Bombesin

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Bombesin
Bombesin skeletal.svg
Names
Other names
Pyr-Gln-Arg-Leu-Gly-Asn-Gln-Trp-Ala-Val-Gly-His-Leu-Met-NH2
Identifiers
3D model (JSmol)
ChEMBL
ChemSpider
PubChem CID
UNII
  • 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/s1 X mark.svgN
    Key: QXZBMSIDSOZZHK-DOPDSADYSA-N X mark.svgN
  • 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/s1
    Key: QXZBMSIDSOZZHK-DOPDSADYBX
  • [H]/N=C(\N)/NCCC[C@@H](C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CC(=O)N)C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](Cc1c[nH]c2c1cccc2)C(=O)N[C@@H](C)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](Cc3c[nH]cn3)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)N)NC(=O)[C@H](CCC(=O)N)NC(=O)[C@@H]4CCC(=O)N4
Properties
C71H110N24O18S
Molar mass 1619.85
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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Bombesin is a 14-amino acid peptide [1] originally isolated from the skin of the European fire-bellied toad (Bombina bombina) [2] by Vittorio Erspamer et al. and named after its source. [3] 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. [4] 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. [5]

Contents

Bombesin is also a tumor marker for small cell carcinoma of lung, gastric cancer, pancreatic cancer, and neuroblastoma. [6]

Receptors

The anuran BB4 receptor homologue is termed frog BB4 (fBB4). [3] 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. [3]

Effects

Erspamer 1988 finds bombesin has a similar effect on the chicken to ranatensin, unreliably increasing or decreasing blood pressure. [7]

See also

Related Research Articles

<span class="mw-page-title-main">Cholecystokinin</span> Hormone of the gastrointestinal system

Cholecystokinin is a peptide hormone of the gastrointestinal system responsible for stimulating the digestion of fat and protein. Cholecystokinin, formerly called pancreozymin, is synthesized and secreted by enteroendocrine cells in the duodenum, the first segment of the small intestine. Its presence causes the release of digestive enzymes and bile from the pancreas and gallbladder, respectively, and also acts as a hunger suppressant.

<span class="mw-page-title-main">Gastrin</span> Mammalian protein found in Homo sapiens

Gastrin is a peptide hormone that stimulates secretion of gastric acid (HCl) by the parietal cells of the stomach and aids in gastric motility. It is released by G cells in the pyloric antrum of the stomach, duodenum, and the pancreas.

<span class="mw-page-title-main">Gastrin-releasing peptide</span>

Gastrin-releasing peptide, also known as GRP, is a neuropeptide, a regulatory molecule that has been implicated in a number of physiological and pathophysiological processes. Most notably, GRP stimulates the release of gastrin from the G cells of the stomach.

Physalaemin is a tachykinin peptide obtained from the Physalaemus frog, closely related to substance P. Its structure was first elucidated in 1964.

<span class="mw-page-title-main">Kassinin</span> Chemical compound

Kassinin is a peptide derived from the Kassina frog. It belongs to tachykinin family of neuropeptides. It is secreted as a defense response, and is involved in neuropeptide signalling.

Signaling peptide receptor is a type of receptor which binds one or more signaling peptides or signaling proteins.

<span class="mw-page-title-main">Enteroendocrine cell</span>

Enteroendocrine cells are specialized cells of the gastrointestinal tract and pancreas with endocrine function. They produce gastrointestinal hormones or peptides in response to various stimuli and release them into the bloodstream for systemic effect, diffuse them as local messengers, or transmit them to the enteric nervous system to activate nervous responses. Enteroendocrine cells of the intestine are the most numerous endocrine cells of the body. They constitute an enteric endocrine system as a subset of the endocrine system just as the enteric nervous system is a subset of the nervous system. In a sense they are known to act as chemoreceptors, initiating digestive actions and detecting harmful substances and initiating protective responses. Enteroendocrine cells are located in the stomach, in the intestine and in the pancreas. Microbiota plays key roles in the intestinal immune and metabolic responses in these enteroendocrine cells via their fermentation product, acetate.

Neuromedin B (NMB) is a bombesin-related peptide in mammals. It was originally purified from pig spinal cord, and later shown to be present in human central nervous system and gastrointestinal tract.

<span class="mw-page-title-main">Bombesin-like receptor 3</span> Protein-coding gene in humans

The bombesin receptor subtype 3 also known as BRS-3 or BB3 is a protein which in humans is encoded by the BRS3 gene.

<span class="mw-page-title-main">Neuromedin B receptor</span> Protein-coding gene in the species Homo sapiens

The neuromedin B receptor (NMBR), now known as BB1 is a G protein-coupled receptor whose endogenous ligand is neuromedin B. In humans, this protein is encoded by the NMBR gene.

<span class="mw-page-title-main">Gastrin-releasing peptide receptor</span> Protein-coding gene in the species Homo sapiens

The gastrin-releasing peptide receptor (GRPR), now properly known as BB2 is a G protein-coupled receptor whose endogenous ligand is gastrin releasing peptide. In humans it is highly expressed in the pancreas and is also expressed in the stomach, adrenal cortex and brain.

The neuromedin U receptors are two G-protein coupled receptors which bind the neuropeptide hormones neuromedin U and neuromedin S. There are two subtypes of the neuromedin U receptor, each encoded by a separate gene.

<span class="mw-page-title-main">Cholecystokinin B receptor</span> Protein-coding gene in the species Homo sapiens

The cholecystokinin B receptor also known as CCKBR or CCK2 is a protein that in humans is encoded by the CCKBR gene.

<span class="mw-page-title-main">Cholecystokinin A receptor</span> Protein-coding gene in the species Homo sapiens

The Cholecystokinin A receptor is a human protein, also known as CCKAR or CCK1, with CCK1 now being the IUPHAR-recommended name.

Neuromedin S is a 36-amino acid neuropeptide found in the brain of humans and other mammals. It is produced in the suprachiasmatic nucleus of the hypothalamus and is related to neuromedin U. It is thought to be involved in regulation of circadian rhythm and also has appetite suppressant effects, as well as regulating the release of several other peptide hormones including vasopressin, luteinizing hormone, and oxytocin.

Bombesin-like peptides comprise a large family of peptides which were initially isolated from amphibian skin, where they stimulate smooth muscle contraction. They were later found to be widely distributed in mammalian neural and endocrine cells.

<span class="mw-page-title-main">Vittorio Erspamer</span>

Vittorio Erspamer was an Italian pharmacologist and chemist, known for the identification, synthesis and pharmacological studies of more than sixty new chemical compounds, most notably serotonin and octopamine.


B))

Deltorphin, also known as deltorphin A and dermenkephalin, is a naturally occurring, exogenous opioid heptapeptide and thus, exorphin, with the amino acid sequence Tyr-D-Met-Phe-His-Leu-Met-Asp-NH2. Along with the other deltorphins (such as deltorphin I and deltorphin II) and the dermorphins, deltorphin is endogenous to frogs of the genus Phyllomedusa such as P. bicolor and P. sauvagei where it is produced in their skin, and is not known to occur naturally in any other species. Deltorphin is one of the highest affinity and most selective naturally occurring opioid peptides known, acting as a very potent and highly specific agonist of the δ-opioid receptor.

Pro-Gastrin-Releasing-Peptide, also known as Pro-GRP, is a Gastrin-Releasing-Peptide (GRP) precursor, a neurotransmitter that belongs to the bombesine/neuromedin B family. GRP stimulates the secretion of gastrin in order to increase the acidity of the gastric acid. Pro-GRP is a peptide composed of 125 amino acids, expressed in the nervous system and digestive tract. It is also important to not confused with progastrin, consisting of 80 amino acids, precursor of gastrin in its intracellular version and oncogene in its extracellular version (hPG80).

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.
  2. ↑
  3. 1 2 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 . American Society for Pharmacology & Experimental Therapeutics (ASPET). 60 (1): 1–42. doi:10.1124/pr.107.07108. ISSN   0031-6997. PMC   2517428 . PMID   18055507. NIHMSID 45053.
  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.
  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.
  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.
  7. ↑
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