref> It has two known ] in ] called ] and ]. It stimulates ] release from ]. It activates three different ]-coupled ] known as BBR1, -2, and -3.<ref name="pmid19115523">{{cite journal \| author = Weber HC \| title = Regulation and signaling of human bombesin receptors and their biological effects \| journal = Current Opinion in Endocrinology, Diabetes and Obesity \| volume = 16 \| issue = 1 \| pages = 66–71 \|date=February 2009 \| pmid = 19115523 \| doi = 10.1097/med.0b013e32831cf5aa\| s2cid = 45482442 }}</ref> It also activates these receptors in the ]. Together with ], it is the second major source of ] signals that stop eating behaviour.<ref name="pmid11127929">{{cite journal \| vauthors = Yamada K, Wada E, Wada K \| title = Bombesin-like peptides: studies on food intake and social behaviour with receptor knock-out mice \| journal = Annals of Medicine \| volume = 32 \| issue = 8 \| pages = 519–29 \|date=November 2000 \| pmid = 11127929 \| doi = 10.3109/07853890008998831\| s2cid = 24431961 }}</ref>

	Bombesin is also a ] marker for small cell carcinoma of lung, gastric cancer, pancreatic cancer, and ].<ref name="pmid10636070">{{cite journal \| vauthors = Ohlsson B, Fredäng N, Axelson J \| title = The effect of bombesin, cholecystokinin, gastrin, and their antagonists on proliferation of pancreatic cancer cell lines \| journal = Scandinavian Journal of Gastroenterology \| volume = 34 \| issue = 12 \| pages = 1224–9 \|date=December 1999 \| pmid = 10636070 \| doi = 10.1080/003655299750024742}}</ref>		Bombesin is also a ] marker for small cell carcinoma of lung, gastric cancer, pancreatic cancer, and ].<ref name="pmid10636070">{{cite journal \| vauthors = Ohlsson B, Fredäng N, Axelson J \| title = The effect of bombesin, cholecystokinin, gastrin, and their antagonists on proliferation of pancreatic cancer cell lines \| journal = Scandinavian Journal of Gastroenterology \| volume = 34 \| issue = 12 \| pages = 1224–9 \|date=December 1999 \| pmid = 10636070 \| doi = 10.1080/003655299750024742}}</ref>

Revision as of 18:45, 27 August 2023

Bombesin
Names

Other names Pyr-Gln-Arg-Leu-Gly-Asn-Gln-Trp-Ala-Val-Gly-His-Leu-Met-NH2
Identifiers
CAS Number	31362-50-2
3D model (JSmol)	Interactive image
ChEMBL	ChEMBL437027
ChemSpider	17290379
IUPHAR/BPS	616
PubChem CID	16133800
UNII	PX9AZU7QPK
CompTox Dashboard (EPA)	DTXSID1037149
InChI InChI=1S/C71H110N24O18S/c1-34(2)24-47(92-62(105)43(14-11-22-79-71(76)77)89-64(107)45(15-18-52(72)96)90-63(106)44-17-20-55(99)85-44)61(104)81-31-56(100)87-51(28-54(74)98)69(112)91-46(16-19-53(73)97)65(108)94-49(26-38-29-80-41-13-10-9-12-40(38)41)66(109)84-37(7)60(103)95-58(36(5)6)70(113)82-32-57(101)86-50(27-39-30-78-33-83-39)68(111)93-48(25-35(3)4)67(110)88-42(59(75)102)21-23-114-8/h9-10,12-13,29-30,33-37,42-51,58,80H,11,14-28,31-32H2,1-8H3,(H2,72,96)(H2,73,97)(H2,74,98)(H2,75,102)(H,78,83)(H,81,104)(H,82,113)(H,84,109)(H,85,99)(H,86,101)(H,87,100)(H,88,110)(H,89,107)(H,90,106)(H,91,112)(H,92,105)(H,93,111)(H,94,108)(H,95,103)(H4,76,77,79)/t37-,42-,43-,44-,45-,46-,47-,48-,49-,50-,51-,58-/m0/s1Key: QXZBMSIDSOZZHK-DOPDSADYSA-N InChI=1/C71H110N24O18S/c1-34(2)24-47(92-62(105)43(14-11-22-79-71(76)77)89-64(107)45(15-18-52(72)96)90-63(106)44-17-20-55(99)85-44)61(104)81-31-56(100)87-51(28-54(74)98)69(112)91-46(16-19-53(73)97)65(108)94-49(26-38-29-80-41-13-10-9-12-40(38)41)66(109)84-37(7)60(103)95-58(36(5)6)70(113)82-32-57(101)86-50(27-39-30-78-33-83-39)68(111)93-48(25-35(3)4)67(110)88-42(59(75)102)21-23-114-8/h9-10,12-13,29-30,33-37,42-51,58,80H,11,14-28,31-32H2,1-8H3,(H2,72,96)(H2,73,97)(H2,74,98)(H2,75,102)(H,78,83)(H,81,104)(H,82,113)(H,84,109)(H,85,99)(H,86,101)(H,87,100)(H,88,110)(H,89,107)(H,90,106)(H,91,112)(H,92,105)(H,93,111)(H,94,108)(H,95,103)(H4,76,77,79)/t37-,42-,43-,44-,45-,46-,47-,48-,49-,50-,51-,58-/m0/s1Key: QXZBMSIDSOZZHK-DOPDSADYBX
SMILES /N=C(\N)/NCCC(C(=O)N(CC(C)C)C(=O)NCC(=O)N(CC(=O)N)C(=O)N(CCC(=O)N)C(=O)N(Cc1cc2c1cccc2)C(=O)N(C)C(=O)N(C(C)C)C(=O)NCC(=O)N(Cc3ccn3)C(=O)N(CC(C)C)C(=O)N(CCSC)C(=O)N)NC(=O)(CCC(=O)N)NC(=O)4CCC(=O)N4
Properties
Chemical formula	C₇₁H₁₁₀N₂₄O₁₈S
Molar mass	1619.85
Except where otherwise noted, data are given for materials in their standard state (at 25 °C , 100 kPa). N verify (what is ?) Infobox references

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.

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.

References

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.
- 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. 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.
- 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.
^ 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.
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.
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.
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.
- 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. doi:10.1111/j.1749-6632.1988.tb23870.x. ISSN 0077-8923.
- 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. 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.

Peptides: neuropeptides

Hormones

see hormones

Opioid peptides

Dynorphins	Dynorphin A Dynorphin A_1–8 Dynorphin B Big dynorphin Leumorphin α-Neoendorphin β-Neoendorphin
Endomorphins	Endomorphin-1 Endomorphin-2
Endorphins	α-Endorphin β-Endorphin γ-Endorphin
Enkephalins	Met-enkephalin Leu-enkephalin
Others	Adrenorphin Amidorphin Hemorphin Hemorphin-4 Nociceptin Opiorphin Spinorphin Valorphin

Other
neuropeptides

Kinins	Bradykinins Tachykinins: mammal Substance P Neurokinin A Neurokinin B amphibian Kassinin Physalaemin
Neuromedins	B N S U
Orexins	A B
Other	Angiotensin Bombesin Calcitonin gene-related peptide Carnosine Cocaine- and amphetamine-regulated transcript Delta-sleep-inducing peptide FMRFamide Galanin Galanin-like peptide Gastrin-releasing peptide Ghrelin Neuropeptide AF Neuropeptide FF Neuropeptide SF Neuropeptide VF Neuropeptide S Neuropeptide Y Neurophysins Neurotensin Pancreatic polypeptide Pituitary adenylate cyclase-activating peptide RVD-Hpα VGF

Categories:

Revision as of 19:11, 28 January 2023 editOAbot (talk \| contribs)Bots441,761 editsm Open access bot: doi added to citation with #oabot.← Previous edit		Revision as of 18:45, 27 August 2023 edit undoOnel5969 (talk \| contribs)Autopatrolled, Extended confirmed users, Page movers, New page reviewers, Pending changes reviewers, Rollbackers937,225 editsm Disambiguating links to Homology (link changed to Homologous series) using DisamAssist.Next edit →
Line 50:		Line 50:
	\|{{cite book \| editor-last=Daniel \| editor-first=Edwin E. \| title=Neuropeptide Function in the Gastrointestinal Tract \| publisher=CRC Press \| date=2019-08-15 \| isbn=978-0-429-28576-9 \| oclc=1112671803}}		\|{{cite book \| editor-last=Daniel \| editor-first=Edwin E. \| title=Neuropeptide Function in the Gastrointestinal Tract \| publisher=CRC Press \| date=2019-08-15 \| isbn=978-0-429-28576-9 \| oclc=1112671803}}
	}}		}}
	</ref> by ] ''et al.'' and named after its source.<ref name="Jensen-et-al-2007">{{cite journal \| last1=Jensen \| first1=R. T. \| last2=Battey \| first2=J. F. \| last3=Spindel \| first3=E. R. \| last4=Benya \| first4=R. V. \| title=International Union of Pharmacology. LXVIII. Mammalian Bombesin Receptors: Nomenclature, Distribution, Pharmacology, Signaling, and Functions in Normal and Disease States \| journal=] \| publisher=] (ASPET) \| volume=60 \| issue=1 \| date=2007-11-30 \| issn=0031-6997 \| doi=10.1124/pr.107.07108 \| pages=1–42 \| pmc=2517428 \| pmid=18055507}} ] 45053.</ref> It has two known ] in ] called ] and ]. It stimulates ] release from ]. It activates three different ]-coupled ] known as BBR1, -2, and -3.<ref name="pmid19115523">{{cite journal \| author = Weber HC \| title = Regulation and signaling of human bombesin receptors and their biological effects \| journal = Current Opinion in Endocrinology, Diabetes and Obesity \| volume = 16 \| issue = 1 \| pages = 66–71 \|date=February 2009 \| pmid = 19115523 \| doi = 10.1097/med.0b013e32831cf5aa\| s2cid = 45482442 }}</ref> It also activates these receptors in the ]. Together with ], it is the second major source of ] signals that stop eating behaviour.<ref name="pmid11127929">{{cite journal \| vauthors = Yamada K, Wada E, Wada K \| title = Bombesin-like peptides: studies on food intake and social behaviour with receptor knock-out mice \| journal = Annals of Medicine \| volume = 32 \| issue = 8 \| pages = 519–29 \|date=November 2000 \| pmid = 11127929 \| doi = 10.3109/07853890008998831\| s2cid = 24431961 }}</ref>		</ref> by ] ''et al.'' and named after its source.<ref name="Jensen-et-al-2007">{{cite journal \| last1=Jensen \| first1=R. T. \| last2=Battey \| first2=J. F. \| last3=Spindel \| first3=E. R. \| last4=Benya \| first4=R. V. \| title=International Union of Pharmacology. LXVIII. Mammalian Bombesin Receptors: Nomenclature, Distribution, Pharmacology, Signaling, and Functions in Normal and Disease States \| journal=] \| publisher=] (ASPET) \| volume=60 \| issue=1 \| date=2007-11-30 \| issn=0031-6997 \| doi=10.1124/pr.107.07108 \| pages=1–42 \| pmc=2517428 \| pmid=18055507}} ] 45053.</ref> It has two known ] in ] called ] and ]. It stimulates ] release from ]. It activates three different ]-coupled ] known as BBR1, -2, and -3.<ref name="pmid19115523">{{cite journal \| author = Weber HC \| title = Regulation and signaling of human bombesin receptors and their biological effects \| journal = Current Opinion in Endocrinology, Diabetes and Obesity \| volume = 16 \| issue = 1 \| pages = 66–71 \|date=February 2009 \| pmid = 19115523 \| doi = 10.1097/med.0b013e32831cf5aa\| s2cid = 45482442 }}</ref> It also activates these receptors in the ]. Together with ], it is the second major source of ] signals that stop eating behaviour.<ref name="pmid11127929">{{cite journal \| vauthors = Yamada K, Wada E, Wada K \| title = Bombesin-like peptides: studies on food intake and social behaviour with receptor knock-out mice \| journal = Annals of Medicine \| volume = 32 \| issue = 8 \| pages = 519–29 \|date=November 2000 \| pmid = 11127929 \| doi = 10.3109/07853890008998831\| s2cid = 24431961 }}</ref>

	Bombesin is also a ] marker for small cell carcinoma of lung, gastric cancer, pancreatic cancer, and ].<ref name="pmid10636070">{{cite journal \| vauthors = Ohlsson B, Fredäng N, Axelson J \| title = The effect of bombesin, cholecystokinin, gastrin, and their antagonists on proliferation of pancreatic cancer cell lines \| journal = Scandinavian Journal of Gastroenterology \| volume = 34 \| issue = 12 \| pages = 1224–9 \|date=December 1999 \| pmid = 10636070 \| doi = 10.1080/003655299750024742}}</ref>		Bombesin is also a ] marker for small cell carcinoma of lung, gastric cancer, pancreatic cancer, and ].<ref name="pmid10636070">{{cite journal \| vauthors = Ohlsson B, Fredäng N, Axelson J \| title = The effect of bombesin, cholecystokinin, gastrin, and their antagonists on proliferation of pancreatic cancer cell lines \| journal = Scandinavian Journal of Gastroenterology \| volume = 34 \| issue = 12 \| pages = 1224–9 \|date=December 1999 \| pmid = 10636070 \| doi = 10.1080/003655299750024742}}</ref>

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